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Conserved domains on  [gi|1907113894|ref|XP_036015442|]
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ankyrin repeat domain-containing protein 33B isoform X1 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-205 1.29e-25

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  85 LLRAACANDVGLLRALVRRGPSseeVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHV 164
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907113894 165 TITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRAL 205
Cdd:COG0666   167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLL 205
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-205 1.29e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  85 LLRAACANDVGLLRALVRRGPSseeVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHV 164
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907113894 165 TITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRAL 205
Cdd:COG0666   167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-209 4.44e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 4.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894 121 LIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYFPGldleRRNIFGFTALMKAAMQGRTE 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLE 75


                  ....*....
gi 1907113894 201 CVRALMMAD 209
Cdd:pfam12796  76 IVKLLLEKG 84
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 82-207 6.64e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  82 AATLLRAACANDVGLLRALVRRGPSSEEvreTDRNGRTGLIVACYHGFVDTVVALAE--CphvDVNWQDSEGNTALITAA 159
Cdd:PLN03192  526 ASNLLTVASTGNAALLEELLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKhaC---NVHIRDANGNTALWNAI 599

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907113894 160 QAGHVTITNYLLNYFP-----------------------------GLDLERRNIFGFTALMKAAMQGRTECVRALMM 207
Cdd:PLN03192  600 SAKHHKIFRILYHFASisdphaagdllctaakrndltamkellkqGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-206 1.22e-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: 43.08  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  72 AESVPEGVPEAAT---------LLRAACANDVGLLRALVRRGPSSEEVRETD---RNGRTGLivaCYHGfvDTVVALAEC 139
Cdd:cd22192    71 MEAAPELVNEPMTsdlyqgetaLHIAVVNQNLNLVRELIARGADVVSPRATGtffRPGPKNL---IYYG--EHPLSFAAC 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894 140 ------------PHVDVNWQDSEGNTAL-ITAAQAGHVTIT---NYLLNYFPGLDLER----RNIFGFTALMKAAMQGRT 199
Cdd:cd22192   146 vgneeivrllieHGADIRAQDSLGNTVLhILVLQPNKTFACqmyDLILSYDKEDDLQPldlvPNNQGLTPFKLAAKEGNI 225


                  ....*..
gi 1907113894 200 ECVRALM 206
Cdd:cd22192   226 VMFQHLV 232
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-205 1.29e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  85 LLRAACANDVGLLRALVRRGPSseeVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHV 164
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907113894 165 TITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRAL 205
Cdd:COG0666   167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-205 2.83e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  84 TLLRAACANDVGLLRALVRRGPsseEVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGH 163
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGA---DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGH 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907113894 164 VTITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRAL 205
Cdd:COG0666   199 LEIVKLLLEA--GADVNAKDNDGKTALDLAAENGNLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-209 4.44e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 4.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894 121 LIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYFPGldleRRNIFGFTALMKAAMQGRTE 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLE 75


                  ....*....
gi 1907113894 201 CVRALMMAD 209
Cdd:pfam12796  76 IVKLLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-183 2.23e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  85 LLRAACANDVGLLRALVRRGPsseEVRETDRNGRTGLIVACYHGFVDTVVALAECPHVDVnwqDSEGNTALITAAQAGHV 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA---DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHL 74

                          90
                  ....*....|....*....
gi 1907113894 165 TITNYLLNYfpGLDLERRN 183
Cdd:pfam12796  75 EIVKLLLEK--GADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-206 1.25e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.52  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  85 LLRAACANDVGLLRALVRRGPsseEVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHV 164
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNL 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907113894 165 TITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALM 206
Cdd:COG0666   233 EIVKLLLEA--GADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-205 5.35e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894 114 DRNGRTGLIVACYHGFVDTVVALAECPHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTALMKA 193
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARDKDGETPLHLA 127

                          90
                  ....*....|..
gi 1907113894 194 AMQGRTECVRAL 205
Cdd:COG0666   128 AYNGNLEIVKLL 139
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 82-207 6.64e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  82 AATLLRAACANDVGLLRALVRRGPSSEEvreTDRNGRTGLIVACYHGFVDTVVALAE--CphvDVNWQDSEGNTALITAA 159
Cdd:PLN03192  526 ASNLLTVASTGNAALLEELLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKhaC---NVHIRDANGNTALWNAI 599

