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Conserved domains on  [gi|15230470|ref|NP_187842|]
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Ankyrin repeat family protein [Arabidopsis thaliana]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12380331)

ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PGG pfam13962
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ...
 413-519 7.55e-37

Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.


:

Pssm-ID: 433609  Cd Length: 114  Bit Score: 132.68  E-value: 7.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   413 EGINNATNSVTVVAVLFATVAFAAIFTVPGG------DNNDGSAVVVGRASFKIFFIFNALALFTSLAVVVVQITLVRGE 486
Cdd:pfam13962   2 EWLKEARNTLLLVATLIATVTFAAGFTPPGGywqdddGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDF 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15230470   487 TKAEKRVVEVINKLMWLASMCTSVAFLASSYIV 519
Cdd:pfam13962  82 LRSLPRKLRIGLKLLWVALLSMLVAFAAGSYRV 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-320 1.08e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 1.08e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  73 HNDTELHLAAQRGDLAAVQQILKDINSQMEGILSGEEFDAEVAEIRASIVNEVNELGETALFTAADKGHLDVVKELLKYs 152
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 153 sRESIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDATLSQTfGPSNATPLVSAAMRGHTEVVNQLLsKAGNLLEISRSNN 232
Cdd:COG0666 110 -GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDG 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 233 KNALHLAARQGHVEVIKALLSKDPQLARRiDKKGQTALHMAVKGQSSEVVKLLLDADpAIVMQPDKSCNTALHVATRKKR 312
Cdd:COG0666 187 ETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGA 264


                ....*...
gi 15230470 313 AEIVELLL 320
Cdd:COG0666 265 ALIVKLLL 272
 
Name Accession Description Interval E-value
PGG pfam13962
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ...
 413-519 7.55e-37

Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.


Pssm-ID: 433609  Cd Length: 114  Bit Score: 132.68  E-value: 7.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   413 EGINNATNSVTVVAVLFATVAFAAIFTVPGG------DNNDGSAVVVGRASFKIFFIFNALALFTSLAVVVVQITLVRGE 486
Cdd:pfam13962   2 EWLKEARNTLLLVATLIATVTFAAGFTPPGGywqdddGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDF 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15230470   487 TKAEKRVVEVINKLMWLASMCTSVAFLASSYIV 519
Cdd:pfam13962  82 LRSLPRKLRIGLKLLWVALLSMLVAFAAGSYRV 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-320 1.08e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 1.08e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  73 HNDTELHLAAQRGDLAAVQQILKDINSQMEGILSGEEFDAEVAEIRASIVNEVNELGETALFTAADKGHLDVVKELLKYs 152
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 153 sRESIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDATLSQTfGPSNATPLVSAAMRGHTEVVNQLLsKAGNLLEISRSNN 232
Cdd:COG0666 110 -GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDG 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 233 KNALHLAARQGHVEVIKALLSKDPQLARRiDKKGQTALHMAVKGQSSEVVKLLLDADpAIVMQPDKSCNTALHVATRKKR 312
Cdd:COG0666 187 ETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGA 264


                ....*...
gi 15230470 313 AEIVELLL 320
Cdd:COG0666 265 ALIVKLLL 272
Ank_2 pfam12796
Ankyrin repeats (3 copies);
236-321 2.80e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   236 LHLAARQGHVEVIKALLSKDPQlARRIDKKGQTALHMAVKGQSSEVVKLLLDadpaiVMQPDKSCN--TALHVATRKKRA 313
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-----HADVNLKDNgrTALHYAARSGHL 74


                  ....*...
gi 15230470   314 EIVELLLS 321
Cdd:pfam12796  75 EIVKLLLE 82
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 133-321 1.15e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  133 LFTAADKGHLDVVKELLKysSRESIAKKNRSGYDPLHIAAIQGHHA-----IVEVLLDHDATLSQTFGPSNaTPLVSAAM 207
Cdd:PHA03100  39 LYLAKEARNIDVVKILLD--NGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGI-TPLLYAIS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  208 R--GHTEVVNQLLSKAGNLlEISRSNNKNALHLAARQGHV--EVIKALLSK--DPQLARRI-------------DKKGQT 268
Cdd:PHA03100 116 KksNSYSIVEYLLDNGANV-NIKNSDGENLLHLYLESNKIdlKILKLLIDKgvDINAKNRVnyllsygvpinikDVYGFT 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15230470  269 ALHMAVKGQSSEVVKLLLD--ADPAIVmqpDKSCNTALHVATRKKRAEIVELLLS 321
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDlgANPNLV---NKYGDTPLHIAILNNNKEIFKLLLN 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 223-321 3.13e-08

