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Conserved domains on  [gi|21539623|ref|NP_081772|]
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ankyrin repeat domain-containing protein 33B isoform 2 [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];
85-260 1.51e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 1.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  85 LLRAACANDVGLLRALVRRGP------SSEETGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTIT 158
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAdvnardKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623 159 NYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVRVIQRLMERPC 238
Cdd:COG0666 170 KLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170       180
                ....*....|....*....|..
gi 21539623 239 PEQFGDKYKLELPLPAEAVLKK 260
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIV 268
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-260 1.51e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 1.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  85 LLRAACANDVGLLRALVRRGP------SSEETGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTIT 158
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAdvnardKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623 159 NYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVRVIQRLMERPC 238
Cdd:COG0666 170 KLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170       180
                ....*....|....*....|..
gi 21539623 239 PEQFGDKYKLELPLPAEAVLKK 260
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIV 268
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-207 5.76e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623   112 LIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYFPGldleRRNIFGFTALMKAAMQGRTE 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 21539623   192 CVRALMMAGADVQARD 207
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 82-216 2.54e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623   82 AATLLRAACANDVGLLRALVRR------GPSSEETGLIVACYHGFVDTVVALAE--CphvDVNWQDSEGNTALITAAQAG 153
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAkldpdiGDSKGRTPLHIAASKGYEDCVLVLLKhaC---NVHIRDANGNTALWNAISAK 602

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  154 HVTITNYLLNYFP-----------------------------GLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQ 204
Cdd:PLN03192 603 HHKIFRILYHFASisdphaagdllctaakrndltamkellkqGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682

                        170
                 ....*....|..
gi 21539623  205 ARDPRRGLSPQE 216
Cdd:PLN03192 683 KANTDDDFSPTE 694
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 85-207 6.29e-06

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: 48.86  E-value: 6.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  85 LLRAACANDVGLLRALVR--------RGPSSEeTGLIVACYHGFVDTVVALAECPHVDVNW----QDSEGNTALITAAQA 152
Cdd:cd22192  21 LLLAAKENDVQAIKKLLKcpscdlfqRGALGE-TALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21539623 153 GHVTITNYLLNYfpGLDLE---------RRNI-----FGFTALMKAAMQGRTECVRALMMAGADVQARD 207
Cdd:cd22192 100 QNLNLVRELIAR--GADVVspratgtffRPGPknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 177-203 2.30e-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: 2.30e-03
                           10        20
                   ....*....|....*....|....*..
gi 21539623    177 GFTALMKAAMQGRTECVRALMMAGADV 203
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-260 1.51e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 1.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  85 LLRAACANDVGLLRALVRRGP------SSEETGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTIT 158
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAdvnardKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623 159 NYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVRVIQRLMERPC 238
Cdd:COG0666 170 KLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170       180
                ....*....|....*....|..
gi 21539623 239 PEQFGDKYKLELPLPAEAVLKK 260
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-228 7.08e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 7.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  82 AATLLRAACANDVGLLRALVRRGP------SSEETGLIVACYHGFVDTVVALAECPhVDVNWQDSEGNTALITAAQAGHV 155
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAAGAdinakdDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNL 133

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21539623 156 TITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVR 228
Cdd:COG0666 134 EIVKLLLEA--GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVK 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-207 5.76e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623   112 LIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYFPGldleRRNIFGFTALMKAAMQGRTE 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 21539623   192 CVRALMMAGADVQARD 207
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-233 1.05e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 1.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  84 TLLRAACANDVGLLRALVRRGP------SSEETGLIVACYHGFVDTVVALAECpHVDVNWQDSEGNTALITAAQAGHVTI 157
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGAdvnaqdNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEI 201

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21539623 158 TNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVRVIQRL 233
Cdd:COG0666 202 VKLLLEA--GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD-KDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-228 1.48e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 1.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  82 AATLLRAACANDVGLLRALVRRGPSSEETGLIVACYHGFVDTVVALAECPHVDVNWQDSEGNTALITAAQAGHVTITNYL 161
Cdd:COG0666  27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21539623 162 LNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVR 228
Cdd:COG0666 107 LEA--GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVK 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 82-216 2.54e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623   82 AATLLRAACANDVGLLRALVRR------GPSSEETGLIVACYHGFVDTVVALAE--CphvDVNWQDSEGNTALITAAQAG 153
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAkldpdiGDSKGRTPLHIAASKGYEDCVLVLLKhaC---NVHIRDANGNTALWNAISAK 602

