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Conserved domains on  [gi|15451856|ref|NP_001744|]
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caveolin-1 isoform alpha [Homo sapiens]

Protein Classification

Caveolin domain-containing protein( domain architecture ID 10471699)

Caveolin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Caveolin pfam01146
Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within ...
 43-174 9.41e-76

Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within their hydrophilic N-terminal domain. Caveolin 2 (Cav-2) is co-localized and co-expressed with Cav-1/VIP21, forms heterodimers with it and needs Cav-1 for proper membrane localization. Cav-3 has greater protein sequence similarity to Cav-1 than to Cav-2. Cellular processes caveolins are involved in include vesicular transport, cholesterol homeostasis, signal transduction, and tumour suppression.


:

Pssm-ID: 460081  Cd Length: 133  Bit Score: 222.85  E-value: 9.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15451856    43 DAHTKEIDLVNRDPKHLNDDVvKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAIL 122
Cdd:pfam01146   2 DEFTKGIDLIDRDPKQINEHL-KVGFEDVIAEPDSTHSFDRVWIGSHALFEVSKYWIYRLLTALLAIPLALIWGILFALL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15451856   123 SFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINL 174
Cdd:pfam01146  81 SCLHIWLVMPCIKSCLIPLPSLQKVWSSLVDTIFDPLFESVGLCFSSINIRL 132
 
Name Accession Description Interval E-value
Caveolin pfam01146
Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within ...
 43-174 9.41e-76

Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within their hydrophilic N-terminal domain. Caveolin 2 (Cav-2) is co-localized and co-expressed with Cav-1/VIP21, forms heterodimers with it and needs Cav-1 for proper membrane localization. Cav-3 has greater protein sequence similarity to Cav-1 than to Cav-2. Cellular processes caveolins are involved in include vesicular transport, cholesterol homeostasis, signal transduction, and tumour suppression.


Pssm-ID: 460081  Cd Length: 133  Bit Score: 222.85  E-value: 9.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15451856    43 DAHTKEIDLVNRDPKHLNDDVvKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAIL 122
Cdd:pfam01146   2 DEFTKGIDLIDRDPKQINEHL-KVGFEDVIAEPDSTHSFDRVWIGSHALFEVSKYWIYRLLTALLAIPLALIWGILFALL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15451856   123 SFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINL 174
Cdd:pfam01146  81 SCLHIWLVMPCIKSCLIPLPSLQKVWSSLVDTIFDPLFESVGLCFSSINIRL 132
 
Name Accession Description Interval E-value
Caveolin pfam01146
Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within ...
 43-174 9.41e-76

Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within their hydrophilic N-terminal domain. Caveolin 2 (Cav-2) is co-localized and co-expressed with Cav-1/VIP21, forms heterodimers with it and needs Cav-1 for proper membrane localization. Cav-3 has greater protein sequence similarity to Cav-1 than to Cav-2. Cellular processes caveolins are involved in include vesicular transport, cholesterol homeostasis, signal transduction, and tumour suppression.


Pssm-ID: 460081  Cd Length: 133  Bit Score: 222.85  E-value: 9.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15451856    43 DAHTKEIDLVNRDPKHLNDDVvKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAIL 122
Cdd:pfam01146   2 DEFTKGIDLIDRDPKQINEHL-KVGFEDVIAEPDSTHSFDRVWIGSHALFEVSKYWIYRLLTALLAIPLALIWGILFALL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15451856   123 SFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINL 174
Cdd:pfam01146  81 SCLHIWLVMPCIKSCLIPLPSLQKVWSSLVDTIFDPLFESVGLCFSSINIRL 132
 
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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