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: 56.56  E-value: 3.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 223 NLLEISRSNNkNALHLAARQGHVEVIKALLSKDpqlarRID-----KKGQTALHMAVKGQSSEVVKLLLDADPAIVMQPD 297
Cdd:cd22192   9 HLLQQKRISE-SPLLLAAKENDVQAIKKLLKCP-----SCDlfqrgALGETALHVAALYDNLEAAVVLMEAAPELVNEPM 82

                        90       100
                ....*....|....*....|....*...
gi 15230470 298 KS----CNTALHVATRKKRAEIVELLLS 321
Cdd:cd22192  83 TSdlyqGETALHIAVVNQNLNLVRELIA 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 81-342 1.23e-04

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: 45.07  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470    81 AAQRGDLAAVQQILkdinsqmegilsgeefdaevAEIRASIVNEVNELGETALFTAADKGHLDVVKELLKYSSRESiakk 160
Cdd:TIGR00870  24 AAERGDLASVYRDL--------------------EEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRG---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   161 nRSGYDPLHIAAiQGHHAIVEVLLDHdatLSQTFGPSNATPLVSAAM-----RGHTevvnqllskagnlleisrsnnknA 235
Cdd:TIGR00870  80 -AVGDTLLHAIS-LEYVDAVEAILLH---LLAAFRKSGPLELANDQYtseftPGIT-----------------------A 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   236 LHLAARQGHVEVIKALLSKDPQLARR------IDKKGQTA-------LHMAVKGQSSEVVKLLLDaDPAIVMQPDKSCNT 302
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARacgdffVKSQGVDSfyhgespLNAAACLGSPSIVALLSE-DPADILTADSLGNT 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15230470   303 ALH--VATRKKRAEIVEL-------LLSLPDTNANT------LTRDHKTALDIAE 342
Cdd:TIGR00870 211 LLHllVMENEFKAEYEELscqmynfALSLLDKLRDSkeleviLNHQGLTPLKLAA 265
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 164-190 1.86e-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: 36.03  E-value: 1.86e-03
                           10        20
                   ....*....|....*....|....*..
gi 15230470    164 GYDPLHIAAIQGHHAIVEVLLDHDATL 190
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
PGG pfam13962
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ...
 413-519 7.55e-37

Domain of unknown function; The PGG domain is named for the highly conserved sequence motif found at the startt of the domain. The function is not known.


Pssm-ID: 433609  Cd Length: 114  Bit Score: 132.68  E-value: 7.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   413 EGINNATNSVTVVAVLFATVAFAAIFTVPGG------DNNDGSAVVVGRASFKIFFIFNALALFTSLAVVVVQITLVRGE 486
Cdd:pfam13962   2 EWLKEARNTLLLVATLIATVTFAAGFTPPGGywqdddGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDF 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15230470   487 TKAEKRVVEVINKLMWLASMCTSVAFLASSYIV 519
Cdd:pfam13962  82 LRSLPRKLRIGLKLLWVALLSMLVAFAAGSYRV 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
73-320 1.08e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 1.08e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  73 HNDTELHLAAQRGDLAAVQQILKDINSQMEGILSGEEFDAEVAEIRASIVNEVNELGETALFTAADKGHLDVVKELLKYs 152
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 153 sRESIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDATLSQTfGPSNATPLVSAAMRGHTEVVNQLLsKAGNLLEISRSNN 232
Cdd:COG0666 110 -GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDG 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 233 KNALHLAARQGHVEVIKALLSKDPQLARRiDKKGQTALHMAVKGQSSEVVKLLLDADpAIVMQPDKSCNTALHVATRKKR 312
Cdd:COG0666 187 ETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGA 264