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907113894 160 QAGHVTITNYLLNYFP-----------------------------GLDLERRNIFGFTALMKAAMQGRTECVRALMM 207
Cdd:PLN03192  600 SAKHHKIFRILYHFASisdphaagdllctaakrndltamkellkqGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-205 1.91e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907113894 151 GNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRAL 205
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-190 2.95e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 2.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907113894 136 LAECPHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTAL 190
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-171 4.21e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 4.21e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907113894 117 GRTGLIVACYHGFVDTVVALAEcPHVDVNWQDSEGNTALITAAQAGHVTITNYLL 171
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-206 1.22e-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: 43.08  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  72 AESVPEGVPEAAT---------LLRAACANDVGLLRALVRRGPSSEEVRETD---RNGRTGLivaCYHGfvDTVVALAEC 139
Cdd:cd22192    71 MEAAPELVNEPMTsdlyqgetaLHIAVVNQNLNLVRELIARGADVVSPRATGtffRPGPKNL---IYYG--EHPLSFAAC 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894 140 ------------PHVDVNWQDSEGNTAL-ITAAQAGHVTIT---NYLLNYFPGLDLER----RNIFGFTALMKAAMQGRT 199
Cdd:cd22192   146 vgneeivrllieHGADIRAQDSLGNTVLhILVLQPNKTFACqmyDLILSYDKEDDLQPldlvPNNQGLTPFKLAAKEGNI 225


                  ....*..
gi 1907113894 200 ECVRALM 206
Cdd:cd22192   226 VMFQHLV 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-250 1.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  78 GVPEAATLLRAACANdVGLLRALVRRGpssEEVRETDRNGRTGLivacyHGFVDTVVALAEC------PHVDVNWQDSEG 151
Cdd:PHA03095  152 GMTPLAVLLKSRNAN-VELLRLLIDAG---ADVYAVDDRFRSLL-----HHHLQSFKPRARIvrelirAGCDPAATDMLG 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894 152 NTALITAAQAG---HVTITNYLLNyfpGLDLERRNIFGFTALMKAAMQGRTecvralmMAdglfgraqptLDRVLQRLAD 228
Cdd:PHA03095  223 NTPLHSMATGSsckRSLVLPLLIA---GISINARNRYGQTPLHYAAVFNNP-------RA----------CRRLIALGAD 282

                         170       180
                  ....*....|....*....|..
gi 1907113894 229 TSVRSEGNRSeilwdPGSFSIH 250
Cdd:PHA03095  283 INAVSSDGNT-----PLSLMVR 299
Ank_5 pfam13857
Ankyrin repeats (many copies);
100-158 1.25e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907113894 100 LVRRGPssEEVRETDRNGRTGLIVACYHGFVDTVVALAEcPHVDVNWQDSEGNTALITA 158
Cdd:pfam13857   1 LLEHGP--IDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-136 3.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 3.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907113894  84 TLLRAACANDVGLLRALVRRGPsseEVRETDRNGRTGLIVACYHGFVDTVVAL 136
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGA---DINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
170-207 3.61e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 3.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907113894 170 LLNYFPgLDLERRNIFGFTALMKAAMQGRTECVRALMM 207
Cdd:pfam13857   1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLA 37
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 85-219 9.60e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 37.30  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113894  85 LLRAACANDVGLLRALVRRgpSSEEVRETDRNGRTGLIVACYHGFVDTVVALAECPHVDVNW----QDSEGNTALITAAQ 160
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC--PSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907113894 161 AGHVTITNYLLNYfpGLDLE---------RRNI-----FGFTALMKAAMQGRTECVRaLMMADGLFGRAQPTL 219
Cdd:cd22192    99 NQNLNLVRELIAR--GADVVspratgtffRPGPknliyYGEHPLSFAACVGNEEIVR-LLIEHGADIRAQDSL 168
 
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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