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UniProtKB/Swiss-Prot entry Q03135


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CAV1_HUMAN
Primary accession number Q03135
Secondary accession numbers Q9UGP1 Q9UNG1 Q9UQH6
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 105)
Name and origin of the protein
Protein name Caveolin-1
Synonyms None
Gene name
Name: CAV1
Synonyms: CAV
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
DOI=10.1016/0014-5793(92)81458-X; PubMed=1360410 [NCBI, ExPASy, EBI, Israel, Japan]
Glenney J.R. Jr.;
"The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles.";
FEBS Lett. 314:45-48(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/sj.onc.1202491; PubMed=10086342 [NCBI, ExPASy, EBI, Israel, Japan]
Hurlstone A.F., Reid G., Reeves J.R., Fraser J., Strathdee G., Rahilly M., Parkinson E.K., Black D.M.;
"Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines.";
Oncogene 18:1881-1890(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0014-5793(99)00365-8; PubMed=10218480 [NCBI, ExPASy, EBI, Israel, Japan]
Engelman J.A., Zhang X.L., Lisanti M.P.;
"Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines.";
FEBS Lett. 448:221-230(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-66, SUBCELLULAR LOCATION, ACETYLATION AT SER-2, AND PHOSPHORYLATION.
TISSUE=Adipose tissue;
DOI=10.1016/j.bbrc.2004.05.196; PubMed=15219854 [NCBI, ExPASy, EBI, Israel, Japan]
Vainonen J.P., Aboulaich N., Turkina M.V., Stralfors P., Vener A.V.;
"N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes.";
Biochem. Biophys. Res. Commun. 320:480-486(2004).
[7]
PROTEIN SEQUENCE OF 58-65.
TISSUE=Adipocyte;
DOI=10.1042/BJ20040647; PubMed=15242332 [NCBI, ExPASy, EBI, Israel, Japan]
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[8]
INTERACTION WITH GLIPR2.
TISSUE=Brain;
PubMed=11865038 [NCBI, ExPASy, EBI, Israel, Japan]
Eberle H.B., Serrano R.L., Fuellekrug J., Schlosser A., Lehmann W.D., Lottspeich F., Kaloyanova D., Wieland F.T., Helms J.B.;
"Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex.";
J. Cell Sci. 115:827-838(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6; TYR-14 AND TYR-25, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-14, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
INTERACTION WITH NOSTRIN.
DOI=10.1091/mbc.E05-08-0709; PubMed=16807357 [NCBI, ExPASy, EBI, Israel, Japan]
Schilling K., Opitz N., Wiesenthal A., Oess S., Tikkanen R., Mueller-Esterl W., Icking A.;
"Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN.";
Mol. Biol. Cell 17:3870-3880(2006).
[13]
INTERACTION WITH ROTAVIRUS A NSP4.
DOI=10.1128/JVI.80.6.2842-2854.2006; PubMed=16501093 [NCBI, ExPASy, EBI, Israel, Japan]
Parr R.D., Storey S.M., Mitchell D.M., McIntosh A.L., Zhou M., Mir K.D., Ball J.M.;
"The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1.";
J. Virol. 80:2842-2854(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-14, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
VARIANT LEU-132.
PubMed=12368209 [NCBI, ExPASy, EBI, Israel, Japan]
Lee H., Park D.S., Razani B., Russell R.G., Pestell R.G., Lisanti M.P.;
"Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia.";
Am. J. Pathol. 161:1357-1369(2002).
[17]
INVOLVEMENT IN CONGENITAL GENERALIZED LIPODYSTROPHY TYPE 3.
DOI=10.1210/jc.2007-1328; PubMed=18211975 [NCBI, ExPASy, EBI, Israel, Japan]
Kim C.A., Delepine M., Boutet E., El Mourabit H., Le Lay S., Meier M., Nemani M., Bridel E., Leite C.C., Bertola D.R., Semple R.K., O'Rahilly S., Dugail I., Capeau J., Lathrop M., Magre J.;
"Association of a homozygous nonsense caveolin-1 mutation with Berardinelli-Seip congenital lipodystrophy.";
J. Clin. Endocrinol. Metab. 93:1129-1134(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z18951; CAA79476.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF095593; AAD23745.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF095591; AAD23745.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF095592; AAD23745.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133269; CAB63654.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125348; AAD34722.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007143; AAP35807.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009685; AAH09685.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC082246; AAH82246.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00009236; -.