                ....*...
gi 15230470 313 AEIVELLL 320
Cdd:COG0666 265 ALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
77-369 5.46e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 5.46e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  77 ELHLAAQRGDLAAVQQILKDINSQMEGILSGEEFDAEVAEIRASIVNEVNELGETALFTAADKGHLDVVKELLKYSsrES 156
Cdd:COG0666   2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG--AD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 157 IAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDATLSQTfGPSNATPLVSAAMRGHTEVVNQLLSKAGNLlEISRSNNKNAL 236
Cdd:COG0666  80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADV-NAQDNDGNTPL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 237 HLAARQGHVEVIKALLSKDPQLARRiDKKGQTALHMAVKGQSSEVVKLLLDADpAIVMQPDKSCNTALHVATRKKRAEIV 316
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIV 235

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230470 317 ELLLSLPDtNANTLTRDHKTALDIAEGLPLSEESSYIKECLARSGALRANELN 369
Cdd:COG0666 236 KLLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-407 1.03e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.13  E-value: 1.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 112 AEVAEIRASIVNEVNELGETALFTAADKGHLDVVKELLKYSSRESIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDATLS 191
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 192 QTFGPSNATPLVSAAMRGHTEVVNQLLsKAGNLLEISRSNNKNALHLAARQGHVEVIKALLSK--DPQLArriDKKGQTA 269
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgaDVNAQ---DNDGNTP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 270 LHMAVKGQSSEVVKLLLDADpAIVMQPDKSCNTALHVATRKKRAEIVELLLSLpDTNANTLTRDHKTALDIAeglpLSEE 349
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLA----AENG 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230470 350 SSYIKECLARSGALRANELNQPRDELRSTVTQIKNDVHIQLEQTKRTNKNVHNISKEL 407
Cdd:COG0666 231 NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-265 5.76e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 5.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  41 ATATAPALVLSNSGKRMDQAGKKKYVKQVTGRHNDTELHLAAQRGDLAAVQQILK---DINSQMEG-----ILSGEEFDA 112
Cdd:COG0666  54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEagaDVNARDKDgetplHLAAYNGNL 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 113 EVAEI---RASIVNEVNELGETALFTAADKGHLDVVKELLKYSSResIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDAT 189
Cdd:COG0666 134 EIVKLlleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD--VNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230470 190 LSQTfGPSNATPLVSAAMRGHTEVVNQLLsKAGNLLEISRSNNKNALHLAARQGHVEVIKALLSKDPQLARRIDKK 265
Cdd:COG0666 212 VNAK-DNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
236-321 2.80e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   236 LHLAARQGHVEVIKALLSKDPQlARRIDKKGQTALHMAVKGQSSEVVKLLLDadpaiVMQPDKSCN--TALHVATRKKRA 313
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-----HADVNLKDNgrTALHYAARSGHL 74


                  ....*...
gi 15230470   314 EIVELLLS 321
Cdd:pfam12796  75 EIVKLLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
205-289 4.01e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 4.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   205 AAMRGHTEVVNQLLsKAGNLLEISRSNNKNALHLAARQGHVEVIKALLSKDPQlarRIDKKGQTALHMAVKGQSSEVVKL 284
Cdd:pfam12796   4 AAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIVKL 79


                  ....*
gi 15230470   285 LLDAD 289
Cdd:pfam12796  80 LLEKG 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 133-321 1.15e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  133 LFTAADKGHLDVVKELLKysSRESIAKKNRSGYDPLHIAAIQGHHA-----IVEVLLDHDATLSQTFGPSNaTPLVSAAM 207
Cdd:PHA03100  39 LYLAKEARNIDVVKILLD--NGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGI-TPLLYAIS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  208 R--GHTEVVNQLLSKAGNLlEISRSNNKNALHLAARQGHV--EVIKALLSK--DPQLARRI-------------DKKGQT 268
Cdd:PHA03100 116 KksNSYSIVEYLLDNGANV-NIKNSDGENLLHLYLESNKIdlKILKLLIDKgvDINAKNRVnyllsygvpinikDVYGFT 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15230470  269 ALHMAVKGQSSEVVKLLLD--ADPAIVmqpDKSCNTALHVATRKKRAEIVELLLS 321
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDlgANPNLV---NKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-188 4.49e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 4.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470    78 LHLAAQRGDLAAVQQILKdinsqmegilsgEEFDAevaeirasivNEVNELGETALFTAADKGHLDVVKELLKYssreSI 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE------------NGADA----------NLQDKNGRTALHLAAKNGHLEIVKLLLEH----AD 54

