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Conserved domains on  [gi|1443089275|ref|XP_015645737|]
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ankyrin repeat-containing protein At5g02620 [Oryza sativa Japonica Group]

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 ...
 500-606 5.16e-24

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: 97.24  E-value: 5.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 500 TSTGTVASVLIATVTFAAALTVPGGYVADD-HPNAGTAASAGRFAFRAFAVSDTMAFLCSIVGTCLLVVGEAREVRPSRG 578
Cdd:pfam13962   8 RNTLLLVATLIATVTFAAGFTPPGGYWQDDdGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFLRSLPR 87

                          90       100
                  ....*....|....*....|....*...
gi 1443089275 579 RLRAyqgSAWALVTAGAqFMVAAFAFGL 606
Cdd:pfam13962  88 KLRI---GLKLLWVALL-SMLVAFAAGS 111
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
206-464 8.81e-20

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 8.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 206 LMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPASAAGPDGRTALHSAATTSKEIAREILDwkpEGR 285
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL---AAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 286 TLLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVELIQKCPNNynDLVDDR 365
Cdd:COG0666    78 ADINAKDDGGNTLLHAAARN--GDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDND 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 366 GRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYR 445
Cdd:COG0666   153 GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAE 228

                         250
                  ....*....|....*....
gi 1443089275 446 HLQPGLHYFLNPRAVVKNL 464
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNA 247
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-325 1.56e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275  76 GHSLSQVAIRVDDDDDGRAPAGASRLLGVTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGH 155
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 156 RDVAACLLsemlrAGGAASAalplrrATNCLGATALHEAVRNGHAGVVALLMaEAPELASVANDGGVSPLYLAATVGSVD 235
Cdd:COG0666   133 LEIVKLLL-----EAGADVN------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 236 IVRALLhplpdgtpspasAAGPD-------GRTALHSAAttsKEIAREILDWKPEGRTLLTKADSSGRTPLHFAISSQIE 308
Cdd:COG0666   201 IVKLLL------------EAGADvnakdndGKTALDLAA---ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                         250
                  ....*....|....*..
gi 1443089275 309 RFDVFQLFLDAEPSLAL 325
Cdd:COG0666   266 LIVKLLLLALLLLAAAL 282
 
Name Accession Description Interval E-value
PGG pfam13962
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ...
 500-606 5.16e-24

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: 97.24  E-value: 5.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 500 TSTGTVASVLIATVTFAAALTVPGGYVADD-HPNAGTAASAGRFAFRAFAVSDTMAFLCSIVGTCLLVVGEAREVRPSRG 578
Cdd:pfam13962   8 RNTLLLVATLIATVTFAAGFTPPGGYWQDDdGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFLRSLPR 87

                          90       100
                  ....*....|....*....|....*...
gi 1443089275 579 RLRAyqgSAWALVTAGAqFMVAAFAFGL 606
Cdd:pfam13962  88 KLRI---GLKLLWVALL-SMLVAFAAGS 111
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
206-464 8.81e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 8.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 206 LMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPASAAGPDGRTALHSAATTSKEIAREILDwkpEGR 285
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL---AAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 286 TLLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVELIQKCPNNynDLVDDR 365
Cdd:COG0666    78 ADINAKDDGGNTLLHAAARN--GDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDND 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 366 GRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYR 445
Cdd:COG0666   153 GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAE 228

                         250
                  ....*....|....*....
gi 1443089275 446 HLQPGLHYFLNPRAVVKNL 464
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNA 247
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-325 1.56e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275  76 GHSLSQVAIRVDDDDDGRAPAGASRLLGVTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGH 155
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 156 RDVAACLLsemlrAGGAASAalplrrATNCLGATALHEAVRNGHAGVVALLMaEAPELASVANDGGVSPLYLAATVGSVD 235
Cdd:COG0666   133 LEIVKLLL-----EAGADVN------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 236 IVRALLhplpdgtpspasAAGPD-------GRTALHSAAttsKEIAREILDWKPEGRTLLTKADSSGRTPLHFAISSQIE 308
Cdd:COG0666   201 IVKLLL------------EAGADvnakdndGKTALDLAA---ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                         250
                  ....*....|....*..
gi 1443089275 309 RFDVFQLFLDAEPSLAL 325
Cdd:COG0666   266 LIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
335-423 4.25e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 335 LHVAAVMGSVRIVVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRDDRFGilmnaMDNEGNTPLHLAAEYGH 414
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGH 73


