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Conserved domains on  [gi|767968838|ref|XP_011543591|]
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mitochondrial disaggregase isoform X4 [Homo sapiens]

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];
132-321 1.19e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 132 SNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDdfssvyktakeqgi 211
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-------------- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 212 hsledggqdgasrhitNQWTSALEFRRWLGLPAGV--LITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGG 289
Cdd:COG0666  151 ----------------NDGNTPLHLAAANGNLEIVklLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAG 209

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767968838 290 ANPLQRNEMGHTPLDYARE---GEVMKLLRTSEAK 321
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAEngnLEIVKLLLEAGAD 244
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-321 1.19e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 132 SNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDdfssvyktakeqgi 211
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-------------- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 212 hsledggqdgasrhitNQWTSALEFRRWLGLPAGV--LITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGG 289
Cdd:COG0666  151 ----------------NDGNTPLHLAAANGNLEIVklLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAG 209

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767968838 290 ANPLQRNEMGHTPLDYARE---GEVMKLLRTSEAK 321
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAEngnLEIVKLLLEAGAD 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-197 2.30e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838  111 AGLGMCALAAALVVHCYSKSPSNKDA--ALLEAARANNMQEVSRLLSEgADVNAKHRlGWTALMVAAINRNNSVVQVLLA 188
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGrtALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 767968838  189 AGADPNLGD 197
Cdd:pfam12796  83 KGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 145-315 1.36e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 145 NNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSV--VQVLLAAGADPNLgddfssvyKTAKeqGIHSLEDggqdgA 222
Cdd:PHA03100  84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNI--------KNSD--GENLLHL-----Y 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 223 SRHITNQwTSALEFrrwlglpagvLITREDDFN--NRLN---------NRASFKGCTALHYAVLADDYRTVKELLDGGAN 291
Cdd:PHA03100 149 LESNKID-LKILKL----------LIDKGVDINakNRVNyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                        170       180
                 ....*....|....*....|....*..
gi 767968838 292 PLQRNEMGHTPLDYA---REGEVMKLL 315
Cdd:PHA03100 218 PNLVNKYGDTPLHIAilnNNKEIFKLL 244
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 138-290 2.16e-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: 46.54  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 138 LLEAARANNMQEVSRLL-SEGADVNAKHRLGWTALMVAAINRNNSVVQVLLaagadpnlgddfssvyktakeqgihsled 216
Cdd:cd22192   21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM----------------------------- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968838 217 ggqDGASRHITNQWTSALefrrwlglpagvlitreddfnnrlnnrasFKGCTALHYAVLADDYRTVKELLDGGA 290
Cdd:cd22192   72 ---EAAPELVNEPMTSDL-----------------------------YQGETALHIAVVNQNLNLVRELIARGA 113
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 265-292 1.64e-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: 38.34  E-value: 1.64e-04
                           10        20
                   ....*....|....*....|....*...
gi 767968838   265 KGCTALHYAVLADDYRTVKELLDGGANP 292
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-321 1.19e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 132 SNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDdfssvyktakeqgi 211
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-------------- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 212 hsledggqdgasrhitNQWTSALEFRRWLGLPAGV--LITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGG 289
Cdd:COG0666  151 ----------------NDGNTPLHLAAANGNLEIVklLLEAGADVNARDND-----GETPLHLAAENGHLEIVKLLLEAG 209

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767968838 290 ANPLQRNEMGHTPLDYARE---GEVMKLLRTSEAK 321
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAEngnLEIVKLLLEAGAD 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-197 2.30e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838  111 AGLGMCALAAALVVHCYSKSPSNKDA--ALLEAARANNMQEVSRLLSEgADVNAKHRlGWTALMVAAINRNNSVVQVLLA 188
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGrtALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 767968838  189 AGADPNLGD 197
Cdd:pfam12796  83 KGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-296 2.31e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838  138 LLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLaAGADPNLGDDfssvyktakeqgihsledg 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN------------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767968838  218 gqdgasrhitnqwtsalefrrwlglpagvlitreddfnnrlnnrasfkGCTALHYAVLADDYRTVKELLDGGANPLQRN 296
Cdd:pfam12796  61 ------------------------------------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 145-315 1.36e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 145 NNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSV--VQVLLAAGADPNLgddfssvyKTAKeqGIHSLEDggqdgA 222
Cdd:PHA03100  84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYsiVEYLLDNGANVNI--------KNSD--GENLLHL-----Y 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 223 SRHITNQwTSALEFrrwlglpagvLITREDDFN--NRLN---------NRASFKGCTALHYAVLADDYRTVKELLDGGAN 291
Cdd:PHA03100 149 LESNKID-LKILKL----------LIDKGVDINakNRVNyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                        170       180
                 ....*....|....*....|....*..
gi 767968838 292 PLQRNEMGHTPLDYA---REGEVMKLL 315
Cdd:PHA03100 218 PNLVNKYGDTPLHIAilnNNKEIFKLL 244
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-238 2.68e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 125 HCYSKS-PSNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGAD---PNLGDDFS 200
Cdd:PLN03192 612 HFASISdPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFS 691