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15230470   158 AKKNRSGYDPLHIAAIQGHHAIVEVLLDHDA 188
Cdd:pfam12796  55 VNLKDNGRTALHYAARSGHLEIVKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
168-255 6.01e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 6.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   168 LHIAAIQGHHAIVEVLL--DHDATLSQTFGPsnaTPLVSAAMRGHTEVVNQLLSKA-GNLleisRSNNKNALHLAARQGH 244
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLenGADANLQDKNGR---TALHLAAKNGHLEIVKLLLEHAdVNL----KDNGRTALHYAARSGH 73

                          90
                  ....*....|.
gi 15230470   245 VEVIKALLSKD 255
Cdd:pfam12796  74 LEIVKLLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
133-220 1.15e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   133 LFTAADKGHLDVVKELLKYSSRESIAKKNrsGYDPLHIAAIQGHHAIVEVLLDHDATLSQTFGpsnATPLVSAAMRGHTE 212
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN--GRTALHLAAKNGHLEIVKLLLEHADVNLKDNG---RTALHYAARSGHLE 75


                  ....*...
gi 15230470   213 VVNQLLSK 220
Cdd:pfam12796  76 IVKLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
69-235 2.69e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.75  E-value: 2.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  69 VTGRHNDTELHLAAQRGDLAAVQQILK---DINSQ--------MEGILSGeefDAEVAEI---RASIVNEVNELGETALF 134
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEagaDVNAQdndgntplHLAAANG---NLEIVKLlleAGADVNARDNDGETPLH 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 135 TAADKGHLDVVKELLKYSSreSIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDATLSQTfGPSNATPLVSAAMRGHTEVV 214
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGA--DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK-DKDGLTALLLAAAAGAALIV 268

                       170       180
                ....*....|....*....|.
gi 15230470 215 NQLLSKAGNLLEISRSNNKNA 235
Cdd:COG0666 269 KLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 75-272 7.76e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 7.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   75 DTELHLAAQRGDLAAVQQILkDINSQMEGILSGEefdaevaeirasivnevnelGETALFTAADKGHLDVVKELLKYSSR 154
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELL-DLGKFADDVFYKD--------------------GMTPLHLATILKKLDIMKLLIARGAD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  155 ESIAKKNRsgYDPLHIAAIQGHHAIVEVLLDHDATLSQTFGpSNATPLVSAAMRGHTEVVNQLLSKAGNLLEISRSNNKN 234
Cdd:PHA02875 128 PDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDC-CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15230470  235 ALHLAARQGHVEVIKALLSK--DPQLARRIDKKGQTALHM 272
Cdd:PHA02875 205 ALCYAIENNKIDIVRLFIKRgaDCNIMFMIEGEECTILDM 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 145-415 5.18e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 5.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  145 VKELLKYSSresIAKKNRSGYD-PLHIAAIQGHHAIVEVLLDHDATLSQTFGPSNATPLVSAAMRGHTEVVNQLLSKAGN 223
Cdd:PHA02875  51 IKLLMKHGA---IPDVKYPDIEsELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  224 LlEISRSNNKNALHLAARQGHVEVIKALLSKDPQLARRiDKKGQTALHMAVKGQSSEVVKLLLDADPAIVMQPDKSCNTA 303
Cdd:PHA02875 128 P-DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE-DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  304 LHVATRKKRAEIVELLLSL-PDTN-ANTLTRDHKTALDIAEGLPLSEESSYIKECLARSgALRANELNQPRDELRSTVTQ 381
Cdd:PHA02875 206 LCYAIENNKIDIVRLFIKRgADCNiMFMIEGEECTILDMICNMCTNLESEAIDALIADI-AIRIHKKTIRRDEGFKNNMS 284