                  ....*....
gi 1443089275 415 PRMVSLLLE 423
Cdd:pfam12796  74 LEIVKLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 179-488 3.27e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 179 LRRATNCLG------ATALHEAVRNGHAGVVALLMAEAPELASVaNDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPA 252
Cdd:PHA02874   21 IKNKGNCINisvdetTTPLIDAIRSGDAKIVELFIKHGADINHI-NTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 253 saagPDgrtalhsaatTSKEIAREILDwkpEGRTLLTKaDSSGRTPLHFAISSQieRFDVFQLFLDAEPSLAlVCDIQGS 332
Cdd:PHA02874  100 ----PC----------IEKDMIKTILD---CGIDVNIK-DAELKTFLHYAIKKG--DLESIKMLFEYGADVN-IEDDNGC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 333 FPLHVAAVMGSVRIVVELIQKcpNNYNDLVDDRGRNFLHCAVEHNKESIVRYICrdDRFGILMNAMDNeGNTPLHLAAEY 412
Cdd:PHA02874  159 YPIHIAIKHNFFDIIKLLLEK--GAYANVKDNNGESPLHNAAEYGDYACIKLLI--DHGNHIMNKCKN-GFTPLHNAIIH 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443089275 413 GHpRMVSLLLETMSVDVaiTNRDGLTAadlayrhlqpgLHYFLNP---RAVVKNLFYcTRAPVTLEGDHARTGIPSAME 488
Cdd:PHA02874  234 NR-SAIELLINNASIND--QDIDGSTP-----------LHHAINPpcdIDIIDILLY-HKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-246 6.30e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 147 LHCAAKSGHRDVAACLLSEMLRAGgaasaalplrrATNCLGATALHEAVRNGHAGVVALLMAEApelASVANDGGVSPLY 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN-----------LQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALH 66

                          90       100
                  ....*....|....*....|
gi 1443089275 227 LAATVGSVDIVRALLHPLPD 246
Cdd:pfam12796  67 YAARSGHLEIVKLLLEKGAD 86
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 141-353 4.33e-09

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: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 141 RFLDTPLHCAAKSGhrDVAAclLSEMLRAggaaSAALPLRRATncLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 220
Cdd:cd22192    15 RISESPLLLAAKEN--DVQA--IKKLLKC----PSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 221 ----GVSPLYLAATVGSVDIVRALLHPLPD-GTPSPASAAGPDGRTAL-----H----SAATTSKEIAREILDwkpegRT 286
Cdd:cd22192    85 dlyqGETALHIAVVNQNLNLVRELIARGADvVSPRATGTFFRPGPKNLiyygeHplsfAACVGNEEIVRLLIE-----HG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 287 LLTKA-DSSGRTPLHFAISSQIERF--DVFQLFLDAEP-----SLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 353
Cdd:cd22192   160 ADIRAqDSLGNTVLHILVLQPNKTFacQMYDLILSYDKeddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA03095 PHA03095
ankyrin-like protein; Provisional
 109-218 1.86e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 109 GNTALHVAATRGHAALAALVcataPALAA-----TRNRFLDTPLHCAAKSGHRDVAACLlsemLRAGGAASAalplrrAT 183
Cdd:PHA03095  222 GNTPLHSMATGSSCKRSLVL----PLLIAgisinARNRYGQTPLHYAAVFNNPRACRRL----IALGADINA------VS 287

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1443089275 184 NClGATALHEAVRNGHAGVVALLMAEAPELASVAN 218
Cdd:PHA03095  288 SD-GNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 401-423 6.86e-04

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: 37.57  E-value: 6.86e-04
                           10        20
                   ....*....|....*....|...
gi 1443089275  401 EGNTPLHLAAEYGHPRMVSLLLE 423
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
 
