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Conserved domains on  [gi|256574786|ref|NP_001157913|]
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ankyrin repeat domain-containing protein 33B isoform 3 [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

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-269 2.57e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 2.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  85 LLRAACANDVGLLRALVRRGPSseeVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHV 164
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 165 TITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVRVIQRLME 244
Cdd:COG0666  167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGA 243

                        170       180
                 ....*....|....*....|....*
gi 256574786 245 RPCPEQFGDKYKLELPLPAEAVLKK 269
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIV 268
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-269 2.57e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 2.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  85 LLRAACANDVGLLRALVRRGPSseeVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHV 164
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 165 TITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVRVIQRLME 244
Cdd:COG0666  167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGA 243

                        170       180
                 ....*....|....*....|....*
gi 256574786 245 RPCPEQFGDKYKLELPLPAEAVLKK 269
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIV 268
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-216 5.98e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 5.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  121 LIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYFPGldleRRNIFGFTALMKAAMQGRTE 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 256574786  201 CVRALMMAGADVQARD 216
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 82-225 1.46e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  82 AATLLRAACANDVGLLRALVRRGPSSEEvreTDRNGRTGLIVACYHGFVDTVVALAE--CphvDVNWQDSEGNTALITAA 159
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKhaC---NVHIRDANGNTALWNAI 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 160 QAGHVTITNYLLNYFP-----------------------------GLDLERRNIFGFTALMKAAMQGRTECVRALMMAGA 210
Cdd:PLN03192 600 SAKHHKIFRILYHFASisdphaagdllctaakrndltamkellkqGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679

                        170
                 ....*....|....*
gi 256574786 211 DVQARDPRRGLSPQE 225
Cdd:PLN03192 680 DVDKANTDDDFSPTE 694
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 85-216 1.26e-05

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: 47.70  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  85 LLRAACANDVGLLRALVRRgpSSEEVRETDRNGRTGLIVACYHGFVDTVVALAECPHVDVNW----QDSEGNTALITAAQ 160
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKC--PSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 161 AGHVTITNYLLNYfpGLDLE---------RRNI-----FGFTALMKAAMQGRTECVRALMMAGADVQARD 216
Cdd:cd22192   99 NQNLNLVRELIAR--GADVVspratgtffRPGPknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 186-212 2.35e-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: 2.35e-03
                           10        20
                   ....*....|....*....|....*..
gi 256574786   186 GFTALMKAAMQGRTECVRALMMAGADV 212
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-269 2.57e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 2.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  85 LLRAACANDVGLLRALVRRGPSseeVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHV 164
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 165 TITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVRVIQRLME 244
Cdd:COG0666  167 EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGA 243

                        170       180
                 ....*....|....*....|....*
gi 256574786 245 RPCPEQFGDKYKLELPLPAEAVLKK 269
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-237 1.49e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.89  E-value: 1.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  82 AATLLRAACANDVGLLRALVRRGpssEEVRETDRNGRTGLIVACYHGFVDTVVALAECPhVDVNWQDSEGNTALITAAQA 161
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256574786 162 GHVTITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVR 237
Cdd:COG0666  131 GNLEIVKLLLEA--GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVK 203
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-242 2.45e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  84 TLLRAACANDVGLLRALVRRGPsseEVRETDRNGRTGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGH 163
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGA---DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGH 198

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256574786 164 VTITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVRVIQRL 242
Cdd:COG0666  199 LEIVKLLLEA--GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD-KDGLTALLLAAAAGAALIVKLLLLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-216 5.98e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 5.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  121 LIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYFPGldleRRNIFGFTALMKAAMQGRTE 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 256574786  201 CVRALMMAGADVQARD 216
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-237 2.55e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.31  E-value: 2.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 114 DRNGRTGLIVACYHGFVDTVVALAECPHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTALMKA 193
Cdd:COG0666   50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA--GADVNARDKDGETPLHLA 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 256574786 194 AMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVR 237
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVK 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-183 7.81e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 7.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786   85 LLRAACANDVGLLRALVRRGPsseEVRETDRNGRTGLIVACYHGFVDTVVALAECPHVDVnwqDSEGNTALITAAQAGHV 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA---DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHL 74

                          90
                  ....*....|....*....
gi 256574786  165 TITNYLLNYfpGLDLERRN 183
Cdd:pfam12796  75 EIVKLLLEK--GADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 82-225 1.46e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  82 AATLLRAACANDVGLLRALVRRGPSSEEvreTDRNGRTGLIVACYHGFVDTVVALAE--CphvDVNWQDSEGNTALITAA 159
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKhaC---NVHIRDANGNTALWNAI 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 160 QAGHVTITNYLLNYFP-----------------------------GLDLERRNIFGFTALMKAAMQGRTECVRALMMAGA 210
Cdd:PLN03192 600 SAKHHKIFRILYHFASisdphaagdllctaakrndltamkellkqGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679