                        250       260       270
                 ....*....|....*....|....*....|....
gi 15230470  382 IKNDvhiqleqTKRTNKNVHNISKELRKLHREGI 415
Cdd:PHA02875 285 TIED-------KEEFKDVFEKCIIELRRIKSEKI 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
234-286 8.52e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 8.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15230470   234 NALHLAARQGHVEVIKALLSKDPQLARRiDKKGQTALHMAVKGQSSEVVKLLL 286
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 142-292 1.27e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  142 LDVVKELLKYSSResIAKKNRSGYDPLHIAAIQ--GHHAIVEVLLDH--DATLSQTFGpSNATPLVSAAMRGHTEVVNQL 217
Cdd:PHA03100  86 KEIVKLLLEYGAN--VNAPDNNGITPLLYAISKksNSYSIVEYLLDNgaNVNIKNSDG-ENLLHLYLESNKIDLKILKLL 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  218 LSKAGNLLEISR----------SNNKN-----ALHLAARQGHVEVIKALLSK--DPQLarrIDKKGQTALHMAVKGQSSE 280
Cdd:PHA03100 163 IDKGVDINAKNRvnyllsygvpINIKDvygftPLHYAVYNNNPEFVKYLLDLgaNPNL---VNKYGDTPLHIAILNNNKE 239

                        170
                 ....*....|..
gi 15230470  281 VVKLLLDADPAI 292
Cdd:PHA03100 240 IFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
270-341 1.54e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 1.54e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230470   270 LHMAVKGQSSEVVKLLLDADPAIVMQpDKSCNTALHVATRKKRAEIVELLLSLPDTNANTltrDHKTALDIA 341
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYA 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 187-343 2.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  187 DATLSQTFGPSNATPLVSAAMRGHTEVVNQLLSKAGNLLEISRSNNKNALHLAARQGHVEVIKALLSKDPQLARRIDKKG 266
Cdd:PHA02875  23 DIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDG 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230470  267 QTALHMAVKGQSSEVVKLLL--DADPAIvmqPDKSCNTALHVATRKKRAEIVELLLslpdtnantltrDHKTALDIAEG 343
Cdd:PHA02875 103 MTPLHLATILKKLDIMKLLIarGADPDI---PNTDKFSPLHLAVMMGDIKGIELLI------------DHKACLDIEDC 166
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 223-321 3.13e-08

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: 56.56  E-value: 3.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 223 NLLEISRSNNkNALHLAARQGHVEVIKALLSKDpqlarRID-----KKGQTALHMAVKGQSSEVVKLLLDADPAIVMQPD 297
Cdd:cd22192   9 HLLQQKRISE-SPLLLAAKENDVQAIKKLLKCP-----SCDlfqrgALGETALHVAALYDNLEAAVVLMEAAPELVNEPM 82

                        90       100
                ....*....|....*....|....*...
gi 15230470 298 KS----CNTALHVATRKKRAEIVELLLS 321
Cdd:cd22192  83 TSdlyqGETALHIAVVNQNLNLVRELIA 110
Ank_4 pfam13637
Ankyrin repeats (many copies);
131-184 3.39e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 3.39e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15230470   131 TALFTAADKGHLDVVKELLKysSRESIAKKNRSGYDPLHIAAIQGHHAIVEVLL 184
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 122-412 2.09e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  122 VNEVNELGETALFTAADKGHLDVVKELLKYSSRESIakKNRSGYDPLHIAAIQGHHAIVEVLLDHdatlsqtfgpsnatp 201
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI--EDDNGCYPIHIAIKHNFFDIIKLLLEK--------------- 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  202 lvsaamrghtevvnqllskaGNLLEISRSNNKNALHLAARQGHVEVIKALLSKDPQLARRIdKKGQTALHMAVKGQSSeV 281
Cdd:PHA02874 180 --------------------GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC-KNGFTPLHNAIIHNRS-A 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  282 VKLLLDAdpAIVMQPDKSCNTALHVATRKK-RAEIVELLLSlpdTNANTLTRDHKTALDIAEGLPLSEESSYIKECLArs 360
Cdd:PHA02874 238 IELLINN--ASINDQDIDGSTPLHHAINPPcDIDIIDILLY---HKADISIKDNKGENPIDTAFKYINKDPVIKDIIA-- 310

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15230470  361 GALRANELNQPRDelrstvTQIKNdvHIQLEQTKRTNKNVHNISKELRKLHR 412
Cdd:PHA02874 311 NAVLIKEADKLKD------SDFLE--HIEIKDNKEFSDFIKECNEEIEDMKK 354
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 133-286 2.18e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  133 LFTAADKGHLDVVKELLKYSSRESIAkkNRSGYDPLHIAAIQGHHAIVEVLLDHDATLSQTFGPSNaTPLVSAAMRGHTE 212
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN-TALWNAISAKHHK 605

