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Conserved domains on  [gi|2289190121|gb|UVI59173|]
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ankyrin-1 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-230 9.19e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 9.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  10 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 89
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  90 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG-- 167
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGad 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 168 --TKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGA 230
Cdd:COG0666   212 vnAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-230 9.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 9.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  10 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 89
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  90 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG-- 167
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGad 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 168 --TKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGA 230
Cdd:COG0666   212 vnAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 32-234 3.64e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.66  E-value: 3.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  32 LRNGVDINTCNQNGLNGLHLASKEGHV-KMVVE----LLHKEIILETTTKKGNTALHIAALA--GQDEVVRELVNYGANV 104
Cdd:PHA03100   55 LDNGADINSSTKNNSTPLHYLSNIKYNlTDVKEivklLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 105 NAQSQKGFTPLYMAAQENH--LEVVKFLLENGANQNVAT----------------EDGFTPLAVALQQGHENVVAHLINY 166
Cdd:PHA03100  135 NIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNrvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDL 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289190121 167 GTkgkvrlpalhiaarnddtrtaavllqndpNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNF 234
Cdd:PHA03100  215 GA-----------------------------NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-139 6.49e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 6.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  49 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 128
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2289190121 129 FLLENGANQNV 139
Cdd:pfam12796  79 LLLEKGADINV 89
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 77-228 1.24e-14

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 72.48  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  77 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 142
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 143 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 213
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274

                         170
                  ....*....|....*
gi 2289190121 214 AHYENLNVAQLLLNR 228
Cdd:cd22194   275 AKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 106-233 1.34e-09

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.78  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 106 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 182
Cdd:TIGR00870  15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 183 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:TIGR00870  92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVP 155
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 110-139 7.81e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 7.81e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2289190121  110 KGFTPLYMAAQENHLEVVKFLLENGANQNV 139
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-230 9.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 9.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  10 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 89
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  90 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG-- 167
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGad 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 168 --TKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGA 230
Cdd:COG0666   212 vnAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-233 5.84e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 5.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  10 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 89
Cdd:COG0666    19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  90 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG-- 167
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGad 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289190121 168 --TKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:COG0666   179 vnARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-195 1.13e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121   8 READAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAAL 87
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  88 AGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG 167
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2289190121 168 ----TKGKVRLPALHIAARNDDTRTAAVLLQN 195
Cdd:COG0666   243 adlnAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-233 1.58e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 1.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  25 LDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANV 104
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 105 NAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG----TKGKVRLPALHIA 180
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGadvnAQDNDGNTPLHLA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2289190121 181 ARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-181 9.74e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 9.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121   8 READAATSFLRAARSGNLD--KALdhLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIA 85
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEivKLL--LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  86 ALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLIN 165
Cdd:COG0666   194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                         170
                  ....*....|....*.
gi 2289190121 166 YGTKGKVRLPALHIAA 181
Cdd:COG0666   274 ALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 32-234 3.64e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.66  E-value: 3.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  32 LRNGVDINTCNQNGLNGLHLASKEGHV-KMVVE----LLHKEIILETTTKKGNTALHIAALA--GQDEVVRELVNYGANV 104
Cdd:PHA03100   55 LDNGADINSSTKNNSTPLHYLSNIKYNlTDVKEivklLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 105 NAQSQKGFTPLYMAAQENH--LEVVKFLLENGANQNVAT----------------EDGFTPLAVALQQGHENVVAHLINY 166
Cdd:PHA03100  135 NIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNrvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDL 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289190121 167 GTkgkvrlpalhiaarnddtrtaavllqndpNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNF 234
Cdd:PHA03100  215 GA-----------------------------NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 49-233 2.12e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 94.35  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  49 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EVVRELVNYGANVNAQSQKGFTPLYMAAQE-- 121
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 122 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHE--NVVAHLINYGT----KGKVRLpalhiaarnddtrtaavLLQN 195
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaKNRVNY-----------------LLSY 181

