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Conserved domains on  [gi|145611446|ref|NP_001012302|]
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anoctamin-9 isoform 1 [Homo sapiens]

Protein Classification

anoctamin( domain architecture ID 11069330)

anoctamin (anion channel with 8 transmembrane domains) is a calcium-activated protein and may mediate the calcium-dependent exposure of phospholipids to the extracellular surface, a process called phospholipid scrambling

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
179-737 4.43e-110

Calcium-activated chloride channel; The family carries eight putative transmembrane domains, and, although it has no similarity to other known channel proteins, it is clearly a calcium-activated ionic channel. It is expressed in various secretory epithelia, the retina and sensory neurons, and mediates receptor-activated chloride currents in diverse physiological processes.


:

Pssm-ID: 461349  Cd Length: 377  Bit Score: 340.33  E-value: 4.43e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  179 IRNYFGEKVALYFVWLGWYTYMLVPAALTGLLVFLSGFSlfeasqiskeiceahdilmcplgdhsrryqrlsetctfakl 258
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLA----------------------------------------- 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  259 tHLFDnDGTVVFAIFMALWATVFLEIWKRQRARVVLHWDLYVWDEEQEEMA-----LQLINCPDYKLRPYQHSYLRSTVI 333
Cdd:pfam04547  40 -TLFD-PYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFEEEEEPRPefkgeKERINPVTGEKEPYYPPWKRRLRR 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  334 LVLTLLMICLMIgmahvlvvyrvlasalfsssavpfleeqvttAVVVTGAlvhyvtIIIMTKINRCVALKLCDFEMPRTF 413
Cdd:pfam04547 118 YLLSIPLVLLLI-------------------------------ALLVLGV------IIYLNFVYTKLAKKLTDWENHRTQ 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  414 SERESRFTIRFFTlqffthfssliyiafilgringhpgkstrlaglwkleechasgcmMDLFVQMAIIMGLKQTLSNCVE 493
Cdd:pfam04547 161 SEYENSLILKVFL---------------------------------------------DRLRIQLAIIMVTKQIINNITE 195
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  494 YLVPWVTHKCRSLR----------ASESGHLPRDPELRDWRRNYLLNPVNTFslfDEFMEMMIQYGFTTIFVAAFPLAPL 563
Cdd:pfam04547 196 VVLPYLKRKRRKKRkkkkkkeepsVSIKDEPEESEFLERVEKEYELEPYDGL---DDYLEMVIQFGYVTLFSAAFPLAPL 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  564 LALFSNLVEIRLDAIKMVWLQRRLVPRKAKDIGTWLQVLETIGVLAVIANGMVI-AFTsefiprvvykyryspclkegns 642
Cdd:pfam04547 273 FALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIyAFT---------------------- 330
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  643 tvdclkgyvnhslsvfhtkdfqdpdgiegsenvtlcryrdyrnppdynfSEQFWFLLAIRLAFVILFEHVALCIKLIAAW 722
Cdd:pfam04547 331 -------------------------------------------------SDQYWSLLALLLAFVIVFEHVVLLLKFLIAW 361
                         570
                  ....*....|....*
gi 145611446  723 FVPDIPQSVKNKVLE 737
Cdd:pfam04547 362 LIPDVPEWVRKERKR 376
Anoct_dimer super family cl24682
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
115-176 3.65e-06

dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be the cytoplasmic domain of the calcium-activated chloride-channel, anoctamin, protein. It is responsible for creating the homodimeric architecture of the chloride-channel proteins.