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15230470  213 VVNQllskagnLLEISRSNNKNA----LHLAARQGHVEVIKALLSKDPQLARRiDKKGQTALHMAVKGQSSEVVKLLL 286
Cdd:PLN03192 606 IFRI-------LYHFASISDPHAagdlLCTAAKRNDLTAMKELLKQGLNVDSE-DHQGATALQVAMAEDHVDMVRLLI 675
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 130-321 5.19e-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: 5.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 130 ETALFTAADKGHLDVVKELLKYSSREsIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDATL------SQTFgpSNATPLV 203
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLLKCPSCD-LFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtSDLY--QGETALH 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 204 SAAMRGHTEVVNQLLSKAGNLLE------ISRSNNKNALH-------LAARQGHVEVIKALLSKDPQLaRRIDKKGQTAL 270
Cdd:cd22192  95 IAVVNQNLNLVRELIARGADVVSpratgtFFRPGPKNLIYygehplsFAACVGNEEIVRLLIEHGADI-RAQDSLGNTVL 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 271 HMAV----KGQSSEVVKLLLDADP-----AIVMQPDKSCNTALHVATRKKRAEIVELLLS 321
Cdd:cd22192 174 HILVlqpnKTFACQMYDLILSYDKeddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_5 pfam13857
Ankyrin repeats (many copies);
251-307 5.76e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 5.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230470   251 LLSKDPQLARRIDKKGQTALHMAVKGQSSEVVKLLLDADPAIVMQpDKSCNTALHVA 307
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLK-DEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-254 6.28e-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: 52.32  E-value: 6.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  72 RHNDTELHLAAQRGDLAAVQQILK--DINSQMEGILsGE----------EFDAEVAEIRAS--IVNEV--NEL--GETAL 133
Cdd:cd22192  15 RISESPLLLAAKENDVQAIKKLLKcpSCDLFQRGAL-GEtalhvaalydNLEAAVVLMEAApeLVNEPmtSDLyqGETAL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 134 FTAADKGHLDVVKELLKYSS------------RESIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDATL--SQTFGpsNa 199
Cdd:cd22192  94 HIAVVNQNLNLVRELIARGAdvvspratgtffRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIraQDSLG--N- 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230470 200 TPLVSAAMRGHTEVVNQ----LLSKAGNLLEISRSNNKN-----ALHLAARQGHVEVIKALLSK 254
Cdd:cd22192 171 TVLHILVLQPNKTFACQmydlILSYDKEDDLQPLDLVPNnqgltPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
200-252 2.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15230470   200 TPLVSAAMRGHTEVVnQLLSKAGNLLEISRSNNKNALHLAARQGHVEVIKALL 252
Cdd:pfam13637   3 TALHAAAASGHLELL-RLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 122-189 4.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 4.36e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15230470  122 VNEVNELGETALFTAADKGHLDVVKELLKYSSreSIAKKNRSGYDPLHIAAIQGHHAIVEVLLDHDAT 189
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA--NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_5 pfam13857
Ankyrin repeats (many copies);
285-341 7.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 7.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230470   285 LLDADPAIVMQPDKSCNTALHVATRKKRAEIVELLLSLPdTNANTLTRDHKTALDIA 341
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 129-252 9.59e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 9.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  129 GETALFTAADKGHLDVVKELLKYSSRESIakKNRSGYDPLHIAAIQGHHAIVEVLLdHDATLSQTFGPSNAtpLVSAAMR 208
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHI--RDANGNTALWNAISAKHHKIFRILY-HFASISDPHAAGDL--LCTAAKR 632

