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Conserved domains on  [gi|169403957|ref|NP_079209|]
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ankyrin repeat domain-containing protein 53 isoform b [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];
100-299 1.21e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 100 AIDQTAIGSYYQLFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPL 178
Cdd:COG0666   79 DINAKDDGGNTLLHAAARnGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 179 HLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 258
Cdd:COG0666  158 HLAAANGNLEI----VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169403957 259 CARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIE 299
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-299 1.21e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 100 AIDQTAIGSYYQLFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPL 178
Cdd:COG0666   79 DINAKDDGGNTLLHAAARnGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 179 HLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 258
Cdd:COG0666  158 HLAAANGNLEI----VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169403957 259 CARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIE 299
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-274 3.28e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957  178 LHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSgANVHAQDaMGYKPIDFCKIWNHR 257
Cdd:pfam12796   1 LHLAAKNGN----LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 169403957  258 ACARFLKDAMWKKDKKD 274
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 137-258 4.96e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 4.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 137 DDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLH 216
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFE-YGADVNIEDDNGCYPIHIAIKHNFFDI----IKLLLEKGAYANVKDNNGESPLH 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 169403957 217 LAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 258
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSA 237
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 140-244 1.74e-07

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: 52.71  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 140 GFTAIHFAAQWGKLACLQVLVEEykfpVDLLTNN--------SQTPLHLVIHRDNTTValpcIYYLLEKGAD-LNAQTCN 210
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEA----APELVNEpmtsdlyqGETALHIAVVNQNLNL----VRELIARGADvVSPRATG 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 169403957 211 -------------GSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMG 244
Cdd:cd22192  123 tffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 175-244 9.84e-07

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: 50.46  E-value: 9.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957  175 QTPLHLVIHRDNttvaLPCIYYLLEKGADLNAqTCNGS---------------TPLHLAARDGLLDCVKVLVQSGANVHA 239
Cdd:TIGR00870 129 ITALHLAAHRQN----YEIVKLLLERGASVPA-RACGDffvksqgvdsfyhgeSPLNAAACLGSPSIVALLSEDPADILT 203


                  ....*
gi 169403957  240 QDAMG 244
Cdd:TIGR00870 204 ADSLG 208
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 210-239 1.05e-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: 44.50  E-value: 1.05e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 169403957   210 NGSTPLHLAARDGLLDCVKVLVQSGANVHA 239
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-299 1.21e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 100 AIDQTAIGSYYQLFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPL 178
Cdd:COG0666   79 DINAKDDGGNTLLHAAARnGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 179 HLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 258
Cdd:COG0666  158 HLAAANGNLEI----VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169403957 259 CARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIE 299
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-266 2.46e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.89  E-value: 2.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 112 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 191
Cdd:COG0666   59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVK 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169403957 192 pciyYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDA 266
Cdd:COG0666  138 ----LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-280 2.54e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 2.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 112 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTVAL 191
Cdd:COG0666  125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIVK 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 192 pciyYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDAMWKKD 271
Cdd:COG0666  204 ----LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279