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2289190121 196 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-139 6.49e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 6.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  49 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 128
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2289190121 129 FLLENGANQNV 139
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-169 1.73e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  82 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENgANQNVaTEDGFTPLAVALQQGHENVVA 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 2289190121 162 HLINYGTK 169
Cdd:pfam12796  79 LLLEKGAD 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-233 6.70e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.63  E-value: 6.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  11 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMV--------------VELLHKEII------ 70
Cdd:PHA02874   34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIkllidngvdtsilpIPCIEKDMIktildc 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  71 ---LETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTP 147
Cdd:PHA02874  114 gidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 148 LAVALQQGHENVVAHLINYGT----KGKVRLPALHIAARNDdtRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYE-NLNVA 222
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNhimnKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDIDGSTPLHHAINPPcDIDII 271

                         250
                  ....*....|.
gi 2289190121 223 QLLLNRGASVN 233
Cdd:PHA02874  272 DILLYHKADIS 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-107 2.83e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  16 FLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMvVELLHKEIILETTTkKGNTALHIAALAGQDEVVR 95
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI-VKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 2289190121  96 ELVNYGANVNAQ 107
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-235 5.09e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 5.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 115 LYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINygtkgkvrlpalHIAARNDDTrtaavllq 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE------------HADVNLKDN-------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2289190121 195 ndpnpdvlsktGFTPLHIAAHYENLNVAQLLLNRGASVNFT 235
Cdd:pfam12796  61 -----------GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 19-233 5.51e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.18  E-value: 5.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  19 AARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 98
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  99 NYGANVN-AQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVR---- 173
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEdccg 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2289190121 174 LPALHIAARNDDTRTAAVLLQNDPNPDVLSKTG-FTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 77-228 1.24e-14

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 72.48  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  77 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 142
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 143 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 213
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274

                         170
                  ....*....|....*
gi 2289190121 214 AHYENLNVAQLLLNR 228
Cdd:cd22194   275 AKMGKAEILKYILSR 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-233 3.06e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  32 LRNGVDINTCNQNGLNGLHLAskeghvkmvveLLHKEIIletttkkgntalhiaalagqdEVVRELVNYGANVNAQSQKG 111
Cdd:PHA03095   70 LEAGADVNAPERCGFTPLHLY-----------LYNATTL---------------------DVIKLLIKAGADVNAKDKVG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 112 FTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAHLINYG----TKGKVRLPALHIAARN 183
Cdd:PHA03095  118 RTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGadvyAVDDRFRSLLHHHLQS 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 184 DDTRTAAV--LLQNDPNPDVLSKTGFTPLHIAAHY---ENLNVAQLLLNrGASVN 233
Cdd:PHA03095  198 FKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLLIA-GISIN 251
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-232 5.38e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  92 EVVRELVNYGANVNAQSQKGFTPL--YMA-AQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGH-ENVVAHLINYG 167
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhlYLHySSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2289190121 168 T----KGKVRLPALHIAARND--DTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVA--QLLLNRGASV 232
Cdd:PHA03095  108 AdvnaKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADV 180
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 5-153 8.37e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 8.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121   5 VGFREADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHI 84
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2289190121  85 AALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVkfLLENGANQNVATEDGFTPLAVALQ 153
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 74-226 1.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  74 TTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQ 153
Cdd:PHA02878  164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 154 QGHE-NVVAHLINYGT----KGKVR-LPALHIAARndDTRTAAVLLQNDPNPDVLSKTGFTPLHIAA-HYENLNVAQLLL 226
Cdd:PHA02878  244 YCKDyDILKLLLEHGVdvnaKSYILgLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILI 321
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 13-167 5.64e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 5.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  13 ATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDE 92
Cdd:PLN03192  526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121  93 VVRELVNYGANVNAQSqkGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG 167
Cdd:PLN03192  606 IFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-169 1.14e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  24 NLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIaALAGQDEV--VRELVNYG 101
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYmsVKTLIDRG 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2289190121 102 ANVNAQSQKGFTPLYMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALqqGHENVVAHLINYGTK 169
Cdd:PHA02876  433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 16-233 2.02e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  16 FLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLhKEII---LETTTKKGNTALHIAALagqdE 92
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-RSINkcsVFYTLVAIKDAFNNRNV----E 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  93 VVRE-LVNYGANVNAQSQKGF-TPLYMAAQENhlEVVKFLLENGANQNVATED-GFTPLAVALQQGHENVVAHLINYGtk 169
Cdd:PHA02878  116 IFKIiLTNRYKNIQTIDLVYIdKKSKDDIIEA--EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYG-- 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2289190121 170 GKVRLP------ALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHY-ENLNVAQLLLNRGASVN 233
Cdd:PHA02878  192 ANVNIPdktnnsPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVN 262
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 17-228 3.13e-11