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15230470  209 GHTEVVNQLLsKAGNLLEISRSNNKNALHLAARQGHVEVIKALL 252
Cdd:PLN03192 633 NDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02946 PHA02946
ankyin-like protein; Provisional
 145-393 2.14e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  145 VKELLK--YSSRESiakkNRSGYDPLHIAAIQGHHAIVEVLLDHDATlSQTFGPSNATPL--VSAAMRGHTEVVNqLLSK 220
Cdd:PHA02946  55 VEELLHrgYSPNET----DDDGNYPLHIASKINNNRIVAMLLTHGAD-PNACDKQHKTPLyyLSGTDDEVIERIN-LLVQ 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  221 AGNLLEISRSNNKNALHLAARQGHVEVIKALLSKDPQlARRIDKKGQTALH---MAVKGQSSEVVKLL-LDADPAivmQP 296
Cdd:PHA02946 129 YGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFE-ARIVDKFGKNHIHrhlMSDNPKASTISWMMkLGISPS---KP 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  297 DKSCNTALHVATRK--KRAEIVELLLSLPDTNANTLTRDHKTALDIAEGLPlseeSSYIKECLARSGALRANELNQPRDE 374
Cdd:PHA02946 205 DHDGNTPLHIVCSKtvKNVDIINLLLPSTDVNKQNKFGDSPLTLLIKTLSP----AHLINKLLSTSNVITDQTVNICIFY 280

                        250
                 ....*....|....*....
gi 15230470  375 LRSTVTQIKNDVHIQLEQT 393
Cdd:PHA02946 281 DRDDVLEIINDKGKQYDST 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
268-320 4.42e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 4.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15230470   268 TALHMAVKGQSSEVVKLLLDADPAIVMQpDKSCNTALHVATRKKRAEIVELLL 320
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
164-218 6.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 6.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15230470   164 GYDPLHIAAIQGHHAIVEVLLDHDATLSQTFGpSNATPLVSAAMRGHTEVVNQLL 218
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 81-342 1.23e-04

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: 45.07  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470    81 AAQRGDLAAVQQILkdinsqmegilsgeefdaevAEIRASIVNEVNELGETALFTAADKGHLDVVKELLKYSSRESiakk 160
Cdd:TIGR00870  24 AAERGDLASVYRDL--------------------EEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRG---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   161 nRSGYDPLHIAAiQGHHAIVEVLLDHdatLSQTFGPSNATPLVSAAM-----RGHTevvnqllskagnlleisrsnnknA 235
Cdd:TIGR00870  80 -AVGDTLLHAIS-LEYVDAVEAILLH---LLAAFRKSGPLELANDQYtseftPGIT-----------------------A 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   236 LHLAARQGHVEVIKALLSKDPQLARR------IDKKGQTA-------LHMAVKGQSSEVVKLLLDaDPAIVMQPDKSCNT 302
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARacgdffVKSQGVDSfyhgespLNAAACLGSPSIVALLSE-DPADILTADSLGNT 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15230470   303 ALH--VATRKKRAEIVEL-------LLSLPDTNANT------LTRDHKTALDIAE 342
Cdd:TIGR00870 211 LLHllVMENEFKAEYEELscqmynfALSLLDKLRDSkeleviLNHQGLTPLKLAA 265
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 129-287 1.72e-04

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: 44.69  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470   129 GETALFTAADKGHLDVVKELLKYSSRESIAKKNRSGYDPLHIAAIQGHHAIVEVLLdhdatLSQTFGPSNATPLVSAAMR 208
Cdd:TIGR00870  17 EEKAFLPAAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELL-----LNLSCRGAVGDTLLHAISL 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230470   209 GHTEVVNQLLskagnlleisrsnnknaLHLAARQGhvEVIKALLSKDPQLARriDKKGQTALHMAVKGQSSEVVKLLLD 287
Cdd:TIGR00870  92 EYVDAVEAIL-----------------LHLLAAFR--KSGPLELANDQYTSE--FTPGITALHLAAHRQNYEIVKLLLE 149
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 237-351 2.66e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  237 HLAArQGHVEVIKALLS--KDPQLarrIDKKGQTALHMAVKGQSSEVVKLLLD--ADPAIVmqpDKSCNTALHVATRKKR 312
Cdd:PTZ00322  88 QLAA-SGDAVGARILLTggADPNC---RDYDGRTPLHIACANGHVQVVRVLLEfgADPTLL---DKDGKTPLELAEENGF 160