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  154 HVTITNYLLNYFP-----------------------------GLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQ 204
Cdd:PLN03192 603 HHKIFRILYHFASisdphaagdllctaakrndltamkellkqGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682

                        170
                 ....*....|..
gi 21539623  205 ARDPRRGLSPQE 216
Cdd:PLN03192 683 KANTDDDFSPTE 694
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 3.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 3.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21539623   127 LAECPHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTAL 181
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY--GVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-196 3.63e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 3.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21539623   142 GNTALITAAQAGHVTITNYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRAL 196
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
161-214 1.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 1.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21539623   161 LLNYFPgLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSP 214
Cdd:pfam13857   1 LLEHGP-IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTA 52
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 85-207 6.29e-06

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: 48.86  E-value: 6.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  85 LLRAACANDVGLLRALVR--------RGPSSEeTGLIVACYHGFVDTVVALAECPHVDVNW----QDSEGNTALITAAQA 152
Cdd:cd22192  21 LLLAAKENDVQAIKKLLKcpscdlfqRGALGE-TALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21539623 153 GHVTITNYLLNYfpGLDLE---------RRNI-----FGFTALMKAAMQGRTECVRALMMAGADVQARD 207
Cdd:cd22192 100 QNLNLVRELIAR--GADVVspratgtffRPGPknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-162 1.93e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 1.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21539623   112 LIVACYHGFVDTVVALAEcPHVDVNWQDSEGNTALITAAQAGHVTITNYLL 162
Cdd:pfam13637   5 LHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
181-228 6.48e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 6.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 21539623   181 LMKAAMQGRTECVRALMMAGADVQARDPrRGLSPQEWAAYTGRAEAVR 228
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVK 47
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-230 9.81e-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: 45.00  E-value: 9.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623 109 ETGLIVACYHGFVDTVVALAECPHVDVNWQDSEGNTALITAAQAGHVTITNYLLNYFPGL-------DLERrnifGFTAL 181
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtsDLYQ----GETAL 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21539623 182 MKAAMQGRTECVRALMMAGADVQ-AR------DPRR------GLSPQEWAAYTGRAEAVRVI 230
Cdd:cd22192  94 HIAVVNQNLNLVRELIARGADVVsPRatgtffRPGPknliyyGEHPLSFAACVGNEEIVRLL 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 177-207 1.43e-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: 1.43e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 21539623   177 GFTALMKAAMQ-GRTECVRALMMAGADVQARD 207
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 133-208 2.79e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 2.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21539623  133 VDVNWQDSEGNTALITAAQAG---HVTITNYLLNyfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDP 208
Cdd:PHA03095 213 CDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA---GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
PHA03095 PHA03095
ankyrin-like protein; Provisional
 84-228 1.04e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623   84 TLLRAACAN---DVGLLRALVRRGPSSEETGLI----VACYHGFVDTVVAL------AECphvDVNWQDSEGNTALitaa 150
Cdd:PHA03095 119 TPLHVYLSGfniNPKVIRLLLRKGADVNALDLYgmtpLAVLLKSRNANVELlrllidAGA---DVYAVDDRFRSLL---- 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21539623  151 qaghvtitNYLLNYF------------PGLDLERRNIFGFTALMKAAMQGRteCVRALM----MAGADVQARDpRRGLSP 214
Cdd:PHA03095 192 --------HHHLQSFkprarivrelirAGCDPAATDMLGNTPLHSMATGSS--CKRSLVlpllIAGISINARN-RYGQTP 260

                        170
                 ....*....|....
gi 21539623  215 QEWAAYTGRAEAVR 228
Cdd:PHA03095 261 LHYAAVFNNPRACR 274
Ank_4 pfam13637
Ankyrin repeats (many copies);
179-228 1.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 21539623   179 TALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYTGRAEAVR 228
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLK 51
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 177-203 2.30e-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: 2.30e-03
                           10        20
                   ....*....|....*....|....*..
gi 21539623    177 GFTALMKAAMQGRTECVRALMMAGADV 203
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 159-221 4.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 4.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21539623  159 NYLLNYfpGLDLERRNIFGFTALMKAAMQGRTECVRALMMAGADVQARDpRRGLSPQEWAAYT 221
Cdd:PHA03100 176 NYLLSY--GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILN 235
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-205 7.22e-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: 7.22e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 21539623   176 FGFTALMKAAMQGRTECVRALMMAGADVQA 205
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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