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  17 LRAARSGNLDkALDHLRNGVDINTCnQNGLNG---LHLASKEGHVKMVVELLH--KEIILETTTK---KGNTALHIAALA 88
Cdd:cd22192    22 LLAAKENDVQ-AIKKLLKCPSCDLF-QRGALGetaLHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  89 GQDEVVRELVNYGANVNAQSQKG--FT------------PLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQ 154
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQ 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 155 GHENVVAHLINygtkgkvrlpalhiaarnddtrtaaVLLQNDPNPD------VLSKTGFTPLHIAAHYENLNVAQLLLNR 228
Cdd:cd22192   180 PNKTFACQMYD-------------------------LILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 113-232 4.22e-11

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.95  E-value: 4.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 113 TPLYMAAQENHLEVVKFLLENganqnvatedgftplavalqqghenvvaHLINYGTKGKVRLPALHIAARNDDTRTAAVL 192
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC----------------------------PSCDLFQRGALGETALHVAALYDNLEAAVVL 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2289190121 193 LQNDP---NPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASV 232
Cdd:cd22192    71 MEAAPelvNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADV 115
Ank_4 pfam13637
Ankyrin repeats (many copies);
78-131 4.28e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 4.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2289190121  78 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 131
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 113-233 1.73e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 113 TPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGH-----ENVVAHLINYGT----KGKVRLPALHIAARN 183
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGAnvnaPDNNGITPLLYAISK 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2289190121 184 DDTRTAAV--LLQNDPNPDVLSKTGFTPLHIAAHY--ENLNVAQLLLNRGASVN 233
Cdd:PHA03100  117 KSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGVDIN 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 85-232 8.62e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 8.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  85 AALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV----- 159
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrily 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2289190121 160 -VAHLINYGTKGKVrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASV 232
Cdd:PLN03192  612 hFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 11-141 1.31e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  11 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQ 90
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2289190121  91 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVAT 141
Cdd:PHA02875  181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 106-233 1.34e-09

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.78  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 106 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 182
Cdd:TIGR00870  15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 183 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:TIGR00870  92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVP 155
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 32-232 1.38e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  32 LRNGVDINTCNQNGLNGLHLASKEGH-VKMVVELLHKEIILETTTKKGNTALHIAA-LAGQDEVVRELVNYGANVNAQSQ 109
Cdd:PHA02876  294 LERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDY 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 110 KGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV-VAHLINYG----TKGKVRLPALHIAARND 184
Cdd:PHA02876  374 CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGanvnSKNKDLSTPLHYACKKN 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2289190121 185 -DTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYEnlNVAQLLLNRGASV 232
Cdd:PHA02876  454 cKLDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-232 1.40e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  32 LRNGVDINTCNQNGLNGLH--LASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD--EVVRELVNYGANVNAQ 107
Cdd:PHA03095  139 LRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 108 SQKGFTPLYMAAQENHLE--VVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPA----LHIAA 181
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDgntpLSLMV 298