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767968838 201 SVYKT---AKEQGIHSL----------EDGGQDGASRHITNQWTSALEFRR 238
Cdd:PLN03192 692 PTELRellQKRELGHSItivdsvpadePDLGRDGGSRPGRLQGTSSDNQCR 742
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-195 1.46e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 1.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767968838 150 VSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNL 195
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-315 1.57e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.18  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 181 SVVQVLLAAGADPNLGDDFSSVYKTAKEQGIHSLEDGGQDGASRHITNQWTSALEFRRWLGLPAGVLITREDDFNNRLNN 260
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767968838 261 RASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYAREG---EVMKLL 315
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNgnlEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
137-187 1.71e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767968838  137 ALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLL 187
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
253-306 3.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 3.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767968838  253 DFNNRLNNRASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA 306
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 124-306 5.38e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 5.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 124 VHCYskspsnkdaalleaARANNMQEVSRLLSE-GADVNAKHRLGWTALMV--AAINRNNSVVQVLLAAGADPNLGDDFS 200
Cdd:PHA03095  87 LHLY--------------LYNATTLDVIKLLIKaGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 201 svyKTAkeqgIHSLEdggqdgASRHITnqwtsaLEFRRWLgLPAGVLITREDDFNNrlnnrasfkgcTALHY--AVLADD 278
Cdd:PHA03095 153 ---MTP----LAVLL------KSRNAN------VELLRLL-IDAGADVYAVDDRFR-----------SLLHHhlQSFKPR 201

                        170       180
                 ....*....|....*....|....*...
gi 767968838 279 YRTVKELLDGGANPLQRNEMGHTPLDYA 306
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNTPLHSM 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 153-306 5.76e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 153 LLSEGADVNAKHR-LGWTALMVAAINRNNSVVQVLLAAGADPNLGD--DFSSVYKTAK---EQGIHSLEDGGQDGASR-- 224
Cdd:PHA02878 153 LLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDktNNSPLHHAVKhynKPIVHILLENGASTDARdk 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 225 ------HITNQWTSALEFRRWLgLPAGVLItreddfnnrlNNRASFKGCTALHYAVlaDDYRTVKELLDGGANPLQRNEM 298
Cdd:PHA02878 233 cgntplHISVGYCKDYDILKLL-LEHGVDV----------NAKSYILGLTALHSSI--KSERKLKLLLEYGADINSLNSY 299


                 ....*...
gi 767968838 299 GHTPLDYA 306
Cdd:PHA02878 300 KLTPLSSA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 139-315 1.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 139 LEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAA-INRNNSVVQVLLAAGADPNLGD--DFSSVYKTAKEQG---IH 212
Cdd:PHA02876 313 LMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDycDKTPIHYAAVRNNvviIN 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 213 SLEDGGQDgasrhitnqwTSALefrrwlglpagvlitreddfnnrlnnraSFKGCTALHYAVLADD-YRTVKELLDGGAN 291
Cdd:PHA02876 393 TLLDYGAD----------IEAL----------------------------SQKIGTALHFALCGTNpYMSVKTLIDRGAN 434

                        170       180
                 ....*....|....*....|....*...
gi 767968838 292 PLQRNEMGHTPLDYAREG----EVMKLL 315
Cdd:PHA02876 435 VNSKNKDLSTPLHYACKKncklDVIEML 462
Ank_2 pfam12796
Ankyrin repeats (3 copies);
247-325 1.71e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838  247 LITREDDFNNRLNNrasfkGCTALHYAVLADDYRTVKELLDGGAnpLQRNEMGHTPLDYA-REG--EVMKLLRTSEAKYQ 323
Cdd:pfam12796  16 LLENGADANLQDKN-----GRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAaRSGhlEIVKLLLEKGADIN 88


                  ..
gi 767968838  324 EK 325
Cdd:pfam12796  89 VK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 138-290 2.16e-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: 46.54  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968838 138 LLEAARANNMQEVSRLL-SEGADVNAKHRLGWTALMVAAINRNNSVVQVLLaagadpnlgddfssvyktakeqgihsled 216
Cdd:cd22192   21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM----------------------------- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968838 217 ggqDGASRHITNQWTSALefrrwlglpagvlitreddfnnrlnnrasFKGCTALHYAVLADDYRTVKELLDGGA 290
Cdd:cd22192   72 ---EAAPELVNEPMTSDL-----------------------------YQGETALHIAVVNQNLNLVRELIARGA 113
Ank_5 pfam13857
Ankyrin repeats (many copies);
153-199 2.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 2.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767968838  153 LLSEG-ADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDF 199
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 167-198 4.26e-05

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: 40.35  E-value: 4.26e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 767968838  167 GWTALMVAAINRNN-SVVQVLLAAGADPNLGDD 198
Cdd:pfam00023   2 GNTPLHLAAGRRGNlEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 265-297 1.44e-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: 1.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767968838  265 KGCTALHYAVL-ADDYRTVKELLDGGANPLQRNE 297
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 265-292 1.64e-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: 38.34  E-value: 1.64e-04
                           10        20
                   ....*....|....*....|....*...
gi 767968838   265 KGCTALHYAVLADDYRTVKELLDGGANP 292
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_2 pfam12796
Ankyrin repeats (3 copies);
270-315 1.78e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 1.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767968838  270 LHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA-REG--EVMKLL 315
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAaKNGhlEIVKLL 49
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 167-195 2.01e-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: 38.34  E-value: 2.01e-04
                           10        20
                   ....*....|....*....|....*....
gi 767968838   167 GWTALMVAAINRNNSVVQVLLAAGADPNL 195
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 167-194 3.11e-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: 37.62  E-value: 3.11e-04
                          10        20
                  ....*....|....*....|....*...
gi 767968838  167 GWTALMVAAINRNNSVVQVLLAAGADPN 194
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 153-210 1.21e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 1.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767968838 153 LLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGD-DFSSVYKTAKEQG 210
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDkDGKTPLELAEENG 159
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 137-192 2.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 2.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767968838 137 ALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGAD 192
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
268-306 3.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 3.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767968838  268 TALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYA 306
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 265-292 6.54e-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: 33.77  E-value: 6.54e-03
                          10        20
                  ....*....|....*....|....*...
gi 767968838  265 KGCTALHYAVLADDYRTVKELLDGGANP 292
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
 
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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