IPI00759683; -.
PIR S26884; S26884.
RefSeq NP_001744.2; -.
UniGene Hs.74034
3D structure databases
ModBase Q03135.
Protein-protein interaction databases
DIP DIP:5960N; -.
IntAct Q03135; 15.
PTM databases
PhosphoSite Q03135; -.
Enzyme and pathway databases
Pathway_Interaction_DB insulin_pathway; Insulin Pathway.
pdgfrapathway; PDGFR-alpha signaling pathway.
ptp1bpathway; Signaling events mediated by PTP1B.
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
tgfbrpathway; TGF-beta receptor signaling.
tnfpathway; TNF receptor signaling pathway.
vegfr1_pathway; VEGFR1 specific signals.
Reactome REACT_12508; Metabolism of nitric oxide.
REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC07P115952; -.
H-InvDB HIX0007018; -.
HGNC HGNC:1527; CAV1.
GenAtlas CAV1.
HPA CAB003791; -.
MIM 601047; gene. [NCBI / EBI]
612526; phenotype. [NCBI / EBI]
Orphanet 528; Lipodystrophy, Berardinelli type.
PharmGKB PA26107; -.
Gene expression databases
ArrayExpress Q03135; -.
Bgee Q03135; -.
CleanEx HS_CAV1; -.
GermOnline ENSG00000105974; Homo sapiens.
Ontologies
GO
GO:0005901; Cellular component: caveola (inferred from direct assay from UniProtKB).
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from HGNC).
GO:0000139; Cellular component: Golgi membrane (inferred from direct assay from HGNC).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005811; Cellular component: lipid particle (inferred from experiment from Reactome).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0015485; Molecular function: cholesterol binding (traceable author statement from HGNC).
GO:0050998; Molecular function: nitric-oxide synthase binding (inferred from physical interaction from UniProtKB).
GO:0016504; Molecular function: peptidase activator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0032947; Molecular function: protein complex scaffold (traceable author statement from UniProtKB).
GO:0006816; Biological process: calcium ion transport (inferred from sequence or structural similarity from UniProtKB).
GO:0042632; Biological process: cholesterol homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0030301; Biological process: cholesterol transport (traceable author statement from HGNC).
GO:0051480; Biological process: cytosolic calcium ion homeostasis (inferred from direct assay from UniProtKB).
GO:0006897; Biological process: endocytosis (inferred from sequence or structural similarity from UniProtKB).
GO:0000188; Biological process: inactivation of MAPK activity (inferred from sequence or structural similarity from UniProtKB).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0019915; Biological process: lipid storage (inferred from sequence or structural similarity from UniProtKB).
GO:0060056; Biological process: mammary gland involution (inferred from sequence or structural similarity from UniProtKB).
GO:0051899; Biological process: membrane depolarization (inferred from sequence or structural similarity from UniProtKB).
GO:0001937; Biological process: negative regulation of endothelial cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0030857; Biological process: negative regulation of epithelial cell differentiation (inferred from sequence or structural similarity from UniProtKB).
GO:0046426; Biological process: negative regulation of JAK-STAT cascade (inferred from sequence or structural similarity from UniProtKB).
GO:0043409; Biological process: negative regulation of MAPKKK cascade (inferred from sequence or structural similarity from UniProtKB).
GO:0045019; Biological process: negative regulation of nitric oxide biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
GO:0045908; Biological process: negative regulation of vasodilation (inferred from sequence or structural similarity from UniProtKB).
GO:0033484; Biological process: nitric oxide homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0010524; Biological process: positive regulation of calcium ion transport into cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0048554; Biological process: positive regulation of metalloenzyme activity (inferred from sequence or structural similarity from UniProtKB).