Name Accession Description Interval E-value
PGG pfam13962
Domain of unknown function; The PGG domain is named for the highly conserved sequence motif ...
 500-606 5.16e-24

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: 97.24  E-value: 5.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 500 TSTGTVASVLIATVTFAAALTVPGGYVADD-HPNAGTAASAGRFAFRAFAVSDTMAFLCSIVGTCLLVVGEAREVRPSRG 578
Cdd:pfam13962   8 RNTLLLVATLIATVTFAAGFTPPGGYWQDDdGPHAGKPILAKNPAFKAFVISNAIAFFASLVAVVLLLSIVSDFLRSLPR 87

                          90       100
                  ....*....|....*....|....*...
gi 1443089275 579 RLRAyqgSAWALVTAGAqFMVAAFAFGL 606
Cdd:pfam13962  88 KLRI---GLKLLWVALL-SMLVAFAAGS 111
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
206-464 8.81e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 8.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 206 LMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPASAAGPDGRTALHSAATTSKEIAREILDwkpEGR 285
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL---AAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 286 TLLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVELIQKCPNNynDLVDDR 365
Cdd:COG0666    78 ADINAKDDGGNTLLHAAARN--GDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDND 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 366 GRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYR 445
Cdd:COG0666   153 GNTPLHLAAANGNLEIVKLLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAE 228

                         250
                  ....*....|....*....
gi 1443089275 446 HLQPGLHYFLNPRAVVKNL 464
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNA 247
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
188-464 5.19e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 5.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 188 ATALHEAVRNGHAGVVALLMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLHPLPDgtpspASAAGPDGRTALHSAA 267
Cdd:COG0666    21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-----INAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 268 TT-SKEIAREILDWKPEgrtlLTKADSSGRTPLHFAISSqiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRI 346
Cdd:COG0666    96 RNgDLEIVKLLLEAGAD----VNARDKDGETPLHLAAYN--GNLEIVKLLLEAGADVNAQ-DNDGNTPLHLAAANGNLEI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 347 VVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMS 426
Cdd:COG0666   169 VKLLLEAGADV--NARDNDGETPLHLAAENGHLEIVKLLLE---AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1443089275 427 vDVAITNRDGLTAADLAYRHLQPGLHYFLNPRAVVKNL 464
Cdd:COG0666   244 -DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-439 7.71e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 7.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 108 NGNTALHVAATRGHAALAALVCATAPALAATRNRFLDTPLHCAAKSGHRDVAACLLsemlraggaasAALPLRRATNCLG 187
Cdd:COG0666    19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL-----------AAGADINAKDDGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 188 ATALHEAVRNGHAGVVALLMAEAPELASVANDGGvSPLYLAATVGSVDIVRALLhplpdgtpspasAAGPDgrtalhsaa 267
Cdd:COG0666    88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLL------------EAGAD--------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 268 ttskeiareildwkpegrtlLTKADSSGRTPLHFAISSQieRFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIV 347
Cdd:COG0666   146 --------------------VNAQDNDGNTPLHLAAANG--NLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIV 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 348 VELIQKCPNnyNDLVDDRGRNFLHCAVEHNKESIVRYIcrdDRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMSV 427
Cdd:COG0666   203 KLLLEAGAD--VNAKDNDGKTALDLAAENGNLEIVKLL---LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277

                         330
                  ....*....|..
gi 1443089275 428 DVAITNRDGLTA 439
Cdd:COG0666   278 LAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-325 1.56e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275  76 GHSLSQVAIRVDDDDDGRAPAGASRLLGVTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGH 155
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 156 RDVAACLLsemlrAGGAASAalplrrATNCLGATALHEAVRNGHAGVVALLMaEAPELASVANDGGVSPLYLAATVGSVD 235
Cdd:COG0666   133 LEIVKLLL-----EAGADVN------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 236 IVRALLhplpdgtpspasAAGPD-------GRTALHSAAttsKEIAREILDWKPEGRTLLTKADSSGRTPLHFAISSQIE 308
Cdd:COG0666   201 IVKLLL------------EAGADvnakdndGKTALDLAA---ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                         250
                  ....*....|....*..
gi 1443089275 309 RFDVFQLFLDAEPSLAL 325
Cdd:COG0666   266 LIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
335-423 4.25e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 335 LHVAAVMGSVRIVVELIQKCPNNynDLVDDRGRNFLHCAVEHNKESIVRYICRDDRFGilmnaMDNEGNTPLHLAAEYGH 414
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGH 73


