Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Caveolin-1

Gene

CAV1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_281850. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_297375. NOSTRIN mediated eNOS trafficking.
REACT_297734. VEGFR2 mediated vascular permeability.
REACT_318385. eNOS activation.
REACT_340332. Basigin interactions.
REACT_348787. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
Caveolin-1
Alternative name(s):
Vesicular integral-membrane protein VIP21
Gene namesi
Name:CAV1
Synonyms:CAV
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Chromosome 14

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 104103CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei105 – 12521HelicalSequence AnalysisAdd
BLAST
Topological domaini126 – 17853CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 178177Caveolin-1PRO_0000004762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei6 – 61PhosphotyrosineBy similarity
Modified residuei14 – 141Phosphotyrosine; by ABL1By similarity
Modified residuei25 – 251PhosphotyrosineBy similarity
Modified residuei37 – 371PhosphoserineBy similarity
Lipidationi133 – 1331S-palmitoyl cysteine1 Publication
Lipidationi143 – 1431S-palmitoyl cysteine1 Publication
Lipidationi156 – 1561S-palmitoyl cysteine1 Publication

Post-translational modificationi

Phosphorylation of isoform Beta on serine residues is constitutive. Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress (By similarity).By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP33724.

Interactioni

Subunit structurei

Homooligomer. Interacts with BMX, BTK, GLIPR2, NOSTRIN, SNAP25 and STX1A. Interacts with PACSIN2 (By similarity). Interacts (via the N-terminus) with DPP4; the interaction is direct. Interacts with SLC7A9 (By similarity). Interacts with CTNNB1, CDH1 and JUP.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352225EBI-79998,EBI-491549From a different organism.

Protein-protein interaction databases

BioGridi139896. 1 interaction.
IntActiP33724. 5 interactions.
STRINGi9615.ENSCAFP00000005060.

Family & Domainsi

Sequence similaritiesi

Belongs to the caveolin family.Curated

Phylogenomic databases

eggNOGiNOG86001.
GeneTreeiENSGT00390000014924.
HOGENOMiHOG000036550.
HOVERGENiHBG003422.
InParanoidiP33724.
KOiK06278.
OMAiVHTFCDP.
OrthoDBiEOG7V1FSD.
TreeFamiTF315736.

Family and domain databases

InterProiIPR001612. Caveolin.
IPR015504. Caveolin_1.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERiPTHR10844. PTHR10844. 1 hit.
PTHR10844:SF5. PTHR10844:SF5. 1 hit.
PfamiPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEiPS01210. CAVEOLIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Alpha (identifier: P33724-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMAEEMSEKQ VYDAHTKEID
60 70 80 90 100
LVNRDPKHLN DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY
110 120 130 140 150
RLLSALFGIP MALIWGIYFA ILSFLHIWAV VPCIKSFLIE IQCISRVYSI
160 170
YVHTFCDPFF EAVGKIFSNI RINMQKET
Length:178
Mass (Da):20,606
Last modified:February 1, 1994 - v1
Checksum:iDD77CE4D436E508D
GO
Isoform Beta (identifier: P33724-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Show »
Length:147
Mass (Da):17,157
Checksum:iE32E90B50FFC5B1F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform Beta. CuratedVSP_018691Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12161 Genomic DNA. Translation: CAA78151.1.
U47060 mRNA. Translation: AAA87050.1.
DP000236 Genomic DNA. Translation: AAR16266.1.
PIRiA43419.
RefSeqiNP_001003296.1. NM_001003296.1. [P33724-1]
XP_005628404.1. XM_005628347.1. [P33724-2]
UniGeneiCfa.3850.

Genome annotation databases

EnsembliENSCAFT00000005462; ENSCAFP00000005060; ENSCAFG00000003404. [P33724-1]
GeneIDi403980.
KEGGicfa:403980.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12161 Genomic DNA. Translation: CAA78151.1.
U47060 mRNA. Translation: AAA87050.1.
DP000236 Genomic DNA. Translation: AAR16266.1.
PIRiA43419.
RefSeqiNP_001003296.1. NM_001003296.1. [P33724-1]
XP_005628404.1. XM_005628347.1. [P33724-2]
UniGeneiCfa.3850.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi139896. 1 interaction.
IntActiP33724. 5 interactions.
STRINGi9615.ENSCAFP00000005060.

Proteomic databases

PaxDbiP33724.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000005462; ENSCAFP00000005060; ENSCAFG00000003404. [P33724-1]
GeneIDi403980.
KEGGicfa:403980.

Organism-specific databases

CTDi857.

Phylogenomic databases

eggNOGiNOG86001.
GeneTreeiENSGT00390000014924.
HOGENOMiHOG000036550.
HOVERGENiHBG003422.
InParanoidiP33724.
KOiK06278.
OMAiVHTFCDP.
OrthoDBiEOG7V1FSD.
TreeFamiTF315736.

Enzyme and pathway databases

ReactomeiREACT_281850. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_297375. NOSTRIN mediated eNOS trafficking.
REACT_297734. VEGFR2 mediated vascular permeability.
REACT_318385. eNOS activation.
REACT_340332. Basigin interactions.
REACT_348787. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

NextBioi20817470.

Family and domain databases

InterProiIPR001612. Caveolin.
IPR015504. Caveolin_1.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERiPTHR10844. PTHR10844. 1 hit.
PTHR10844:SF5. PTHR10844:SF5. 1 hit.
PfamiPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEiPS01210. CAVEOLIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles."
    Kurzchalia T.V., Dupree P., Parton R.G., Kellner R., Virta H., Lehnert M., Simons K.
    J. Cell Biol. 118:1003-1014(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-74 AND 166-176.
    Tissue: Epithelium.
  2. "Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells."
    Sargiacomo M., Sudol M., Tang Z., Lisanti M.P.
    J. Cell Biol. 122:789-807(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Cocker spaniel.
    Tissue: Kidney.
  3. "Comparative analyses of multi-species sequences from targeted genomic regions."
    Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G., Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C., Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S., Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R.
    , Cutler D.J., Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q., Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N., Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S., Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E., Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A., Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E., Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D., Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B., Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A., Haussler D., Green P., Miller W., Green E.D.
    Nature 424:788-793(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Caveolae and sorting in the trans-Golgi network of epithelial cells."
    Dupree P., Parton R.G., Raposo G., Kurzchalia T.V., Simons K.
    EMBO J. 12:1597-1605(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Oligomeric structure of caveolin: implications for caveolae membrane organization."
    Sargiacomo M., Scherer P.E., Tang Z., Kubler E., Song K.S., Sanders M.C., Lisanti M.P.
    Proc. Natl. Acad. Sci. U.S.A. 92:9407-9411(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae."
    Dietzen D.J., Hastings W.R., Lublin D.M.
    J. Biol. Chem. 270:6838-6842(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-133; CYS-143 AND CYS-156.
  7. "Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe."
    Scherer P.E., Tang Z., Chun M., Sargiacomo M., Lodish H.F., Lisanti M.P.
    J. Biol. Chem. 270:16395-16401(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION.
  8. "Caveolin-1 expression inhibits Wnt/beta-catenin/Lef-1 signaling by recruiting beta-catenin to caveolae membrane domains."
    Galbiati F., Volonte D., Brown A.M., Weinstein D.E., Ben-Ze'ev A., Pestell R.G., Lisanti M.P.
    J. Biol. Chem. 275:23368-23377(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNB1; CDH1 AND JUP, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCAV1_CANFA
AccessioniPrimary (citable) accession number: P33724
Secondary accession number(s): A0M8U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 24, 2015
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.