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2289190121 182 RNDDTRTAAVLLQNDPNPDVLSKTgftpLHIAAHYENLN--------VAQLLLNRGASV 232
Cdd:PHA03095  299 RNNNGRAVRAALAKNPSAETVAAT----LNTASVAGGDIpsdatrlcVAKVVLRGAFSL 353
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 90-233 1.57e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  90 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 166
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289190121 167 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVN 233
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVN 301
PHA02946 PHA02946
ankyin-like protein; Provisional
 59-226 2.28e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.60  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  59 KMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYM--AAQENHLEVVKFLLENGAN 136
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 137 -QNVATEDGFTPLaVALQQGHENVVAHLINYGTKGKV------RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTP 209
Cdd:PHA02946  133 iNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIvdkfgkNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211

                         170
                  ....*....|....*....
gi 2289190121 210 LHI--AAHYENLNVAQLLL 226
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLL 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 32-167 2.51e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  32 LRNGVDINTCNQNGLN-GLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQK 110
Cdd:PHA02878  154 LSYGADINMKDRHKGNtALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC 233

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2289190121 111 GFTPLYMAAQE-NHLEVVKFLLENGANQNV-ATEDGFTPLAVALQQghENVVAHLINYG 167
Cdd:PHA02878  234 GNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYG 290
PHA02798 PHA02798
ankyrin-like protein; Provisional
 92-233 1.07e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.84  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  92 EVVRELVNYGANVNAQSQKGFTPL-----YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLIny 166
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILL-- 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 167 gtkgkvrlpalhiaarnddtrtaaVLLQNDPNPDVLSKTGFTPLHI---AAHYENLNVAQLLLNRGASVN 233
Cdd:PHA02798  130 ------------------------FMIENGADTTLLDKDGFTMLQVylqSNHHIDIEIIKLLLEKGVDIN 175
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 67-236 1.76e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 54.12  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  67 KEIILETTTK---KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF-------------TPLYMAAQENHLEVVKFL 130
Cdd:cd21882    59 KELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 131 LENGANqnvatedgftPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPL 210
Cdd:cd21882   139 LENGAQ----------PAALEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPL 208

                         170       180
                  ....*....|....*....|....*.
gi 2289190121 211 HIAAHYENLNVAQLLLNRGASVNFTP 236
Cdd:cd21882   209 KLAAVEGKIVMFQHILQREFSGPYQP 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 83-166 2.67e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  83 HIAAlAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAH 162
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 2289190121 163 LINY 166
Cdd:PTZ00322  167 LSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-164 3.07e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 3.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2289190121 113 TPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI 164
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 25-228 4.05e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 53.27  E-value: 4.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  25 LDKALDHLRNGVdintcNQNGLNGLHLASKEGHVKMVVELLHKEiiletTTKKGNTALHIAALAGQDEVVRELVNYGANV 104
Cdd:cd22196    51 LLKAMLNLHNGQ-----NDTISLLLDIAEKTGNLKEFVNAAYTD-----SYYKGQTALHIAIERRNMHLVELLVQNGADV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 105 NA----------QSQKGF----TPLYMAAQENHLEVVKFLLENGANQ-NVATEDGFTplavalqqgheNVVAHlinygtk 169
Cdd:cd22196   121 HArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENPHSPaDISARDSMG-----------NTVLH------- 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2289190121 170 gkvrlpALHIAARNDDTRTAAV--------LLQNDPNP-----DVLSKTGFTPLHIAAHYENLNVAQLLLNR 228
Cdd:cd22196   183 ------ALVEVADNTPENTKFVtkmyneilILGAKIRPllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
173-226 4.94e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 4.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2289190121 173 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLL 226
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 116-233 5.03e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 116 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHEN---VVAHLINYG----TKGKVRLPALHIAARNDDT-R 187
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGadvnAPERCGFTPLHLYLYNATTlD 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2289190121 188 TAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN--VAQLLLNRGASVN 233
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVN 146
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 16-228 7.45e-08