                  ....*....
gi 1443089275 415 PRMVSLLLE 423
Cdd:pfam12796  74 LEIVKLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 179-488 3.27e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 179 LRRATNCLG------ATALHEAVRNGHAGVVALLMAEAPELASVaNDGGVSPLYLAATVGSVDIVRALLHPLPDGTPSPA 252
Cdd:PHA02874   21 IKNKGNCINisvdetTTPLIDAIRSGDAKIVELFIKHGADINHI-NTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 253 saagPDgrtalhsaatTSKEIAREILDwkpEGRTLLTKaDSSGRTPLHFAISSQieRFDVFQLFLDAEPSLAlVCDIQGS 332
Cdd:PHA02874  100 ----PC----------IEKDMIKTILD---CGIDVNIK-DAELKTFLHYAIKKG--DLESIKMLFEYGADVN-IEDDNGC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 333 FPLHVAAVMGSVRIVVELIQKcpNNYNDLVDDRGRNFLHCAVEHNKESIVRYICrdDRFGILMNAMDNeGNTPLHLAAEY 412
Cdd:PHA02874  159 YPIHIAIKHNFFDIIKLLLEK--GAYANVKDNNGESPLHNAAEYGDYACIKLLI--DHGNHIMNKCKN-GFTPLHNAIIH 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443089275 413 GHpRMVSLLLETMSVDVaiTNRDGLTAadlayrhlqpgLHYFLNP---RAVVKNLFYcTRAPVTLEGDHARTGIPSAME 488
Cdd:PHA02874  234 NR-SAIELLINNASIND--QDIDGSTP-----------LHHAINPpcdIDIIDILLY-HKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-246 6.30e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 147 LHCAAKSGHRDVAACLLSEMLRAGgaasaalplrrATNCLGATALHEAVRNGHAGVVALLMAEApelASVANDGGVSPLY 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN-----------LQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALH 66

                          90       100
                  ....*....|....*....|
gi 1443089275 227 LAATVGSVDIVRALLHPLPD 246
Cdd:pfam12796  67 YAARSGHLEIVKLLLEKGAD 86
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 141-353 4.33e-09

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: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 141 RFLDTPLHCAAKSGhrDVAAclLSEMLRAggaaSAALPLRRATncLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 220
Cdd:cd22192    15 RISESPLLLAAKEN--DVQA--IKKLLKC----PSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 221 ----GVSPLYLAATVGSVDIVRALLHPLPD-GTPSPASAAGPDGRTAL-----H----SAATTSKEIAREILDwkpegRT 286
Cdd:cd22192    85 dlyqGETALHIAVVNQNLNLVRELIARGADvVSPRATGTFFRPGPKNLiyygeHplsfAACVGNEEIVRLLIE-----HG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 287 LLTKA-DSSGRTPLHFAISSQIERF--DVFQLFLDAEP-----SLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 353
Cdd:cd22192   160 ADIRAqDSLGNTVLHILVLQPNKTFacQMYDLILSYDKeddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
370-443 6.11e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 6.11e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443089275 370 LHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLETMSVDVaitNRDGLTAADLA 443
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYA 68
Ank_2 pfam12796
Ankyrin repeats (3 copies);
113-213 6.74e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 6.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 113 LHVAATRGHAALA-ALVcaTAPALAATRNRFLDTPLHCAAKSGHRDVAACLLSEMlraggaasaalplRRATNCLGATAL 191
Cdd:pfam12796   1 LHLAAKNGNLELVkLLL--ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-------------DVNLKDNGRTAL 65

                          90       100
                  ....*....|....*....|..
gi 1443089275 192 HEAVRNGHAGVVALLMAEAPEL 213
Cdd:pfam12796  66 HYAARSGHLEIVKLLLEKGADI 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-318 7.43e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 225 LYLAATVGSVDIVRALLHPLPDgtpspASAAGPDGRTALHSAATT-SKEIAREILDwkpegrTLLTKADSSGRTPLHFAI 303
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-----ANLQDKNGRTALHLAAKNgHLEIVKLLLE------HADVNLKDNGRTALHYAA 69

