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Protein

Caveolin-1

Gene

Cav1

Organism
Mus musculus (Mouse)
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. 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.1 Publication

GO - Molecular functioni

  • ATPase binding Source: MGI
  • enzyme binding Source: MGI
  • identical protein binding Source: MGI
  • inward rectifier potassium channel inhibitor activity Source: MGI
  • ion channel binding Source: MGI
  • nitric-oxide synthase binding Source: BHF-UCL
  • peptidase activator activity Source: MGI
  • protein binding, bridging Source: BHF-UCL
  • protein complex scaffold Source: BHF-UCL
  • protein heterodimerization activity Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL
  • receptor binding Source: MGI
  • structural molecule activity Source: MGI

GO - Biological processi

  • angiogenesis Source: MGI
  • angiotensin-activated signaling pathway involved in heart process Source: BHF-UCL
  • apoptotic signaling pathway Source: MGI
  • calcium ion homeostasis Source: MGI
  • calcium ion transport Source: MGI
  • caveola assembly Source: BHF-UCL
  • caveolin-mediated endocytosis Source: MGI
  • cellular calcium ion homeostasis Source: MGI
  • cellular response to exogenous dsRNA Source: MGI
  • cellular response to hyperoxia Source: MGI
  • cellular response to mechanical stimulus Source: Ensembl
  • cellular response to peptide hormone stimulus Source: BHF-UCL
  • cellular response to starvation Source: Ensembl
  • cellular response to transforming growth factor beta stimulus Source: MGI
  • cellular senescence Source: Ensembl
  • cholesterol efflux Source: Ensembl
  • cholesterol homeostasis Source: MGI
  • cytosolic calcium ion homeostasis Source: MGI
  • endocytosis Source: MGI
  • inactivation of MAPK activity Source: MGI
  • lactation Source: MGI
  • lipid storage Source: MGI
  • mammary gland development Source: MGI
  • mammary gland involution Source: MGI
  • MAPK cascade Source: MGI
  • membrane depolarization Source: MGI
  • microtubule polymerization Source: Ensembl
  • negative regulation of anoikis Source: UniProtKB
  • negative regulation of BMP signaling pathway Source: MGI
  • negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  • negative regulation of cation channel activity Source: Ensembl
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of cytokine-mediated signaling pathway Source: MGI
  • negative regulation of endothelial cell proliferation Source: MGI
  • negative regulation of epithelial cell differentiation Source: MGI
  • negative regulation of ERK1 and ERK2 cascade Source: Ensembl
  • negative regulation of JAK-STAT cascade Source: MGI
  • negative regulation of MAPK cascade Source: MGI
  • negative regulation of MAP kinase activity Source: MGI
  • negative regulation of muscle cell apoptotic process Source: Ensembl
  • negative regulation of necroptotic process Source: CACAO
  • negative regulation of neuron differentiation Source: Ensembl
  • negative regulation of nitric oxide biosynthetic process Source: MGI
  • negative regulation of nitric-oxide synthase activity Source: MGI
  • negative regulation of peptidyl-serine phosphorylation Source: MGI
  • negative regulation of peptidyl-tyrosine autophosphorylation Source: BHF-UCL
  • negative regulation of pinocytosis Source: MGI
  • negative regulation of potassium ion transmembrane transport Source: MGI
  • negative regulation of protein binding Source: MGI
  • negative regulation of protein tyrosine kinase activity Source: BHF-UCL
  • negative regulation of protein ubiquitination Source: UniProtKB
  • negative regulation of signal transduction Source: MGI
  • negative regulation of smooth muscle cell proliferation Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of tyrosine phosphorylation of Stat5 protein Source: MGI
  • nitric oxide homeostasis Source: MGI
  • organ regeneration Source: Ensembl
  • positive regulation of calcium ion transport into cytosol Source: BHF-UCL
  • positive regulation of canonical Wnt signaling pathway Source: MGI
  • positive regulation of cell adhesion molecule production Source: MGI
  • positive regulation of endocytosis Source: Ensembl
  • positive regulation of endothelial cell proliferation Source: Ensembl
  • positive regulation of extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of gap junction assembly Source: BHF-UCL
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of intrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of metalloenzyme activity Source: MGI
  • positive regulation of microtubule polymerization Source: Ensembl
  • positive regulation of peptidase activity Source: GOC
  • positive regulation of peptidyl-serine phosphorylation Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • positive regulation of toll-like receptor 3 signaling pathway Source: MGI
  • positive regulation of vasoconstriction Source: MGI
  • posttranscriptional regulation of gene expression Source: BHF-UCL
  • protein homooligomerization Source: MGI
  • protein localization Source: MGI
  • protein oligomerization Source: MGI
  • receptor internalization involved in canonical Wnt signaling pathway Source: MGI
  • receptor-mediated endocytosis of virus by host cell Source: MGI
  • regulation of blood coagulation Source: MGI
  • regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  • regulation of fatty acid metabolic process Source: MGI
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • regulation of inward rectifier potassium channel activity Source: MGI
  • regulation of membrane repolarization during action potential Source: MGI
  • regulation of peptidase activity Source: MGI
  • regulation of smooth muscle contraction Source: MGI
  • regulation of the force of heart contraction Source: MGI
  • regulation of the force of heart contraction by chemical signal Source: MGI
  • regulation of ventricular cardiac muscle cell action potential Source: BHF-UCL
  • response to calcium ion Source: BHF-UCL
  • response to drug Source: Ensembl
  • response to estrogen Source: MGI
  • response to gamma radiation Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to hypoxia Source: MGI
  • response to ischemia Source: MGI
  • response to nutrient Source: Ensembl
  • response to progesterone Source: MGI
  • skeletal muscle tissue development Source: MGI
  • T cell costimulation Source: UniProtKB
  • triglyceride metabolic process Source: MGI
  • vasculogenesis Source: MGI
  • vasoconstriction Source: MGI
  • wound healing Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_316390. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_321965. VEGFR2 mediated vascular permeability.
REACT_323105. Basigin interactions.
REACT_342348. eNOS activation.
REACT_351979. NOSTRIN mediated eNOS trafficking.