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 7.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  16 FLRAARSGNLDKALDHLRNG--VDINTCNQNGLNGLHLASKEGHVKMVVELLHKeiiLETTTKKGNTALHIAALAGQDeV 93
Cdd:TIGR00870  21 FLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-A 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  94 VRELVNYGAN----------VNAQS----QKGFTPLYMAAQENHLEVVKFLLENGANQNVA------------------- 140
Cdd:TIGR00870  97 VEAILLHLLAafrksgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvdsfyhge 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 141 ------------------TEDGFTPLAvALQQGheNVVAHLINYGTKGKVRLPALHIA---------ARNDDTRTAAVLL 193
Cdd:TIGR00870 177 splnaaaclgspsivallSEDPADILT-ADSLG--NTLLHLLVMENEFKAEYEELSCQmynfalsllDKLRDSKELEVIL 253

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2289190121 194 QNDpnpdvlsktGFTPLHIAAHYENLNVAQLLLNR 228
Cdd:TIGR00870 254 NHQ---------GLTPLKLAAKEGRIVLFRLKLAI 279
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 77-228 3.43e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 50.56  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  77 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENganqnvate 142
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 143 dGFTPLAVALQQGHENVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPN--PDV-----LSKTGFTP 209
Cdd:cd22193   146 -EHQPADIEAQDSRGNTVLH-------------ALVTVADNTKENTKFVtrmydmILIRGAKlcPTVeleeiRNNDGLTP 211

                         170
                  ....*....|....*....
gi 2289190121 210 LHIAAHYENLNVAQLLLNR 228
Cdd:cd22193   212 LQLAAKMGKIEILKYILQR 230
Ank_5 pfam13857
Ankyrin repeats (many copies);
97-151 5.30e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 5.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121  97 LVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVA 151
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-131 6.27e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 6.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2289190121  78 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 131
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-235 7.46e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  25 LDKALDH-LRNGVDINTCNQNGLNglhlASKEgHVKMVVELLHKE--IILETTTKKG----------NTALHIAALAGQD 91
Cdd:PHA02876  117 LDEACIHiLKEAISGNDIHYDKIN----ESIE-YMKLIKERIQQDelLIAEMLLEGGadvnakdiycITPIHYAAERGNA 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  92 EVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQN---------VATEDGFTPLAVALQQGHENVVAH 162
Cdd:PHA02876  192 KMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINkndlsllkaIRNEDLETSLLLYDAGFSVNSIDD 271

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 163 LINYGTKGKVRLPALhiaarnddTRTAAVLLQNDPNPDVLSKTGFTPLHIAAH--YENLNVaQLLLNRGASVNFT 235
Cdd:PHA02876  272 CKNTPLHHASQAPSL--------SRLVPKLLERGADVNAKNIKGETPLYLMAKngYDTENI-RTLIMLGADVNAA 337
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 110-139 7.81e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 7.81e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2289190121  110 KGFTPLYMAAQENHLEVVKFLLENGANQNV 139
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02795 PHA02795
ankyrin-like protein; Provisional
 92-155 1.39e-05

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 45.37  E-value: 1.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2289190121  92 EVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQG 155
Cdd:PHA02795  202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
Ank_4 pfam13637
Ankyrin repeats (many copies);
49-98 2.19e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 2.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2289190121  49 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 98
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 77-106 2.62e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 2.62e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2289190121   77 KGNTALHIAALAGQDEVVRELVNYGANVNA 106
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 168-232 3.08e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.49  E-value: 3.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2289190121 168 TKGKVRLPALHIAARNDDTR---TAAVLLQNDPNPDVLSK-----------TGFTPLHIAAHYENLNVAQLLLNRGASV 232
Cdd:cd21882    21 QRGATGKTCLHKAALNLNDGvneAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADV 99
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-107 3.27e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 3.27e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2289190121  77 KGNTALHIAAL-AGQDEVVRELVNYGANVNAQ 107
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 91-153 6.61e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.05  E-value: 6.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2289190121  91 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQ 153
Cdd:PHA02884   83 DDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 206-233 7.36e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 7.36e-05
                           10        20
                   ....*....|....*....|....*...
gi 2289190121  206 GFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
64-118 7.48e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 7.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121  64 LLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMA 118
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-106 8.72e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 8.72e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2289190121  77 KGNTALHIAALAGQDEVVRELVNYGANVNA 106
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 88-233 1.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  88 AGQDEVVRELV-NYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINY 166
Cdd:PHA02874   11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 167 GTKGKVrLPA----------------------------LHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYEN 218
Cdd:PHA02874   91 GVDTSI-LPIpciekdmiktildcgidvnikdaelktfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169