                          90
                  ....*....|....*
gi 1443089275 304 SSQieRFDVFQLFLD 318
Cdd:pfam12796  70 RSG--HLEIVKLLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
 200-446 8.20e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 8.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 200 AGVVALLMAEApelASVANDG--GVSPL--YLAATVG-SVDIVRALLhplpdgtpspasAAGPD-------GRTALHSAA 267
Cdd:PHA03095   27 VEEVRRLLAAG---ADVNFRGeyGKTPLhlYLHYSSEkVKDIVRLLL------------EAGADvnapercGFTPLHLYL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 268 TTSKEIarEILDwkpegrtLLTKA-------DSSGRTPLHFAISSQIERFDVFQLFLDAEPSLAlVCDIQGSFPLHVaaV 340
Cdd:PHA03095   92 YNATTL--DVIK-------LLIKAgadvnakDKVGRTPLHVYLSGFNINPKVIRLLLRKGADVN-ALDLYGMTPLAV--L 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 341 MGSVRIVVE----LIQKCPNNYNdlVDDRGRNFLH--CAVEHNKESIVRYICR-------DDRF---------------- 391
Cdd:PHA03095  160 LKSRNANVEllrlLIDAGADVYA--VDDRFRSLLHhhLQSFKPRARIVRELIRagcdpaaTDMLgntplhsmatgssckr 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443089275 392 ---------GILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLAYRH 446
Cdd:PHA03095  238 slvlplliaGISINARNRYGQTPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRN 300
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 326-438 1.66e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 326 VCDIQGSFPLHVAAV--MGSVRIVVELIQkcpNNYN-DLVDDRGRNFLHCAVE--HNKESIVRY----------ICRDDR 390
Cdd:PHA03100  101 APDNNGITPLLYAISkkSNSYSIVEYLLD---NGANvNIKNSDGENLLHLYLEsnKIDLKILKLlidkgvdinaKNRVNY 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1443089275 391 F---GILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLT 438
Cdd:PHA03100  178 LlsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD-LGANPNLVNKYGDT 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
299-386 2.72e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 299 LHFAISSqiERFDVFQLFLDAEPSlALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPNNyndlVDDRGRNFLHCAVEHNK 378
Cdd:pfam12796   1 LHLAAKN--GNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN----LKDNGRTALHYAARSGH 73


                  ....*...
gi 1443089275 379 ESIVRYIC 386
Cdd:pfam12796  74 LEIVKLLL 81
PHA03095 PHA03095
ankyrin-like protein; Provisional
 142-424 3.21e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 142 FLDTPLHCAAKSGHRDVAACLLSeMLRAGGAASAAlplrraTNClGATALHEAVRNGH-AGVVALLMAEAPELaSVANDG 220
Cdd:PHA03095   46 YGKTPLHLYLHYSSEKVKDIVRL-LLEAGADVNAP------ERC-GFTPLHLYLYNATtLDVIKLLIKAGADV-NAKDKV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 221 GVSPLYLAATVGSVD--IVRALLHPLPDgtpspASAAGPDGRTALHsAATTSKEIAREILdwkpegRTLLTK------AD 292
Cdd:PHA03095  117 GRTPLHVYLSGFNINpkVIRLLLRKGAD-----VNALDLYGMTPLA-VLLKSRNANVELL------RLLIDAgadvyaVD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 293 SSGRTPLH-FAISSQiERFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVR--IVVELIQKcpNNYNDLVDDRGRNF 369
Cdd:PHA03095  185 DRFRSLLHhHLQSFK-PRARIVRELIRAGCDPAAT-DMLGNTPLHSMATGSSCKrsLVLPLLIA--GISINARNRYGQTP 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 370 LHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLET 424
Cdd:PHA03095  261 LHYAAVFNNPRACRRLIA---LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_5 pfam13857
Ankyrin repeats (many copies);
389-443 3.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 3.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 389 DRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLA 443
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 222-423 3.65e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 222 VSPLYLAATVGSVDIVRALLHplpDGTPSPASAAgpDGRTALHSAA------TTSKEIAREILdwkpEGRTLLTKADSSG 295
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLD---NGADINSSTK--NNSTPLHYLSnikynlTDVKEIVKLLL----EYGANVNAPDNNG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 296 RTPLHFAISSQIERFDVFQLFLDAEPSLALVCDIQGSfPLHVAAVMGSVRI-VVELIQKcpNNYN--------------- 359
Cdd:PHA03100  107 ITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGEN-LLHLYLESNKIDLkILKLLID--KGVDinaknrvnyllsygv 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443089275 360 --DLVDDRGRNFLHCAVEHNKESIVRYICRddrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLE 423
Cdd:PHA03100  184 piNIKDVYGFTPLHYAVYNNNPEFVKYLLD---LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-164 8.78e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 8.78e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443089275 103 GVTTGNGNTALHVAATRGHAALAALVCATAPALAATRNRfldTPLHCAAKSGHRDVAACLLS 164
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIVKLLLE 82
Ank_4 pfam13637
Ankyrin repeats (many copies);
366-422 2.10e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1443089275 366 GRNFLHCAVEHNKESIVRYiCRDdrFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLL 422
Cdd:pfam13637   1 ELTALHAAAASGHLELLRL-LLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 259-423 1.31e-05