The actual alignment was detected with superfamily member pfam16178:

Pssm-ID: 465044  Cd Length: 224  Bit Score: 48.71  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  115 TTSLRIRIVNFVvMNNKTSAGETFED-----LMKDGVFEARFPLHKGEGRLKKT-------------WARWRHMFREQPV 176
Cdd:pfam16178 146 TNATRSRIVYEI-LSRTRYGGRKKKEvgikrLLNEGVYLAAYPLHDGPYKLPKDpselnerqllyeeWARWGKWYKYQPL 224
 
Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
179-737 4.43e-110

Calcium-activated chloride channel; The family carries eight putative transmembrane domains, and, although it has no similarity to other known channel proteins, it is clearly a calcium-activated ionic channel. It is expressed in various secretory epithelia, the retina and sensory neurons, and mediates receptor-activated chloride currents in diverse physiological processes.


Pssm-ID: 461349  Cd Length: 377  Bit Score: 340.33  E-value: 4.43e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  179 IRNYFGEKVALYFVWLGWYTYMLVPAALTGLLVFLSGFSlfeasqiskeiceahdilmcplgdhsrryqrlsetctfakl 258
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLA----------------------------------------- 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  259 tHLFDnDGTVVFAIFMALWATVFLEIWKRQRARVVLHWDLYVWDEEQEEMA-----LQLINCPDYKLRPYQHSYLRSTVI 333
Cdd:pfam04547  40 -TLFD-PYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFEEEEEPRPefkgeKERINPVTGEKEPYYPPWKRRLRR 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  334 LVLTLLMICLMIgmahvlvvyrvlasalfsssavpfleeqvttAVVVTGAlvhyvtIIIMTKINRCVALKLCDFEMPRTF 413
Cdd:pfam04547 118 YLLSIPLVLLLI-------------------------------ALLVLGV------IIYLNFVYTKLAKKLTDWENHRTQ 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  414 SERESRFTIRFFTlqffthfssliyiafilgringhpgkstrlaglwkleechasgcmMDLFVQMAIIMGLKQTLSNCVE 493
Cdd:pfam04547 161 SEYENSLILKVFL---------------------------------------------DRLRIQLAIIMVTKQIINNITE 195
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  494 YLVPWVTHKCRSLR----------ASESGHLPRDPELRDWRRNYLLNPVNTFslfDEFMEMMIQYGFTTIFVAAFPLAPL 563
Cdd:pfam04547 196 VVLPYLKRKRRKKRkkkkkkeepsVSIKDEPEESEFLERVEKEYELEPYDGL---DDYLEMVIQFGYVTLFSAAFPLAPL 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  564 LALFSNLVEIRLDAIKMVWLQRRLVPRKAKDIGTWLQVLETIGVLAVIANGMVI-AFTsefiprvvykyryspclkegns 642
Cdd:pfam04547 273 FALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIyAFT---------------------- 330
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  643 tvdclkgyvnhslsvfhtkdfqdpdgiegsenvtlcryrdyrnppdynfSEQFWFLLAIRLAFVILFEHVALCIKLIAAW 722
Cdd:pfam04547 331 -------------------------------------------------SDQYWSLLALLLAFVIVFEHVVLLLKFLIAW 361
                         570
                  ....*....|....*
gi 145611446  723 FVPDIPQSVKNKVLE 737
Cdd:pfam04547 362 LIPDVPEWVRKERKR 376
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
115-176 3.65e-06

dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be the cytoplasmic domain of the calcium-activated chloride-channel, anoctamin, protein. It is responsible for creating the homodimeric architecture of the chloride-channel proteins.


Pssm-ID: 465044  Cd Length: 224  Bit Score: 48.71  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  115 TTSLRIRIVNFVvMNNKTSAGETFED-----LMKDGVFEARFPLHKGEGRLKKT-------------WARWRHMFREQPV 176
Cdd:pfam16178 146 TNATRSRIVYEI-LSRTRYGGRKKKEvgikrLLNEGVYLAAYPLHDGPYKLPKDpselnerqllyeeWARWGKWYKYQPL 224
 
Name Accession Description Interval E-value
Anoctamin pfam04547
Calcium-activated chloride channel; The family carries eight putative transmembrane domains, ...
179-737 4.43e-110

Calcium-activated chloride channel; The family carries eight putative transmembrane domains, and, although it has no similarity to other known channel proteins, it is clearly a calcium-activated ionic channel. It is expressed in various secretory epithelia, the retina and sensory neurons, and mediates receptor-activated chloride currents in diverse physiological processes.


