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Conserved domains on  [gi|392921545|ref|NP_001256524|]
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Caveolin-2 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Caveolin super family cl07832
Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within ...
139-265 2.62e-29

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.


The actual alignment was detected with superfamily member pfam01146:

Pssm-ID: 460081  Cd Length: 133  Bit Score: 108.06  E-value: 2.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921545  139 MNMDDRDPKDSAQYLNTSFFEVFNEPSEQyHSIACVWTLSFKIFEIVRIYSYKILTLIFGLIIAFLGGILFALFAFLNIW 218
Cdd:pfam01146   8 IDLIDRDPKQINEHLKVGFEDVIAEPDST-HSFDRVWIGSHALFEVSKYWIYRLLTALLAIPLALIWGILFALLSCLHIW 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 392921545  219 IFRPILILTRMAFAQIVLIWPMFLIYIVRPFFYSVGAIFSTARLHTS 265
Cdd:pfam01146  87 LVMPCIKSCLIPLPSLQKVWSSLVDTIFDPLFESVGLCFSSINIRLY 133
 
Name Accession Description Interval E-value
Caveolin pfam01146
Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within ...
139-265 2.62e-29

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: 108.06  E-value: 2.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921545  139 MNMDDRDPKDSAQYLNTSFFEVFNEPSEQyHSIACVWTLSFKIFEIVRIYSYKILTLIFGLIIAFLGGILFALFAFLNIW 218
Cdd:pfam01146   8 IDLIDRDPKQINEHLKVGFEDVIAEPDST-HSFDRVWIGSHALFEVSKYWIYRLLTALLAIPLALIWGILFALLSCLHIW 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 392921545  219 IFRPILILTRMAFAQIVLIWPMFLIYIVRPFFYSVGAIFSTARLHTS 265
Cdd:pfam01146  87 LVMPCIKSCLIPLPSLQKVWSSLVDTIFDPLFESVGLCFSSINIRLY 133
 
Name Accession Description Interval E-value
Caveolin pfam01146
Caveolin; All three known Caveolin forms have the FEDVIAEP caveolin 'signature motif' within ...
139-265 2.62e-29

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: 108.06  E-value: 2.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921545  139 MNMDDRDPKDSAQYLNTSFFEVFNEPSEQyHSIACVWTLSFKIFEIVRIYSYKILTLIFGLIIAFLGGILFALFAFLNIW 218
Cdd:pfam01146   8 IDLIDRDPKQINEHLKVGFEDVIAEPDST-HSFDRVWIGSHALFEVSKYWIYRLLTALLAIPLALIWGILFALLSCLHIW 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 392921545  219 IFRPILILTRMAFAQIVLIWPMFLIYIVRPFFYSVGAIFSTARLHTS 265
Cdd:pfam01146  87 LVMPCIKSCLIPLPSLQKVWSSLVDTIFDPLFESVGLCFSSINIRLY 133
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
181-237 9.48e-03

Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 37.14  E-value: 9.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921545  181 IFEIVRIYSYKILTLIFGLIIAFLGGILFALFAFLNIWI---FRPILILTRMAFAQIVLI 237
Cdd:pfam00654 148 LFSVGEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVqrlFRKLLKIPPVLRPALGGL 207
 
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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