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: 48.60  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 259 GRTALHSA----ATTSKEIAREILDWKPEGRTL-------LTKADSSGRTPLHFAIssqiER--FDVFQLFLDA------ 319
Cdd:cd22194    94 GKTCLMKAllniNENTKEIVRILLAFAEENGILdrfinaeYTEEAYEGQTALNIAI----ERrqGDIVKLLIAKgadvna 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 320 -------EPSLALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPNNYNdLVDDRGRNFLHCAV------EHNKESIVRY-- 384
Cdd:cd22194   170 hakgvffNPKYKHEGFYFGETPLALAACTNQPEIVQLLMEKESTDIT-SQDSRGNTVLHALVtvaedsKTQNDFVKRMyd 248

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1443089275 385 -ICRDDRFGILMNAMDNEGNTPLHLAAEYGHPRMVSLLLE 423
Cdd:cd22194   249 mILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 297-443 2.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 297 TPLHFAIssQIERFDVFQLFLDAEPSLALVCDIQGSFPLHVAAVMGSVR-IVVELIQKCP------------NNY----- 358
Cdd:PHA02876   43 TAIHQAL--QLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICIIPNVMdIVISLTLDCDiildikyasiilNKHkldea 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 359 -----------NDLVDDRgrnfLHCAVEHNKeSIVRYICRDD--------RFGILMNAMDNEGNTPLHLAAEYGHPRMVS 419
Cdd:PHA02876  121 cihilkeaisgNDIHYDK----INESIEYMK-LIKERIQQDElliaemllEGGADVNAKDIYCITPIHYAAERGNAKMVN 195

                         170       180
                  ....*....|....*....|....
gi 1443089275 420 LLLeTMSVDVAITNRDGLTAADLA 443
Cdd:PHA02876  196 LLL-SYGADVNIIALDDLSVLECA 218
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 396-490 3.28e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 396 NAMDNEGNTPLHLAAEYGHPRMVSLLLEtMSVDVAITNRDGLTAADLAYRHlqpglhyflNPRAVVKNLFYCTRAPVTLE 475
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLE-FGADPTLLDKDGKTPLELAEEN---------GFREVVQLLSRHSQCHFELG 178

                          90
                  ....*....|....*...
gi 1443089275 476 GDHAR---TGIPSAMEDA 490
Cdd:PTZ00322  179 ANAKPdsfTGKPPSLEDS 196
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
104-220 4.80e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.72  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 104 VTTGNGNTALHVAATRGHAALAALVCAtAPALAATRNRFLDTPLHCAAKSGHRDVAACLLsemlraggaasAALPLRRAT 183
Cdd:COG0666   181 ARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLL-----------EAGADLNAK 248