Pssm-ID: 461349  Cd Length: 377  Bit Score: 340.33  E-value: 4.43e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  179 IRNYFGEKVALYFVWLGWYTYMLVPAALTGLLVFLSGFSlfeasqiskeiceahdilmcplgdhsrryqrlsetctfakl 258
Cdd:pfam04547   1 IRDYFGEKIAFYFAFLGFYTKWLLPPAIVGLLVFLYGLA----------------------------------------- 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  259 tHLFDnDGTVVFAIFMALWATVFLEIWKRQRARVVLHWDLYVWDEEQEEMA-----LQLINCPDYKLRPYQHSYLRSTVI 333
Cdd:pfam04547  40 -TLFD-PYTVFFAIFMSLWATLFLEFWKRREAELAYRWGTTGFEEEEEPRPefkgeKERINPVTGEKEPYYPPWKRRLRR 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  334 LVLTLLMICLMIgmahvlvvyrvlasalfsssavpfleeqvttAVVVTGAlvhyvtIIIMTKINRCVALKLCDFEMPRTF 413
Cdd:pfam04547 118 YLLSIPLVLLLI-------------------------------ALLVLGV------IIYLNFVYTKLAKKLTDWENHRTQ 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  414 SERESRFTIRFFTlqffthfssliyiafilgringhpgkstrlaglwkleechasgcmMDLFVQMAIIMGLKQTLSNCVE 493
Cdd:pfam04547 161 SEYENSLILKVFL---------------------------------------------DRLRIQLAIIMVTKQIINNITE 195
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  494 YLVPWVTHKCRSLR----------ASESGHLPRDPELRDWRRNYLLNPVNTFslfDEFMEMMIQYGFTTIFVAAFPLAPL 563
Cdd:pfam04547 196 VVLPYLKRKRRKKRkkkkkkeepsVSIKDEPEESEFLERVEKEYELEPYDGL---DDYLEMVIQFGYVTLFSAAFPLAPL 272
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  564 LALFSNLVEIRLDAIKMVWLQRRLVPRKAKDIGTWLQVLETIGVLAVIANGMVI-AFTsefiprvvykyryspclkegns 642
Cdd:pfam04547 273 FALLNNIIEIRSDAFKLCTELRRPVPERADSIGPWLNILEFLSWLAVITNAALIyAFT---------------------- 330
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  643 tvdclkgyvnhslsvfhtkdfqdpdgiegsenvtlcryrdyrnppdynfSEQFWFLLAIRLAFVILFEHVALCIKLIAAW 722
Cdd:pfam04547 331 -------------------------------------------------SDQYWSLLALLLAFVIVFEHVVLLLKFLIAW 361
                         570
                  ....*....|....*
gi 145611446  723 FVPDIPQSVKNKVLE 737
Cdd:pfam04547 362 LIPDVPEWVRKERKR 376
Anoct_dimer pfam16178
dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be ...
115-176 3.65e-06

dimerization domain of Ca+-activated chloride-channel, anoctamin; This family appears to be the cytoplasmic domain of the calcium-activated chloride-channel, anoctamin, protein. It is responsible for creating the homodimeric architecture of the chloride-channel proteins.


Pssm-ID: 465044  Cd Length: 224  Bit Score: 48.71  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145611446  115 TTSLRIRIVNFVvMNNKTSAGETFED-----LMKDGVFEARFPLHKGEGRLKKT-------------WARWRHMFREQPV 176
Cdd:pfam16178 146 TNATRSRIVYEI-LSRTRYGGRKKKEvgikrLLNEGVYLAAYPLHDGPYKLPKDpselnerqllyeeWARWGKWYKYQPL 224
 
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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