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P49817 (CAV1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:Cav1
Synonyms:Cav
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. Ref.7

Subunit structure

Homooligomer By similarity. Interacts (via the N-terminus) with DPP4; the interaction is direct By similarity. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Interacts with BMX, BTK, CTNNB1, CDH1, GLIPR2, JUP, NOSTRIN, SNAP25 and STX1A. Interacts with SLC7A9 By similarity. Interacts with PACSIN2. Ref.12

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein By similarity. Cell membrane; Peripheral membrane protein By similarity. Membranecaveola; Peripheral membrane protein. Membrane raft By similarity. Note: Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae By similarity. Ref.12

Post-translational modification

The N-terminus of both isoforms are blocked.

Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. Ref.8 Ref.9

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 mutant phenotype PubMed 12388746. Source: MGI

T cell costimulation

Inferred from sequence or structural similarity. Source: UniProtKB

angiogenesis

Inferred from genetic interaction PubMed 12759260. Source: MGI

apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

calcium ion transport

Inferred from mutant phenotype PubMed 17416589. Source: MGI

caveola assembly

Inferred from mutant phenotype PubMed 12759260. Source: MGI

caveolin-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 17098833. Source: MGI

cellular response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from mutant phenotype PubMed 16603689. Source: MGI

cytosolic calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

endocytosis

Traceable author statement PubMed 10373486. Source: MGI

inactivation of MAPK activity

Inferred from mutant phenotype PubMed 12388077. Source: MGI

lactation

Inferred from mutant phenotype PubMed 12388746. Source: MGI

lipid storage

Inferred from mutant phenotype PubMed 11884617. Source: MGI

mammary gland involution

Inferred from mutant phenotype PubMed 12388746. Source: MGI

membrane depolarization

Inferred from mutant phenotype PubMed 17098833. Source: MGI

negative regulation of BMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of anoikis

Inferred from mutant phenotype PubMed 22277751. Source: UniProtKB

negative regulation of canonical Wnt signaling pathway

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of cytokine-mediated signaling pathway

Inferred from mutant phenotype PubMed 12388746. Source: MGI

negative regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 11884617. Source: MGI

negative regulation of epithelial cell differentiation

Inferred from mutant phenotype PubMed 12388746. Source: MGI

negative regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype PubMed 12388077. Source: MGI

negative regulation of nitric-oxide synthase activity

Inferred from mutant phenotype PubMed 16380094PubMed 18951881. Source: MGI

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 mutant phenotype PubMed 22277751. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of tyrosine phosphorylation of Stat5 protein

Inferred from direct assay PubMed 12388746. Source: MGI

nitric oxide homeostasis

Inferred from mutant phenotype PubMed 12177436. Source: MGI

positive regulation of calcium ion transport into cytosol

Inferred from direct assay PubMed 19052258. Source: BHF-UCL

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 mutant phenotype PubMed 17349656. Source: MGI

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasoconstriction

Inferred from mutant phenotype PubMed 11884617. Source: MGI

protein homooligomerization

Inferred from direct assay PubMed 8552590. Source: MGI

protein localization

Inferred from mutant phenotype PubMed 17416589. Source: MGI

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 mutant phenotype PubMed 11884617. Source: MGI

regulation of smooth muscle contraction

Inferred from mutant phenotype PubMed 16782699PubMed 17098833. Source: MGI

regulation of the force of heart contraction by chemical signal

Inferred from genetic interaction PubMed 18951881. Source: MGI

response to calcium ion

Inferred from direct assay PubMed 19052258. Source: BHF-UCL

response to estrogen

Inferred from direct assay PubMed 12388746. Source: MGI

response to hypoxia

Inferred from mutant phenotype PubMed 16601228. Source: MGI

response to ischemia

Inferred from mutant phenotype PubMed 17293479. Source: MGI

response to progesterone

Inferred from sequence orthology PubMed 12388746. Source: MGI

skeletal muscle tissue development

Inferred from mutant phenotype PubMed 17200204. Source: MGI

triglyceride metabolic process

Inferred from mutant phenotype PubMed 11884617. Source: MGI

vasculogenesis

Inferred from mutant phenotype PubMed 16601228. Source: MGI

vasoconstriction

Inferred from mutant phenotype PubMed 17098833. Source: MGI

vesicle organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from sequence or structural similarity. Source: HGNC

acrosomal membrane

Inferred from direct assay PubMed 11784086. Source: MGI

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

caveola

Inferred from sequence or structural similarity. Source: UniProtKB

cell cortex

Inferred from direct assay Ref.2. Source: MGI

cilium

Inferred from direct assay PubMed 11784086. Source: MGI

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: HGNC

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay PubMed 8552590. Source: MGI

perinuclear region of cytoplasm

Inferred from direct assay PubMed 8552590. Source: MGI

protein complex

Inferred from physical interaction PubMed 17416589. Source: MGI

   Molecular_functionpeptidase activator activity

Inferred from mutant phenotype PubMed 17349656. Source: MGI

structural molecule activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MCL1Q078203EBI-1161338,EBI-1003422From a different organism.
SCP2P223073EBI-1161338,EBI-1050999From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Alpha (identifier: P49817-1)