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1443089275 184 NCLGATALHEAVRNGHAGVVALLMAEAPELASVANDG 220
Cdd:COG0666   249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 223-443 1.55e-04

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: 45.00  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 223 SPLYLAATVGSVDIVRALLhplpdGTPS-PASAAGPDGRTALHSAATTSK-EIAREILDWKPEgrtLLTKADSSgrtplh 300
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-----KCPScDLFQRGALGETALHVAALYDNlEAAVVLMEAAPE---LVNEPMTS------ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 301 faissqierfdvfQLFldaepslalvcdiQGSFPLHVAAVMGSVRIVVELIQKCPnnynDLVDDR--------------- 365
Cdd:cd22192    85 -------------DLY-------------QGETALHIAVVNQNLNLVRELIARGA----DVVSPRatgtffrpgpknliy 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 366 -GRNFLHCAVEHNKESIVRYICRDdrfGILMNAMDNEGNTPLH---------LAAEyghprMVSLLL------ETMSVDV 429
Cdd:cd22192   135 yGEHPLSFAACVGNEEIVRLLIEH---GADIRAQDSLGNTVLHilvlqpnktFACQ-----MYDLILsydkedDLQPLDL 206

                         250
                  ....*....|....
gi 1443089275 430 aITNRDGLTAADLA 443
Cdd:cd22192   207 -VPNNQGLTPFKLA 219
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-163 1.86e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1443089275 109 GNTALHVAATRGH-AALAALVCATAPALAatRNRFLDTPLHCAAKSGHRDVAACLL 163
Cdd:pfam13637   1 ELTALHAAAASGHlELLRLLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 109-218 1.86e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 109 GNTALHVAATRGHAALAALVcataPALAA-----TRNRFLDTPLHCAAKSGHRDVAACLlsemLRAGGAASAalplrrAT 183
Cdd:PHA03095  222 GNTPLHSMATGSSCKRSLVL----PLLIAgisinARNRYGQTPLHYAAVFNNPRACRRL----IALGADINA------VS 287

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1443089275 184 NClGATALHEAVRNGHAGVVALLMAEAPELASVAN 218
Cdd:PHA03095  288 SD-GNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 145-353 3.18e-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: 44.10  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 145 TPLHCAAKSGHRDVAACLLSeMLRAGGAASAALPLRRATnCL-----GATALHEAVRNGHAGVVALLMAEAPELASVAND 219
Cdd:cd21882    28 TCLHKAALNLNDGVNEAIML-LLEAAPDSGNPKELVNAP-CTdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 220 G------------GVSPLYLAATVGSVDIVRALL-HPlpdgtPSPASAAGPD--GRTALHsaattskeIAREILDWKPEG 284
Cdd:cd21882   106 RffrkspgnlfyfGELPLSLAACTNQEEIVRLLLeNG-----AQPAALEAQDslGNTVLH--------ALVLQADNTPEN 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443089275 285 RTLLTKadssgrtpLHFAISSQIERFDVFQlfldaepSLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 353
Cdd:cd21882   173 SAFVCQ--------MYNLLLSYGAHLDPTQ-------QLEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
PHA02741 PHA02741
hypothetical protein; Provisional
 287-434 6.57e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 41.18  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 287 LLTKADSSGRTPLHFAISSQ----IERFDVFqLFLDAEPSLALVCDIQGSFPLHVAAVMGSVRIVVELIQKCPN-----N 357
Cdd:PHA02741   13 MIAEKNSEGENFFHEAARCGcfdiIARFTPF-IRGDCHAAALNATDDAGQMCIHIAAEKHEAQLAAEIIDHLIElgadiN 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443089275 358 YNDLVDdrGRNFLHCAVEHNKESIVRYICRDDRFGILMNAMDNEgnTPLHLAAEYGHPRMVSLLLETMSVDVAITNR 434
Cdd:PHA02741   92 AQEMLE--GDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNK--SPFELAIDNEDVAMMQILREIVATSRGFSNE 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 401-423 6.86e-04