                 ....*....
gi 169403957 272 KKDFAREMT 280
Cdd:COG0666  280 AALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-274 3.28e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957  178 LHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSgANVHAQDaMGYKPIDFCKIWNHR 257
Cdd:pfam12796   1 LHLAAKNGN----LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 169403957  258 ACARFLKDAMWKKDKKD 274
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
137-266 2.04e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 137 DDKGFTAIHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVAlpcIYYLLEKGADLNAQTCNGSTPLH 216
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLV---ALLLLAAGADINAKDDGGNTLLH 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 169403957 217 LAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDA 266
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
113-241 1.26e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957  113 FAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEEykfpvdlltnnsqtplhlvihrdnttvalp 192
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH------------------------------ 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 169403957  193 ciyyllekgADLNAQtCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQD 241
Cdd:pfam12796  53 ---------ADVNLK-DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 137-258 4.96e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 4.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 137 DDKGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLH 216
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFE-YGADVNIEDDNGCYPIHIAIKHNFFDI----IKLLLEKGAYANVKDNNGESPLH 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 169403957 217 LAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRA 258
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSA 237
PHA03095 PHA03095
ankyrin-like protein; Provisional
 176-251 3.78e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 3.78e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169403957 176 TPLHLVIHRDNTTVAlPCIYYLLEKGADLNAQTCNGSTPLHLAARDG-LLDCVKVLVQSGANVHAQDAMGYKPIDFC 251
Cdd:PHA03095  49 TPLHLYLHYSSEKVK-DIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLHVY 124
PHA03095 PHA03095
ankyrin-like protein; Provisional
 167-285 5.41e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 167 VDLLTNNSQTPLHLVIHRDNTtvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARdGL---LDCVKVLVQSGANVHAQDAM 243
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATT---LDVIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLY 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 169403957 244 GYKPIDfCKIWNHRACARFLKdAMWKKDKKDFAREMTKMKMF 285
Cdd:PHA03095 152 GMTPLA-VLLKSRNANVELLR-LLIDAGADVYAVDDRFRSLL 191
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 158-248 2.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 158 VLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVALPciyYLLEKGADLNAQTCNGSTPLHLAARDGL-LDCVKVLVQSGAN 236
Cdd:PHA02876 257 LLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVP---KLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGAD 333

                         90
                 ....*....|..
gi 169403957 237 VHAQDAMGYKPI 248
Cdd:PHA02876 334 VNAADRLYITPL 345
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 210-241 6.85e-08

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: 48.05  E-value: 6.85e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 169403957  210 NGSTPLHLAA-RDGLLDCVKVLVQSGANVHAQD 241
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
197-251 6.86e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 6.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 169403957  197 LLEKG-ADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFC 251
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 167-265 8.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 8.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 167 VDLLTNNSQTPLHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYK 246
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGD----LESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                         90
                 ....*....|....*....
gi 169403957 247 PIDFCKIWNHRACARFLKD 265
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLID 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 144-266 1.24e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 144 IHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGL 223
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK----LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 169403957 224 LDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDA 266
Cdd:PHA02875 148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 136-294 1.50e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 136 TDDKGFTAIHFAAQwgKLACLQVLVE---EYKFPVDLLTNNSQTPLHLV---IHRDNTTV-----------ALPCIYYLL 198
Cdd:PHA03100 102 PDNNGITPLLYAIS--KKSNSYSIVEyllDNGANVNIKNSDGENLLHLYlesNKIDLKILkllidkgvdinAKNRVNYLL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 199 EKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIdfckiwnHRACARFLKD------------- 265
Cdd:PHA03100 180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL-------HIAILNNNKEifklllnngpsik 252

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169403957 266 -----AMWKKDKKDFARemTKMKMFKSQLTLMEH 294
Cdd:PHA03100 253 tiietLLYFKDKDLNTI--TKIKMLKKSIMYMFL 284
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 140-244 1.74e-07

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: 52.71  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 140 GFTAIHFAAQWGKLACLQVLVEEykfpVDLLTNN--------SQTPLHLVIHRDNTTValpcIYYLLEKGAD-LNAQTCN 210
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEA----APELVNEpmtsdlyqGETALHIAVVNQNLNL----VRELIARGADvVSPRATG 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 169403957 211 -------------GSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMG 244
Cdd:cd22192  123 tffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 137-249 2.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 137 DDKGFTAIHFAAQWGKLACLQVLVEEYKFpVDLLTNNSQTPLHLVIHRDNTTVALpciyylLEKGADLNAQTCNGSTPLH 216
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNH-IMNKCKNGFTPLHNAIIHNRSAIEL------LINNASINDQDIDGSTPLH 259

                         90       100       110
                 ....*....|....*....|....*....|....
gi 169403957 217 LAARDGL-LDCVKVLVQSGANVHAQDAMGYKPID 249
Cdd:PHA02874 260 HAINPPCdIDIIDILLYHKADISIKDNKGENPID 293
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-263 2.34e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 169403957  211 GSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFL 263
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 175-244 9.84e-07

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: 50.46  E-value: 9.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957  175 QTPLHLVIHRDNttvaLPCIYYLLEKGADLNAqTCNGS---------------TPLHLAARDGLLDCVKVLVQSGANVHA 239
Cdd:TIGR00870 129 ITALHLAAHRQN----YEIVKLLLERGASVPA-RACGDffvksqgvdsfyhgeSPLNAAACLGSPSIVALLSEDPADILT 203


                  ....*
gi 169403957  240 QDAMG 244
Cdd:TIGR00870 204 ADSLG 208
Ank_5 pfam13857
Ankyrin repeats (many copies);
159-218 1.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957  159 LVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVALpciyYLLEKGADLNAQTCNGSTPLHLA 218
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVR----VLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 210-239 1.05e-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: 44.50  E-value: 1.05e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 169403957   210 NGSTPLHLAARDGLLDCVKVLVQSGANVHA 239
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 117-244 2.14e-06

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: 49.49  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 117 VGNVEWLRFCLNQSLREIPTddKGFTAIHFAA---QWGKLACLQVLVEEYKFPVDL--LTNNS--------QTPLHLVIH 183
Cdd:cd21882    5 LGLLECLRWYLTDSAYQRGA--TGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPkeLVNAPctdefyqgQTALHIAIE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169403957 184 RDNttvaLPCIYYLLEKGADLNAQTCN-------------GSTPLHLAARDGLLDCVKVLVQSG---ANVHAQDAMG 244
Cdd:cd21882   83 NRN----LNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLG 155
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 137-255 3.63e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 137 DDKGFTAIHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTvalPCIYYLLEKGADLNAQTCNGSTPLH 216
Cdd:PHA02876 270 DDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDT---ENIRTLIMLGADVNAADRLYITPLH 346

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 169403957 217 LAAR-DGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWN 255
Cdd:PHA02876 347 QASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 134-240 3.89e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 134 IPTDDKGFTAIHFAAQwGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVI-HRDNttvalPCIYYLLEKGADLNAQTCNGS 212
Cdd:PHA02878 162 MKDRHKGNTALHYATE-NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVkHYNK-----PIVHILLENGASTDARDKCGN 235

                         90       100
                 ....*....|....*....|....*....
gi 169403957 213 TPLHLAARDGL-LDCVKVLVQSGANVHAQ 240
Cdd:PHA02878 236 TPLHISVGYCKdYDILKLLLEHGVDVNAK 264
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 139-237 4.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 139 KGFTAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHL-VIHRDNTTVALpciyyLLEKGADLNAQTCNGSTPLHL 217
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIA-RGADPDIPNTDKFSPLHLaVMMGDIKGIEL-----LIDHKACLDIEDCCGCTPLII 174

                         90       100
                 ....*....|....*....|
gi 169403957 218 AARDGLLDCVKVLVQSGANV 237
Cdd:PHA02875 175 AMAKGDIAICKMLLDSGANI 194
PHA03095 PHA03095
ankyrin-like protein; Provisional
 140-242 4.40e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 140 GFTAIHFAAQWG-KLACLQVLVEeYKFPVDLLTNNSQTPLHlvIHRDNTTVALPCIYYLLEKGADLNAQTCNGSTPLH-- 216
Cdd:PHA03095  83 GFTPLHLYLYNAtTLDVIKLLIK-AGADVNAKDKVGRTPLH--VYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvl 159

                         90       100
                 ....*....|....*....|....*.
gi 169403957 217 LAARDGLLDCVKVLVQSGANVHAQDA 242
Cdd:PHA03095 160 LKSRNANVELLRLLIDAGADVYAVDD 185
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 197-244 4.59e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 4.59e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 169403957 197 LLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMG 244
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG 591
PHA03095 PHA03095
ankyrin-like protein; Provisional
 119-264 4.60e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 4.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 119 NVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKL--ACLQVLVEEYKFP--VDLLTNnsqTPLHLVihRDNTTVALPCI 194
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPaaTDMLGN---TPLHSM--ATGSSCKRSLV 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169403957 195 YYLLEKGADLNAQTCNGSTPLHLAA---RDGLLDCvkvLVQSGANVHAQDAMGYKPIDF----CkiwNHRACARFLK 264
Cdd:PHA03095 241 LPLLIAGISINARNRYGQTPLHYAAvfnNPRACRR---LIALGADINAVSSDGNTPLSLmvrnN---NGRAVRAALA 311
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 197-249 4.77e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 4.77e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169403957 197 LLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPID 249
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
Ank_4 pfam13637
Ankyrin repeats (many copies);
176-231 5.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 5.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 169403957  176 TPLHLVIHRDNttvaLPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLV 231
Cdd:pfam13637   3 TALHAAAASGH----LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 142-248 5.95e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 142 TAIHFAAQWGKLACLQVLVEeYKFPVDLLTNNSQTPLHLVIHRDNTTVAlpcIYYLLEKGADLNAQTCNGSTPLHLAARD 221
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLD-YGADIEALSQKIGTALHFALCGTNPYMS---VKTLIDRGANVNSKNKDLSTPLHYACKK 452

                         90       100
                 ....*....|....*....|....*...
gi 169403957 222 GL-LDCVKVLVQSGANVHAQDAMGYKPI 248
Cdd:PHA02876 453 NCkLDVIEMLLDNGADVNAINIQNQYPL 480
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 175-244 9.52e-06

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: 47.49  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 175 QTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCN--------------GSTPLHLAARDGLLDCVKVLVQ---SGANV 237
Cdd:cd22196   95 QTALHIAIERRNMHL----VELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADI 170


                 ....*..
gi 169403957 238 HAQDAMG 244
Cdd:cd22196  171 SARDSMG 177
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-198 3.61e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 3.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 169403957  142 TAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNttvaLPCIYYLL 198
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGN----VEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 154-262 3.86e-05

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: 45.46  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957  154 ACLQVLVEEYKFPVDLLTNnsqtpLHLVIHRDNTTVALPciyyllekgadlNAQTCN----GSTPLHLAARDGLLDCVKV 229
Cdd:TIGR00870  84 TLLHAISLEYVDAVEAILL-----HLLAAFRKSGPLELA------------NDQYTSeftpGITALHLAAHRQNYEIVKL 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 169403957  230 LVQSGANVHAQdAMGykpiDFCKIWNHRACARF 262
Cdd:TIGR00870 147 LLERGASVPAR-ACG----DFFVKSQGVDSFYH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-160 6.51e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 6.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 169403957  112 LFAAAV-GNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLV 160
Cdd:pfam13637   5 LHAAAAsGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 175-244 6.98e-05

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: 44.40  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 175 QTPLHLVIHRDNTTvalpCIYYLLEKGADLNAQTCN--------------GSTPLHLAARDGLLDCVKVLVQSG---ANV 237
Cdd:cd22193   77 QTALHIAIERRQGD----IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADI 152


                 ....*..
gi 169403957 238 HAQDAMG 244
Cdd:cd22193  153 EAQDSRG 159
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 171-248 8.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 171 TNNSQTPLH-LVIHRDNTTVALPCIYYLLEKGADLNAQTCNGSTPLHLAA--RDGLLDCVKVLVQSGANVHAQDAMGYKP 247
Cdd:PHA03100  65 TKNNSTPLHyLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENL 144


                 .
gi 169403957 248 I 248
Cdd:PHA03100 145 L 145
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 210-239 1.58e-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: 38.39  E-value: 1.58e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 169403957  210 NGSTPLHLAARDGLLDCVKVLVQSGANVHA 239
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 172-248 1.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169403957 172 NNSQTPLHLVIHRDNTTVAlpciYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPI 248
Cdd:PHA02878 166 HKGNTALHYATENKDQRLT----ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 176-248 4.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 4.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169403957 176 TPLHLVIHRdntTVALPCIYYLLEKGADLNAQ-TCNGSTPLHLAARDGllDCVKVLVQSGANVHAQDAMGYKPI 248
Cdd:PHA02878 236 TPLHISVGY---CKDYDILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPL 304
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 155-244 5.61e-04

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: 41.67  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 155 CLQVLV------EEYKfpvdlltnnSQTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCN--------------GSTP 214
Cdd:cd22194  125 ILDRFInaeyteEAYE---------GQTALNIAIERRQGDI----VKLLIAKGADVNAHAKGvffnpkykhegfyfGETP 191

                         90       100       110
                 ....*....|....*....|....*....|.
gi 169403957 215 LHLAARDGLLDCVKVLVQSGA-NVHAQDAMG 244
Cdd:cd22194  192 LALAACTNQPEIVQLLMEKEStDITSQDSRG 222
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 193-240 6.66e-04

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: 41.38  E-value: 6.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169403957 193 CIYYLLEKGAD-------LNAQTCN----GSTPLHLAARDGLLDCVKVLVQSGANVHAQ 240
Cdd:cd22197   65 CIMPLLEIDKDsgnpkplVNAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGADVHAR 123
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 157-251 1.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 157 QVLVEEYKFPVdlltnnsqTPLHLVIHRDNTTValpcIYYLLEKGADLNAQTCNGSTPLHLAARDGL-----LDCVKVLV 231
Cdd:PHA03100  26 DLNDYSYKKPV--------LPLYLAKEARNIDV----VKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLL 93

                         90       100
                 ....*....|....*....|
gi 169403957 232 QSGANVHAQDAMGYKPIDFC 251
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLYA 113
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 185-248 1.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 1.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169403957 185 DNTTVALPC-----IYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPI 248
Cdd:PHA02874  93 DTSILPIPCiekdmIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 151-244 1.65e-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: 40.22  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 151 GKLACLQVLVEE------YKFPVDLLTNNS----QTPLHLVIHRDNttvaLPCIYYLLEKGADLNAQTCN---------- 210
Cdd:cd22197   61 GVNACIMPLLEIdkdsgnPKPLVNAQCTDEyyrgHSALHIAIEKRS----LQCVKLLVENGADVHARACGrffqkkqgtc 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 169403957 211 ---GSTPLHLAARDGLLDCVKVLVQSG---ANVHAQDAMG 244
Cdd:cd22197  137 fyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLG 176
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 112-263 1.72e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 112 LFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLVIHRDNTTval 191
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLL-KHACNVHIRDANGNTALWNAISAKHHK--- 605

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169403957 192 pcIYYLLEKGADLNAQTCNGSTpLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFL 263
Cdd:PLN03192 606 --IFRILYHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 175-250 1.78e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 1.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169403957 175 QTPLHLVIHRDNTTVALpciyYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGyKPIDF 250
Cdd:PTZ00322 116 RTPLHIACANGHVQVVR----VLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA-KPDSF 186
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 175-208 3.42e-03

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: 34.57  E-value: 3.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 169403957  175 QTPLHLVIHRDNttvALPCIYYLLEKGADLNAQT 208
Cdd:pfam00023   3 NTPLHLAAGRRG---NLEIVKLLLSKGADVNARD 33
PHA02741 PHA02741
hypothetical protein; Provisional
 175-253 4.79e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 37.33  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169403957 175 QTPLHLVIHRDNTTVALPCIYYLLEKGADLNAQ-TCNGSTPLHLAARDGLLDCVKVLV-QSGANVHAQDAMGYKPIDFCK 252
Cdd:PHA02741  61 QMCIHIAAEKHEAQLAAEIIDHLIELGADINAQeMLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAI 140


                 .
gi 169403957 253 I 253
Cdd:PHA02741 141 D 141
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 197-238 5.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 5.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 169403957 197 LLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVH 238
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-181 8.94e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.24  E-value: 8.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 169403957  136 TDDKGFTAIHFAAQWGKLACLQVLVeEYKFPVDLLTNNSQTPLHLV 181
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
 
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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