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: P49817-2)

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_0000004766

Regions

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

Amino acid modifications

Modified residue21N-acetylserine
Modified residue51N6-acetyllysine
Modified residue61Phosphotyrosine By similarity
Modified residue141Phosphotyrosine; by ABL1 and INSR Ref.8 Ref.9
Modified residue251Phosphotyrosine By similarity
Modified residue421Phosphotyrosine By similarity
Lipidation1331S-palmitoyl cysteine By similarity
Lipidation1431S-palmitoyl cysteine By similarity
Lipidation1561S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence2 – 3130Missing in isoform Beta.
VSP_018693

Experimental info

Sequence conflict1701I → F in BAC29118. Ref.4

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: CF88FE9B1D3D67AE

FASTA17820,539
        10         20         30         40         50         60 
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADEVTEKQ VYDAHTKEID LVNRDPKHLN 

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

       130        140        150        160        170 
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTFCDPLF EAIGKIFSNI RISTQKEI 

« Hide

Isoform Beta [UniParc].

Checksum: F19874C9347CDD0C
Show »

FASTA14817,221

References

« Hide 'large scale' references
[1]"The primary sequence of murine caveolin reveals a conserved consensus site for phosphorylation by protein kinase C."
Tang Z., Scherer P.E., Lisanti M.P.
Gene 147:299-300(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Strain: BALB/c.
[2]"Caveolin-1 isoforms are encoded in distinct mRNAs: identification of mouse caveolin-1 mRNA variants caused by alternative transcription initiation and splicing."
Kogo H., Fujimoto T.
FEBS Lett. 465:119-123(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS ALPHA AND BETA).
[3]"Met gene is a candidate for the mouse pulmonary adenoma resistance 4 (Par4) locus."
Zaffaroni D., Dragani T.A.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Strain: SWR/J.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA).
Strain: C57BL/6J.
Tissue: Embryo, Skin and Urinary bladder.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Strain: C3H/He.
Tissue: Mesenchymal cell.
[6]"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: PROTEIN SEQUENCE OF 5-26; 47-77 AND 165-176.
[7]"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: FUNCTION.
[8]"The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1."
Kimura A., Mora S., Shigematsu S., Pessin J.E., Saltiel A.R.
J. Biol. Chem. 277:30153-30158(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-14.
[9]"c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14."
Sanguinetti A.R., Mastick C.C.
Cell. Signal. 15:289-298(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-14.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[12]"Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting."
Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.
J. Cell Sci. 124:2032-2040(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PACSIN2, SUBCELLULAR LOCATION.
[13]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07645 mRNA. Translation: AAA85784.1.
AB029929 mRNA. Translation: BAA89461.1.
AB029930 mRNA. Translation: BAA89462.1.
AB029931 Genomic DNA. Translation: BAA89463.1.
AY439333 mRNA. Translation: AAR99702.1.
AK003489 mRNA. Translation: BAB22817.1.
AK028738 mRNA. Translation: BAC26091.1.
AK035592 mRNA. Translation: BAC29118.1.
AK090074 mRNA. Translation: BAC41079.1.
BC038280 mRNA. Translation: AAH38280.1.
BC052859 mRNA. Translation: AAH52859.1.
PIRI48976.
RefSeqNP_001229993.1. NM_001243064.1.
NP_031642.1. NM_007616.4.
XP_006505037.1. XM_006504974.1.
XP_006505038.1. XM_006504975.1.
XP_006505039.1. XM_006504976.1.
UniGeneMm.28278.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198514. 9 interactions.
DIPDIP-35140N.
IntActP49817. 10 interactions.
MINTMINT-1542313.

PTM databases

PhosphoSiteP49817.

Proteomic databases

PaxDbP49817.
PRIDEP49817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007799; ENSMUSP00000007799; ENSMUSG00000007655. [P49817-1]
ENSMUST00000115453; ENSMUSP00000111113; ENSMUSG00000007655. [P49817-2]
ENSMUST00000115454; ENSMUSP00000111114; ENSMUSG00000007655. [P49817-2]
ENSMUST00000115456; ENSMUSP00000111116; ENSMUSG00000007655. [P49817-1]
GeneID12389.
KEGGmmu:12389.
UCSCuc009azo.2. mouse. [P49817-1]

Organism-specific databases

CTD857.
MGIMGI:102709. Cav1.

Phylogenomic databases

eggNOGNOG86001.
GeneTreeENSGT00390000014924.
HOGENOMHOG000036550.
HOVERGENHBG003422.
InParanoidP49817.
KOK06278.
OMAVHTFCDP.
OrthoDBEOG7V1FSD.
TreeFamTF315736.

Gene expression databases

ArrayExpressP49817.
BgeeP49817.
CleanExMM_CAV1.
GenevestigatorP49817.

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

NextBio281122.
PROP49817.
SOURCESearch...

Entry information

Entry nameCAV1_MOUSE
AccessionPrimary (citable) accession number: P49817
Secondary accession number(s): Q8C1X7 expand/collapse secondary AC list , Q8CBP4, Q9QYH3, Q9QYH4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 148 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot