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P33724 (CAV1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caveolin-1
Alternative name(s):
Vesicular integral-membrane protein VIP21
Gene names
Name:CAV1
Synonyms:CAV
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.5 Ref.8

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membranecaveola; Peripheral membrane protein. Membrane raft By similarity. Note: Colocalized with DPP4 in membrane rafts By similarity. Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Ref.4 Ref.8

Post-translational modification

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

Sequence similarities

Belongs to the caveolin family.

Ontologies

Keywords
   Cellular componentCell membrane
Golgi apparatus
Membrane
   Coding sequence diversityAlternative initiation
   PTMAcetylation
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from electronic annotation. Source: Ensembl

T cell costimulation

Inferred from sequence or structural similarity. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: Ensembl

apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

caveola assembly

Inferred from electronic annotation. Source: Ensembl

caveolin-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

cellular response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from electronic annotation. Source: Ensembl

cytosolic calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

inactivation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

lipid storage

Inferred from electronic annotation. Source: Ensembl

mammary gland involution

Inferred from electronic annotation. Source: Ensembl

membrane depolarization

Inferred from electronic annotation. Source: Ensembl

negative regulation of BMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of anoikis

Inferred from electronic annotation. Source: Ensembl

negative regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytokine-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of tyrosine phosphorylation of Stat5 protein

Inferred from electronic annotation. Source: Ensembl

nitric oxide homeostasis

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport into cytosol

Inferred from electronic annotation. Source: Ensembl

positive regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of metalloenzyme activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein localization

Inferred from electronic annotation. Source: Ensembl

receptor internalization involved in canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of blood coagulation

Inferred from electronic annotation. Source: Ensembl

regulation of fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

regulation of the force of heart contraction by chemical signal

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to ischemia

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

vasoconstriction

Inferred from electronic annotation. Source: Ensembl

vesicle organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

acrosomal membrane

Inferred from electronic annotation. Source: Ensembl

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

caveola

Inferred from direct assay Ref.4. Source: UniProtKB

cell cortex

Inferred from electronic annotation. Source: Ensembl

cilium

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionpeptidase activator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 17785436. Source: IntAct

structural molecule activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P352225EBI-79998,EBI-491549From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Alpha (identifier: P33724-1)

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.
Isoform Beta (identifier: P33724-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-31: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 178177Caveolin-1
PRO_0000004762

Regions

Topological domain2 – 104103Cytoplasmic Potential
Intramembrane105 – 12521Helical; Potential
Topological domain126 – 17853Cytoplasmic Potential

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue51N6-acetyllysine By similarity
Modified residue61Phosphotyrosine By similarity
Modified residue141Phosphotyrosine; by ABL1 By similarity
Modified residue251Phosphotyrosine By similarity
Modified residue371Phosphoserine By similarity
Modified residue421Phosphotyrosine By similarity
Lipidation1331S-palmitoyl cysteine Ref.6
Lipidation1431S-palmitoyl cysteine Ref.6
Lipidation1561S-palmitoyl cysteine Ref.6

Natural variations

Alternative sequence2 – 3130Missing in isoform Beta.
VSP_018691

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: DD77CE4D436E508D

FASTA17820,606
        10         20         30         40         50         60 
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMAEEMSEKQ VYDAHTKEID LVNRDPKHLN 

        70         80         90        100        110        120 
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSALFGIP MALIWGIYFA 

       130        140        150        160        170 
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTFCDPFF EAVGKIFSNI RINMQKET 

« Hide

Isoform Beta [UniParc].

Checksum: E367441F6A2FEA2F
Show »

FASTA14817,288

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z12161 Genomic DNA. Translation: CAA78151.1.
U47060 mRNA. Translation: AAA87050.1.
DP000236 Genomic DNA. Translation: AAR16266.1.
PIRA43419.
RefSeqNP_001003296.1. NM_001003296.1. [P33724-1]
UniGeneCfa.3850.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid139896. 1 interaction.
IntActP33724. 5 interactions.

Proteomic databases

PaxDbP33724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000005462; ENSCAFP00000005060; ENSCAFG00000003404. [P33724-1]
GeneID403980.
KEGGcfa:403980.

Organism-specific databases

CTD857.

Phylogenomic databases

eggNOGNOG86001.
GeneTreeENSGT00390000014924.
HOGENOMHOG000036550.
HOVERGENHBG003422.
InParanoidP33724.
KOK06278.
OMARINMQKE.
OrthoDBEOG7V1FSD.
TreeFamTF315736.

Family and domain databases

InterProIPR001612. Caveolin.
IPR015504. Caveolin_1.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERPTHR10844. PTHR10844. 1 hit.
PTHR10844:SF5. PTHR10844:SF5. 1 hit.
PfamPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEPS01210. CAVEOLIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20817470.

Entry information

Entry nameCAV1_CANFA
AccessionPrimary (citable) accession number: P33724
Secondary accession number(s): A0M8U8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 11, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families