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Conserved domains on  [gi|489182180|ref|WP_003091630|]
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MULTISPECIES: ankyrin repeat domain-containing protein [Pseudomonas]

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];
9-167 1.16e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   9 LDMETQEFVHQLFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAG 88
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489182180  89 AAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-167 1.16e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   9 LDMETQEFVHQLFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAG 88
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489182180  89 AAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-145 2.78e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   53 LMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAgGADVEGASaDGKTALMMAAMFNQAEVAA 132
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 489182180  133 SLLAHGARRDAQD 145
Cdd:pfam12796  79 LLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-143 1.39e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  20 LFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQT--------------- 84
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTalwnaisakhhkifr 608

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489182180  85 ----------PLAG------AAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDA 143
Cdd:PLN03192 609 ilyhfasisdPHAAgdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 20-152 6.85e-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: 59.64  E-value: 6.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  20 LFDLARQGNSQRLEQLL-QQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLayKADPDLRNLA-------GQTPLAGAAF 91
Cdd:cd22192   21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EAAPELVNEPmtsdlyqGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489182180  92 KGDLAMVELLLAGGADVEGASAD--------------GKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPL 152
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 20-159 2.40e-06

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: 46.61  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   20 LFDLARQGNSQRLEQLLqqgLPPNLRNHKGDSLLMLASYHGHaDTVRLLLAY--KADPDLRNL------------AGQTP 85
Cdd:TIGR00870  56 LFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYV-DAVEAILLHllAAFRKSGPLelandqytseftPGITA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   86 LAGAAFKGDLAMVELLLAGGADVEGA-------SADGKTA-------LMMAAMFNQAEVAASLLAHGARRDAQDAAGLTP 151
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTL 211


                  ....*...
gi 489182180  152 LAAARMMN 159
Cdd:TIGR00870 212 LHLLVMEN 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-77 1.23e-03

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: 34.87  E-value: 1.23e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 489182180    48 KGDSLLMLASYHGHADTVRLLLAYKADPDL 77
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-167 1.16e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   9 LDMETQEFVHQLFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAG 88
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489182180  89 AAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-167 5.00e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.42  E-value: 5.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  20 LFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVE 99
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489182180 100 LLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:COG0666  138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-167 9.16e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 9.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  24 ARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLA 103
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489182180 104 GGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-167 1.24e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  20 LFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVE 99
Cdd:COG0666   25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489182180 100 LLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:COG0666  105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-145 2.78e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   53 LMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAgGADVEGASaDGKTALMMAAMFNQAEVAA 132
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 489182180  133 SLLAHGARRDAQD 145
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-152 5.95e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.15  E-value: 5.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  24 ARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLA 103
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489182180 104 GGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPL 152
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
20-108 4.97e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   20 LFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYkADPDLRNlAGQTPLAGAAFKGDLAMVE 99
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*....
gi 489182180  100 LLLAGGADV 108
Cdd:pfam12796  79 LLLEKGADI 87
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-143 1.39e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  20 LFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQT--------------- 84
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTalwnaisakhhkifr 608

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489182180  85 ----------PLAG------AAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDA 143
Cdd:PLN03192 609 ilyhfasisdPHAAgdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 19-142 3.11e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  19 QLFDLARQGNSQRLEQLLQQGLPPN-LRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAM 97
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489182180  98 VELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRD 142
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 27-167 5.26e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 5.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  27 GNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGA 106
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489182180 107 DVEGA-SADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:PHA02875  93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 20-152 6.85e-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: 59.64  E-value: 6.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  20 LFDLARQGNSQRLEQLL-QQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLayKADPDLRNLA-------GQTPLAGAAF 91
Cdd:cd22192   21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EAAPELVNEPmtsdlyqGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489182180  92 KGDLAMVELLLAGGADVEGASAD--------------GKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPL 152
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-109 1.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 1.33e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489182180  31 RLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVE 109
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-170 1.88e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  49 GDSLL--MLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLA--MVELLLAGGADVEGASADGKTALMMAAM 124
Cdd:PHA03095 187 FRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAV 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489182180 125 FNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATV--ALLSRP 170
Cdd:PHA03095 267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVraALAKNP 314
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-167 5.13e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 5.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  52 LLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPL-AGAAFKGDLAMVELLLAGGADVEGASADGKTAL--MMAAMFNQA 128
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINP 132

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489182180 129 EVAASLLAHGARRDAQDAAGLTPLAAArMMNAEATVALL 167
Cdd:PHA03095 133 KVIRLLLRKGADVNALDLYGMTPLAVL-LKSRNANVELL 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-167 8.96e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 8.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  32 LEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGA 111
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489182180 112 SADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-155 1.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  10 DMETQEFVHQLFdlaRQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGA 89
Cdd:PHA02874 121 DAELKTFLHYAI---KKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489182180  90 AFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAevAASLLAHGARRDAQDAAGLTPLAAA 155
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHA 261
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 60-148 1.21e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  60 GHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGA 139
Cdd:PTZ00322  93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                 ....*....
gi 489182180 140 RRDAQDAAG 148
Cdd:PTZ00322 173 CHFELGANA 181
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 19-116 3.85e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 3.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  19 QLFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMV 98
Cdd:PTZ00322  85 ELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                         90
                 ....*....|....*...
gi 489182180  99 ELLLAGGADVEGASADGK 116
Cdd:PTZ00322 165 QLLSRHSQCHFELGANAK 182
PHA03095 PHA03095
ankyrin-like protein; Provisional
 62-152 2.30e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  62 ADTVRLLLAYKADPDLRNLAGQTPLA---GAAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQ-AEVAASLLAH 137
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106