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: 37.57  E-value: 6.86e-04
                           10        20
                   ....*....|....*....|...
gi 1443089275  401 EGNTPLHLAAEYGHPRMVSLLLE 423
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 401-434 7.23e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 7.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1443089275 401 EGNTPLHLAA-EYGHPRMVSLLLEtMSVDVAITNR 434
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLS-KGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 401-431 9.13e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 9.13e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1443089275 401 EGNTPLHLAAEYGHPRMVSLLLEtMSVDVAI 431
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLE-NGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 191-433 9.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 191 LHEAVRNGHAGVVALLMAEAPELASVANDGGVSPLYLAATVGSVDIVRALLhplpdgtpspASAAGPDgrtalhsAATTS 270
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLI----------ARGADPD-------IPNTD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 271 KEiareildwkpegrtlltkadssgrTPLHFAISSQieRFDVFQLFLDAEPSLALVcDIQGSFPLHVAAVMGSVRIVVEL 350
Cdd:PHA02875  135 KF------------------------SPLHLAVMMG--DIKGIELLIDHKACLDIE-DCCGCTPLIIAMAKGDIAICKML 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 351 IQKCPNnyNDLVDDRGRNFLHC-AVEHNKESIVRYICRDDRFGILMNAMDNEGNTPLHLAAEYghprmvSLLLETMSVDV 429
Cdd:PHA02875  188 LDSGAN--IDYFGKNGCVAALCyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTILDMICNM------CTNLESEAIDA 259


                  ....
gi 1443089275 430 AITN 433
Cdd:PHA02875  260 LIAD 263
Ank_4 pfam13637
Ankyrin repeats (many copies);
402-455 1.37e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1443089275 402 GNTPLHLAAEYGHPRMVSLLLETmSVDVAITNRDGLTAADLAYRHLQPG-LHYFL 455
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEvLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 330-445 1.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 330 QGSFPLHVAAVMGSVRIVVELIQKC--PNnyndlVDDRGRNF-LHCAVEHNKESIVRYICRDdrfGILMNAMDNEGNTPL 406
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGanVN-----IPDKTNNSpLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPL 238

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1443089275 407 HLAAEY-GHPRMVSLLLET-MSVDVAITNRdGLTAADLAYR 445
Cdd:PHA02878  239 HISVGYcKDYDILKLLLEHgVDVNAKSYIL-GLTALHSSIK 278
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 187-320 1.56e-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: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 187 GATALHEAVRNGHAGVVALLMAEAPELASVA----------NDG---GVSPLYLAATVGSVDIVRALLhplpDGTPSPAS 253
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLM----EKESTDIT 216

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443089275 254 AAGPDGRTALHSAATTS----------KEIAREILDwKPEGRTLLTKADSSGRTPLHFAisSQIERFDVFQLFLDAE 320
Cdd:cd22194   217 SQDSRGNTVLHALVTVAedsktqndfvKRMYDMILL-KSENKNLETIRNNEGLTPLQLA--AKMGKAEILKYILSRE 290
Ank_2 pfam12796
Ankyrin repeats (3 copies);
292-353 1.97e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 1.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443089275 292 DSSGRTPLHFAISSQieRFDVFQLFLDaepSLALVCDIQGSFPLHVAAVMGSVRIVVELIQK 353
Cdd:pfam12796  27 DKNGRTALHLAAKNG--HLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLEK 83
PHA02741 PHA02741
hypothetical protein; Provisional
 335-443 2.33e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443089275 335 LHVAAVMGSVRIVVELIQKCPNNYN----DLVDDRGRNFLH-CAVEHNKESIVRYICRDDRFGILMNAMDN-EGNTPLHL 408
Cdd:PHA02741   25 FHEAARCGCFDIIARFTPFIRGDCHaaalNATDDAGQMCIHiAAEKHEAQLAAEIIDHLIELGADINAQEMlEGDTALHL 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1443089275 409 AAEYGHPRMVSLLLETMSVDVAITNRDGLTAADLA 443
Cdd:PHA02741  105 AAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
334-384 9.36e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 9.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1443089275 334 PLHVAAVMGSVRIVVELIQKcPNNYNDlVDDRGRNFLHCAVEHNKESIVRY 384
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEK-GADINA-VDGNGETALHFAASNGNVEVLKL 52
 
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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