                         170
                  ....*....|....*
gi 2289190121 219 LNVAQLLLNRGASVN 233
Cdd:PHA02874  170 FDIIKLLLEKGAYAN 184
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-142 1.55e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 1.55e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2289190121 110 KGFTPLYMAA-QENHLEVVKFLLENGANQNVATE 142
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 92-233 1.92e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.21  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  92 EVVRELVNYGANVNAQSQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGhENVVAHLINY--- 166
Cdd:PHA02716  193 DILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI-DNINPEITNIyie 271

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 167 ---GTKGKVRLPALHI---AARNDDTRTAAVLLQNDPNPDVLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVN 233
Cdd:PHA02716  272 sldGNKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLN 346
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-233 2.55e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 2.55e-04
                          10        20
                  ....*....|....*....|....*....
gi 2289190121 206 GFTPLHIAA-HYENLNVAQLLLNRGASVN 233
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-233 4.87e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 4.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2289190121 192 LLQNDP-NPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN 43
Ank_4 pfam13637
Ankyrin repeats (many copies);
14-65 5.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 5.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2289190121  14 TSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELL 65
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-139 7.98e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 7.98e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2289190121 110 KGFTPLYMAAQENHLEVVKFLLENGANQNV 139
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-233 8.06e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 8.06e-04
                          10        20
                  ....*....|....*....|....*...
gi 2289190121 206 GFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
 32-166 1.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  32 LRNGVDINT-CNQNGLNGLHLASKEGHVKMVVELLhKEII--------LETTTKKGNTALHIAALAGQDEVVRELVNY-- 100
Cdd:PHA02798  168 LEKGVDINThNNKEKYDTLHCYFKYNIDRIDADIL-KLFVdngfiinkENKSHKKKFMEYLNSLLYDNKRFKKNILDFif 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2289190121 101 -GANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINY 166
Cdd:PHA02798  247 sYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 32-115 1.14e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  32 LRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNY-------GANV 104
Cdd:PTZ00322  102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGANA 181

                          90
                  ....*....|.
gi 2289190121 105 NAQSQKGFTPL 115
Cdd:PTZ00322  182 KPDSFTGKPPS 192
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 38-172 1.15e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  38 INTCNQN--GLNGLHLASKEGHVkmvVELL-HKEIILETT-------TKKGNTALHIAALAGQ---DEVVRELVNYGANV 104
Cdd:PHA02736    8 IFASEPDieGENILHYLCRNGGV---TDLLaFKNAISDENrylvleyNRHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 105 NAQSQK-GFTPLYMAAQENHLEVVKFLLEN-GANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKV 172
Cdd:PHA02736   85 NGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 92-167 1.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  92 EVVRELVNYGANVNAQSQ-KGFTPL--YMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALQQGHEN--VVAHLIN 165
Cdd:PHA02859   67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRinVIKLLID 146