GO:0045907; Biological process: positive regulation of vasoconstriction (inferred from sequence or structural similarity from UniProtKB).
GO:0051260; Biological process: protein homooligomerization (inferred from sequence or structural similarity from UniProtKB).
GO:0008104; Biological process: protein localization (inferred from sequence or structural similarity from UniProtKB).
GO:0030193; Biological process: regulation of blood coagulation (inferred from mutant phenotype from UniProtKB).
GO:0019217; Biological process: regulation of fatty acid metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0052547; Biological process: regulation of peptidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006940; Biological process: regulation of smooth muscle contraction (inferred from sequence or structural similarity from UniProtKB).
GO:0051592; Biological process: response to calcium ion (inferred from sequence or structural similarity from UniProtKB).
GO:0043627; Biological process: response to estrogen stimulus (inferred from direct assay from MGI).
GO:0001666; Biological process: response to hypoxia (inferred from sequence or structural similarity from UniProtKB).
GO:0032570; Biological process: response to progesterone stimulus (inferred from direct assay from MGI).
GO:0007519; Biological process: skeletal muscle tissue development (inferred from sequence or structural similarity from UniProtKB).
GO:0006641; Biological process: triglyceride metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0001570; Biological process: vasculogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0016050; Biological process: vesicle organization (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001612; Caveolin.
IPR015504; Caveolin_1.
IPR018361; Caveolin_CS.
Graphical view of domain structure.
PANTHER PTHR10844; Caveolin; 1.
PTHR10844:SF5; Caveolin_1; 1.
Pfam PF01146; Caveolin; 1.
Pfam graphical view of domain structure.
PROSITE PS01210; CAVEOLIN; 1.
Proteomic databases
PeptideAtlas Q03135; -.
PRIDE Q03135; -.
Genome annotation databases
Ensembl ENSG00000105974; Homo sapiens. [Contig view]
GeneID 857; -.
KEGG hsa:857; -.
Phylogenomic databases
HOVERGEN Q03135; -.
OMA Q03135; VHTFCDP.
Other
NextBio 3556; -.
SOURCE CAV1; Homo sapiens.
ProtoNet Q03135.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Alternative initiation; Cell membrane; Congenital generalized lipodystrophy; Direct protein sequencing; Disease mutation; Golgi apparatus; Host-virus interaction; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   178  177     Caveolin-1. PRO_0000004764
TOPO_DOM   2   104  103     Cytoplasmic (Potential). 
TRANSMEM   105   125  21     Potential. 
TOPO_DOM   126   178  53     Cytoplasmic (Potential). 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   6     6        Phosphotyrosine. 
MOD_RES   14    14        Phosphotyrosine. 
MOD_RES   25    25        Phosphotyrosine. 
MOD_RES   37    37        Phosphoserine. 
LIPID   133   133        S-palmitoyl cysteine (By similarity). 
LIPID   143   143        S-palmitoyl cysteine (By similarity). 
LIPID   156   156        S-palmitoyl cysteine (By similarity). 
VAR_SEQ   1    31        Missing (in isoform Beta). VSP_018692
VARIANT   132   132  1     P -> L (in breast cancer; seems to form misfolded oligomers that are retained within the Golgi complex and are not targeted to caveolae or the plasma membrane). VAR_015103 
CONFLICT   82    82        D -> H (in Ref. 1; CAA79476). 
CONFLICT   144   144        I -> T (in Ref. 1; CAA79476). 
Sequence information
Length: 178 AA [This is the length of the unprocessed precursor] Molecular weight: 20472 Da [This is the MW of the unprocessed precursor] CRC64: 2424DE9B5E6521D5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADELSEKQ VYDAHTKEID LVNRDPKHLN 

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

       130        140        150        160        170 
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTVCDPLF EAVGKIFSNV RINLQKEI 

Q03135 in FASTA format

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