                         90
                 ....*....|....*
gi 489182180 138 GARRDAQDAAGLTPL 152
Cdd:PHA03095 107 GADVNAKDKVGRTPL 121
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-139 3.01e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  28 NSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGAD 107
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489182180 108 VEGASADGKTALMMAAM-FNQAEVAASLLAHGA 139
Cdd:PHA02875 194 IDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGA 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 28-168 1.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  28 NSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGAD 107
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489182180 108 VEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALLS 168
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLIN 243
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 9-167 1.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   9 LDMETQEFVHQLFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKAD------PDL----- 77
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpiPCIekdmi 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  78 ------------RNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQD 145
Cdd:PHA02874 108 ktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187

                        170       180
                 ....*....|....*....|..
gi 489182180 146 AAGLTPLAAARMMNAEATVALL 167
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLL 209
Ank_4 pfam13637
Ankyrin repeats (many copies);
49-102 1.74e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.74e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489182180   49 GDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLL 102
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 8-155 3.05e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   8 ELDMETQEFVHQLFDLARQGNSQRL-EQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPL 86
Cdd:PHA02878 159 DINMKDRHKGNTALHYATENKDQRLtELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489182180  87 -AGAAFKGDLAMVELLLAGGADVEGASA-DGKTALMMAamFNQAEVAASLLAHGARRDAQDAAGLTPLAAA 155
Cdd:PHA02878 239 hISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 32-145 8.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 8.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  32 LEQLLQQGLPPNLRNHKGDSLLMLASYHGHA-----DTVRLLLAYKADPDLRNLAGQTPLAGAAFK--GDLAMVELLLAG 104
Cdd:PHA03100  51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489182180 105 GADVEGASADGKTALMMAAMFNQA--EVAASLLAHGARRDAQD 145
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKN 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-157 9.00e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 9.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  61 HADTVRLLLAYKADPDLRNLAGQTPLA------GAafkgDLAMVELLLAGGADVEGASADGKTALMMAAMF--NQAEVAA 132
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPLAvllksrNA----NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVR 206

                         90       100
                 ....*....|....*....|....*
gi 489182180 133 SLLAHGARRDAQDAAGLTPLAAARM 157
Cdd:PHA03095 207 ELIRAGCDPAATDMLGNTPLHSMAT 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 90-169 1.10e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  90 AFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALLSR 169
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-169 2.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  62 ADTVRLLLAYKADPDLRNL-AGQTPLAGAAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGAR 140
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489182180 141 RDAQDAAGLTPL--AAARMMNAEATVALLSR 169
Cdd:PHA02878 227 TDARDKCGNTPLhiSVGYCKDYDILKLLLEH 257
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 20-159 2.40e-06

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: 46.61  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   20 LFDLARQGNSQRLEQLLqqgLPPNLRNHKGDSLLMLASYHGHaDTVRLLLAY--KADPDLRNL------------AGQTP 85
Cdd:TIGR00870  56 LFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYV-DAVEAILLHllAAFRKSGPLelandqytseftPGITA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180   86 LAGAAFKGDLAMVELLLAGGADVEGA-------SADGKTA-------LMMAAMFNQAEVAASLLAHGARRDAQDAAGLTP 151
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTL 211


                  ....*...
gi 489182180  152 LAAARMMN 159
Cdd:TIGR00870 212 LHLLVMEN 219
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 18-154 3.20e-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: 45.95  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  18 HQLFDLARQGNSQRLEQLLqqglPPNLRNHK------------GDSLL---MLASYHGHADTVRLLL--AYKAD--PDLR 78
Cdd:cd22196    8 RRIFDAVAKGDCKELDGLL----EYLMRTKKrltdsefkdpetGKTCLlkaMLNLHNGQNDTISLLLdiAEKTGnlKEFV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  79 NLA-------GQTPLAGAAFKGDLAMVELLLAGGADVEgASADGK---------------TALMMAAMFNQAEVAASLLA 136
Cdd:cd22196   84 NAAytdsyykGQTALHIAIERRNMHLVELLVQNGADVH-ARASGEffkkkkggpgfyfgeLPLSLAACTNQLDIVKFLLE 162

                        170       180
                 ....*....|....*....|.
gi 489182180 137 H---GARRDAQDAAGLTPLAA 154
Cdd:cd22196  163 NphsPADISARDSMGNTVLHA 183
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-152 5.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  35 LLQQGLPPNLRN-HKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGASA 113
Cdd:PHA02878 153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489182180 114 DGKTALMMAAMF-NQAEVAASLLAHGARRDAQDAA-GLTPL 152
Cdd:PHA02878 233 CGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTAL 273
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-131 7.35e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 7.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  32 LEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEga 111
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE-- 317

                         90       100
                 ....*....|....*....|
gi 489182180 112 sadgktalMMAAMFNQAEVA 131
Cdd:PHA03095 318 --------TVAATLNTASVA 329
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-80 1.89e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 1.89e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489182180  24 ARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNL 80
Cdd:PLN03192 630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-143 5.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 5.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  29 SQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGH-ADTVRLLLAYKADPDLRNLAGQTPLAGAA-FKGDLAMVELLLAGGA 106
Cdd:PHA02876 287 SRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGA 366

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489182180 107 DVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDA 143
Cdd:PHA02876 367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-89 6.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489182180   35 LLQQG-LPPNLRNHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGA 89
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 63-139 7.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 7.41e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489182180  63 DTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGA 139
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 46-167 1.24e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  46 NHKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMF 125
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489182180 126 NQAEVaASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:PLN03192 602 KHHKI-FRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELL 642
Ank_2 pfam12796
Ankyrin repeats (3 copies);
119-167 2.74e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.17  E-value: 2.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489182180  119 LMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPLAAARMMNAEATVALL 167
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-79 3.46e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 3.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489182180   24 ARQGNSQRLEQLLQQGlPPNLRNHkGDSLLMLASYHGHADTVRLLLAYKADPDLRN 79
Cdd:pfam12796  38 AKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 54-154 3.78e-04

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: 39.86  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  54 MLASYHGHADTVRLLLayKADPDLRNLA-------------GQTPLAGAAFKGDLAMVELLLAGGADVEGASAD------ 114
Cdd:cd21882   34 ALNLNDGVNEAIMLLL--EAAPDSGNPKelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrks 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489182180 115 -------GKTALMMAAMFNQAEVAASLLAHGAR---RDAQDAAGLTPLAA 154
Cdd:cd21882  112 pgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHA 161
Ank_4 pfam13637
Ankyrin repeats (many copies);
20-69 5.43e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 5.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 489182180   20 LFDLARQGNSQRLEQLLQQGLPPNLRNHKGDSLLMLASYHGHADTVRLLL 69
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 67-166 6.87e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  67 LLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLLAHGARRDAQDa 146
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND- 241

                         90       100
                 ....*....|....*....|
gi 489182180 147 agLTPLAAARMMNAEATVAL 166
Cdd:PHA02876 242 --LSLLKAIRNEDLETSLLL 259
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-135 9.60e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 9.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489182180   84 TPLAGAAFKGDLAMVELLLAGGADVEGASADGKTALMMAAMFNQAEVAASLL 135
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-77 1.23e-03

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: 34.87  E-value: 1.23e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 489182180    48 KGDSLLMLASYHGHADTVRLLLAYKADPDL 77
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-167 2.25e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.56  E-value: 2.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489182180  117 TALMMAAMFNQAEVAASLLAHGARRDAQDAAGLTPL-AAARMMNAEATVALL 167
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALhFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 47-114 2.43e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 2.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489182180  47 HKGDSLLMLASYHGHADTVRLLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGASAD 114
Cdd:PLN03192 620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-79 2.80e-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: 33.80  E-value: 2.80e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 489182180   48 KGDSLLMLASYH-GHADTVRLLLAYKADPDLRN 79
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 32-154 3.03e-03

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: 37.47  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  32 LEQLLQQGL--PPNLRNHK------GDSLLMLASYH---GHADTVRLLLAYKADPD-LRNLA----------GQTPLAGA 89
Cdd:cd22193    4 LLGFLQDLCrrRKDLTDSEftesstGKTCLMKALLNlnpGTNDTIRILLDIAEKTDnLKRFInaeytdeyyeGQTALHIA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  90 AFKGDLAMVELLLAGGADVEGASAD--------------GKTALMMAAMFNQAEVAASLLAHG---ARRDAQDAAGLTPL 152
Cdd:cd22193   84 IERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVL 163


                 ..
gi 489182180 153 AA 154
Cdd:cd22193  164 HA 165
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-122 3.03e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.24  E-value: 3.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489182180   67 LLLAYKADPDLRNLAGQTPLAGAAFKGDLAMVELLLAGGADVEGASADGKTALMMA 122
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 47-155 5.17e-03

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: 36.53  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182180  47 HKGDSLLMLASYHGHADTVRLLLAYKAD------------PDLRNLA--GQTPLAGAAFKGDLAMVELLLAGGADVEGAS 112
Cdd:cd22192   87 YQGETALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489182180 113 ADGKTALMMAAMFNQAEVAAS----LLAHGARRDAQ------DAAGLTPLAAA 155
Cdd:cd22192  167 SLGNTVLHILVLQPNKTFACQmydlILSYDKEDDLQpldlvpNNQGLTPFKLA 219
 
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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