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15230470  313 AEIVELLLSLPDTNANTltrDHKTALDIAEGLPLSEESS 351
Cdd:PTZ00322 161 REVVQLLSRHSQCHFEL---GANAKPDSFTGKPPSLEDS 196
PHA02741 PHA02741
hypothetical protein; Provisional
 214-342 8.02e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 40.41  E-value: 8.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  214 VNQLLSKAGNLLEISRSNNKNALHLAARQGHVEVIKALL-----SKDPQLARRIDKKGQTALHMAV----KGQSSEVVKL 284
Cdd:PHA02741   3 SPHFMTCLEEMIAEKNSEGENFFHEAARCGCFDIIARFTpfirgDCHAAALNATDDAGQMCIHIAAekheAQLAAEIIDH 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230470  285 LLDADPAIVMQPDKSCNTALHVATRKKRAEIVELLLSLPDTNANTLTRDHKTALDIAE 342
Cdd:PHA02741  83 LIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAI 140
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 143-310 9.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  143 DVVKELLKYSSRESIAKKNRsGYDPLHIAAIQGHHAIVEVLLDHDATLSqTFGPSNATPLVSAAMRGHTEVVNQLLSKAG 222
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHK-GNTALHYATENKDQRLTELLLSYGANVN-IPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  223 NLLEISRSNNkNALHLA-ARQGHVEVIKALLSKDPQLARRIDKKGQTALHMAVKgqSSEVVKLLLD--ADPAIVmqpDKS 299
Cdd:PHA02878 226 STDARDKCGN-TPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIK--SERKLKLLLEygADINSL---NSY 299

                        170
                 ....*....|.
gi 15230470  300 CNTALHVATRK 310
Cdd:PHA02878 300 KLTPLSSAVKQ 310
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 164-191 1.26e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*...
gi 15230470   164 GYDPLHIAAIQGHHAIVEVLLDHDATLS 191
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 117-255 1.30e-03

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: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 117 IRASIVNEVNElGETALFTAADKGHLDVVKELL-KYSSRESIAK------KNRS-----GYDPLHIAAIQGHHAIVEVLL 184
Cdd:cd22194 130 INAEYTEEAYE-GQTALNIAIERRQGDIVKLLIaKGADVNAHAKgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLM 208

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470 185 DH---DATLSQTFGPSNATPLVSAA--MRGHTEVVNQLL------SKAGNLLEISRSNNKNALHLAARQGHVEVIKALLS 253
Cdd:cd22194 209 EKestDITSQDSRGNTVLHALVTVAedSKTQNDFVKRMYdmillkSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288


                ..
gi 15230470 254 KD 255
Cdd:cd22194 289 RE 290
Ank_5 pfam13857
Ankyrin repeats (many copies);
217-273 1.65e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230470   217 LLSKAGNLLEISRSNNKNALHLAARQGHVEVIKALLsKDPQLARRIDKKGQTALHMA 273
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 164-190 1.86e-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: 36.03  E-value: 1.86e-03
                           10        20
                   ....*....|....*....|....*..
gi 15230470    164 GYDPLHIAAIQGHHAIVEVLLDHDATL 190
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 231-256 2.29e-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: 35.64  E-value: 2.29e-03
                           10        20
                   ....*....|....*....|....*.
gi 15230470    231 NNKNALHLAARQGHVEVIKALLSKDP 256
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 236-286 2.73e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 2.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15230470  236 LHLAARQGHVEVIKALLS--KDPQLarrIDKKGQTALHMAVKGQSSEVVKLLL 286
Cdd:PTZ00322 119 LHIACANGHVQVVRVLLEfgADPTL---LDKDGKTPLELAEENGFREVVQLLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 167-362 4.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  167 PLHIAAIQGHHAIVEVLLDHDATLSQTfGPSNATPLVSAAMRGHTEVVNQLLSKagnLLEISRSNNKNALHLAARQGHVE 246
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQP-DHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVFYTLVAIKDAFNNRNVE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230470  247 VIKALLSKDPQLARRIDKKgQTALHMAVKGQSSEVVKLLLDADPAIVMQPDKSCNTALHVATRKKRAEIVELLLSLpDTN 326
Cdd:PHA02878 116 IFKIILTNRYKNIQTIDLV-YIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSY-GAN 193

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15230470  327 ANTLTRDHKTALDIAeglpLSEESSYIKECLARSGA 362
Cdd:PHA02878 194 VNIPDKTNNSPLHHA----VKHYNKPIVHILLENGA 225
 
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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