                        170
                 ....*....|....*
gi 256574786 211 DVQARDPRRGLSPQE 225
Cdd:PLN03192 680 DVDKANTDDDFSPTE 694
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
133-237 8.62e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 8.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 133 VVALAECPHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADV 212
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA--GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                         90       100
                 ....*....|....*....|....*
gi 256574786 213 QARDpRRGLSPQEWAAYTGRAEAVR 237
Cdd:COG0666  114 NARD-KDGETPLHLAAYNGNLEIVK 137
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-190 3.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 3.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256574786  136 LAECPHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTAL 190
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-205 3.70e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 3.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256574786  151 GNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRAL 205
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-217 1.73e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  78 GVPEAATLLRAACANdVGLLRALVRRGpssEEVRETDRNGRTGLivacyHGFVDTVVALAEC------PHVDVNWQDSEG 151
Cdd:PHA03095 152 GMTPLAVLLKSRNAN-VELLRLLIDAG---ADVYAVDDRFRSLL-----HHHLQSFKPRARIvrelirAGCDPAATDMLG 222

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256574786 152 NTALITAAQAG---HVTITNYLLNyfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDP 217
Cdd:PHA03095 223 NTPLHSMATGSsckRSLVLPLLIA---GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
Ank_5 pfam13857
Ankyrin repeats (many copies);
170-223 1.98e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 1.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 256574786  170 LLNYFPgLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSP 223
Cdd:pfam13857   1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTA 52
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-171 7.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 7.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256574786  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 ...
 85-216 1.26e-05

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: 47.70  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  85 LLRAACANDVGLLRALVRRgpSSEEVRETDRNGRTGLIVACYHGFVDTVVALAECPHVDVNW----QDSEGNTALITAAQ 160
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKC--PSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 161 AGHVTITNYLLNYfpGLDLE---------RRNI-----FGFTALMKAAMQGRTECVRALMMAGADVQARD 216
Cdd:cd22192   99 NQNLNLVRELIAR--GADVVspratgtffRPGPknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
Ank_2 pfam12796
Ankyrin repeats (3 copies);
190-237 6.61e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 6.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 256574786  190 LMKAAMQGRTECVRALMMAGADVQARDPrRGLSPQEWAAYTGRAEAVR 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVK 47
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 186-216 1.46e-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: 38.81  E-value: 1.46e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 256574786  186 GFTALMKAAMQ-GRTECVRALMMAGADVQARD 216
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 121-239 2.40e-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: 43.46  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 121 LIVACYHGFVDTVVALAECPHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYFPGL-------DLERrnifGFTALMKA 193
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtsDLYQ----GETALHIA 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 256574786 194 AMQGRTECVRALMMAGADVQ-AR------DPRR------GLSPQEWAAYTGRAEAVRVI 239
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVsPRatgtffRPGPknliyyGEHPLSFAACVGNEEIVRLL 155
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-206 3.60e-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: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  72 AESVPEGVPEAAT---------LLRAACANDVGLLRALVRRGPSSEEVRETD---RNGRTGLivaCYHGfvDTVVALAEC 139
Cdd:cd22192   71 MEAAPELVNEPMTsdlyqgetaLHIAVVNQNLNLVRELIARGADVVSPRATGtffRPGPKNL---IYYG--EHPLSFAAC 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786 140 ------------PHVDVNWQDSEGNTAL-ITAAQAGHVTIT---NYLLNYFPGLDLER----RNIFGFTALMKAAMQGRT 199
Cdd:cd22192  146 vgneeivrllieHGADIRAQDSLGNTVLhILVLQPNKTFACqmyDLILSYDKEDDLQPldlvPNNQGLTPFKLAAKEGNI 225


                 ....*..
gi 256574786 200 ECVRALM 206
Cdd:cd22192  226 VMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
188-237 1.18e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 256574786  188 TALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVR 237
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLK 51
Ank_5 pfam13857
Ankyrin repeats (many copies);
100-158 1.46e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256574786  100 LVRRGPssEEVRETDRNGRTGLIVACYHGFVDTVVALAEcPHVDVNWQDSEGNTALITA 158
Cdd:pfam13857   1 LLEHGP--IDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 84-219 2.06e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256574786  84 TLLRAACANDVGLLRALVRRGPsseEVRETDRNGRTGLIVACYHGFVDTVVALAECPHVDVNWQDSEGNTALIT--AAQA 161
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGA---DVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFN 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256574786 162 GHVTITNYLLNYfpGLDLERRNIFGFTALmkAAMQGRTEC----VRALMMAGADVQARDPRR 219
Cdd:PHA03095 130 INPKVIRLLLRK--GADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVYAVDDRF 187
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 186-212 2.35e-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: 2.35e-03
                           10        20
                   ....*....|....*....|....*..
gi 256574786   186 GFTALMKAAMQGRTECVRALMMAGADV 212
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 168-230 4.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 4.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256574786 168 NYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYT 230
Cdd:PHA03100 176 NYLLSY--GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILN 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-136 5.83e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 5.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 256574786   84 TLLRAACANDVGLLRALVRRGPsseEVRETDRNGRTGLIVACYHGFVDTVVAL 136
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGA---DINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 185-214 7.35e-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: 34.16  E-value: 7.35e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 256574786  185 FGFTALMKAAMQGRTECVRALMMAGADVQA 214
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
 
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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