                  ..
gi 2289190121 166 YG 167
Cdd:PHA02859  147 SG 148
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 73-228 1.64e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.07  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  73 TTTKKGNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGANQN 138
Cdd:cd22197    42 TEGSTGKTCLMKAVLNLQDgvnacimpllEIDKDSGNPKPLVNAQCTdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 139 VATEDGF-------------TPLAVALQQGHENVVAHLIN----------YGTKGKVRLPALHIAARNDDTRTAAV---- 191
Cdd:cd22197   122 ARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLEnphqpaslqaQDSLGNTVLHALVMIADNSPENSALVikmy 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2289190121 192 --LLQN----DPN---PDVLSKTGFTPLHIAAHYENLNVAQLLLNR 228
Cdd:cd22197   202 dgLLQAgarlCPTvqlEEISNHEGLTPLKLAAKEGKIEIFRHILQR 247
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 77-134 2.58e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 38.68  E-value: 2.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2289190121  77 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENG 134
Cdd:cd22195   136 RGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFfqpkdeggyfyfgeLPLSLAACTNQPDIVHYLTENA 207
Ank_5 pfam13857
Ankyrin repeats (many copies);
36-85 3.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 3.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2289190121  36 VDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIA 85
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-235 3.73e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.96  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121 117 MAAQENHLEVVKfLLEN---GANQNVATEDGFTPlavalqqghenVVAHLINygtkgkVRLpaLHIAArNDDTRTAAVLL 193
Cdd:PTZ00322   44 IARIDTHLEALE-ATENkdaTPDHNLTTEEVIDP-----------VVAHMLT------VEL--CQLAA-SGDAVGARILL 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2289190121 194 QNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFT 235
Cdd:PTZ00322  103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 92-233 4.13e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 37.80  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  92 EVVRELVNYGANVNA-QSQKGFTPLYMAAQENHL--EVVKFLLENGANQNVATE-DGFTPLAVALQQGHENVVAHLINYG 167
Cdd:PHA02989  125 DMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDIDVISIKVIKYL 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2289190121 168 TKGKVRLP---ALHIAARNDDTRTAAVLLQND----------PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:PHA02989  205 IKKGVNIEtnnNGSESVLESFLDNNKILSKKEfkvlnfilkyIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIY 283
PHA02946 PHA02946
ankyin-like protein; Provisional
 86-204 5.14e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.73  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  86 ALAGQDE-VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAH 162
Cdd:PHA02946   46 GIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINL 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2289190121 163 LINYGTKgkvrlpalhIAARNDDTRTAAVLLQNDPNPDVLSK 204
Cdd:PHA02946  126 LVQYGAK---------INNSVDEEGCGPLLACTDPSERVFKK 158
PHA02741 PHA02741
hypothetical protein; Provisional
 42-159 5.63e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 36.56  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  42 NQNGLNGLHLASKEGHVKMVVELL------HKEIILETTTKKGNTALHIAALAGQD----EVVRELVNYGANVNAQ-SQK 110
Cdd:PHA02741   18 NSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2289190121 111 GFTPLYMAAQENHLEVVKFLL-ENGANQNVATEDGFTPLAVAlqQGHENV 159
Cdd:PHA02741   98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELA--IDNEDV 145
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 104-164 5.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 37.41  E-value: 5.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2289190121 104 VNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI 164
Cdd:PHA02989  249 INKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
PHA02798 PHA02798
ankyrin-like protein; Provisional
 25-233 8.29e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.12  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  25 LDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKmvvellHKEIIL-------ETT--TKKGNTALHIAALAG---QDE 92
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYIN------NLEILLfmiengaDTTllDKDGFTMLQVYLQSNhhiDIE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289190121  93 VVRELVNYGANVNAQSQK-GFTPLYMAAQEN----HLEVVKFLLENG---ANQNVATEDGFTPLAVALQQGHENVVAHL- 163
Cdd:PHA02798  163 IIKLLLEKGVDINTHNNKeKYDTLHCYFKYNidriDADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRFKKNIl 242

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2289190121 164 ------INYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVN 233
Cdd:PHA02798  243 dfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
PHA02917 PHA02917
ankyrin-like protein; Provisional
 100-154 9.52e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 36.90  E-value: 9.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2289190121 100 YGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQ 154
Cdd:PHA02917  441 YLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINE 495
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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