Names & Taxonomyi

Protein namesi
Recommended name:
Caveolin-1
Gene namesi
Name:Cav1
Synonyms:Cav
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:102709. Cav1.

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

  • acrosomal membrane Source: MGI
  • apical plasma membrane Source: MGI
  • basal plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: MGI
  • caveola Source: UniProtKB
  • cell cortex Source: MGI
  • cell surface Source: Ensembl
  • cilium Source: MGI
  • cytoplasmic vesicle Source: MGI
  • cytosol Source: MGI
  • endoplasmic reticulum Source: HGNC
  • endosome Source: UniProtKB
  • focal adhesion Source: MGI
  • Golgi apparatus Source: MGI
  • Golgi membrane Source: HGNC
  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: MGI
  • intracellular Source: MGI
  • lipid particle Source: Ensembl
  • membrane Source: MGI
  • membrane raft Source: MGI
  • mitochondrion Source: Ensembl
  • perinuclear region of cytoplasm Source: MGI
  • peroxisomal membrane Source: Ensembl
  • plasma membrane Source: MGI
  • protein complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 178177Caveolin-1PRO_0000004766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei5 – 51N6-acetyllysine1 Publication
Modified residuei6 – 61PhosphotyrosineBy similarity
Modified residuei14 – 141Phosphotyrosine; by ABL1 and INSR2 Publications
Modified residuei25 – 251PhosphotyrosineBy similarity
Lipidationi133 – 1331S-palmitoyl cysteineBy similarity
Lipidationi143 – 1431S-palmitoyl cysteineBy similarity
Lipidationi156 – 1561S-palmitoyl cysteineBy similarity

Post-translational modificationi

The N-terminus of both isoforms are blocked.
Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress.2 Publications

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP49817.
PaxDbiP49817.
PRIDEiP49817.

PTM databases

PhosphoSiteiP49817.

Expressioni

Gene expression databases

BgeeiP49817.
CleanExiMM_CAV1.
ExpressionAtlasiP49817. baseline and differential.
GenevisibleiP49817. MM.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MCL1Q078203EBI-1161338,EBI-1003422From a different organism.
SCP2P223073EBI-1161338,EBI-1050999From a different organism.

Protein-protein interaction databases

BioGridi198514. 9 interactions.
DIPiDIP-35140N.
IntActiP49817. 11 interactions.
MINTiMINT-1542313.
STRINGi10090.ENSMUSP00000007799.

Family & Domainsi

Sequence similaritiesi

Belongs to the caveolin family.Curated

Phylogenomic databases

eggNOGiNOG86001.
GeneTreeiENSGT00390000014924.
HOGENOMiHOG000036550.
HOVERGENiHBG003422.
InParanoidiP49817.
KOiK06278.
OMAiIYVHTFC.
OrthoDBiEOG7V1FSD.
PhylomeDBiP49817.
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 1 (identifier: P49817-1) [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 AMADEVTEKQ VYDAHTKEID
60 70 80 90 100
LVNRDPKHLN DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY
110 120 130 140 150
RLLSTIFGIP MALIWGIYFA ILSFLHIWAV VPCIKSFLIE IQCISRVYSI
160 170
YVHTFCDPLF EAIGKIFSNI RISTQKEI
Length:178
Mass (Da):20,539
Last modified:October 1, 1996 - v1
Checksum:iCF88FE9B1D3D67AE
GO
Isoform 2 (identifier: P49817-2) [UniParc]FASTAAdd to basket

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

Show »
Length:147
Mass (Da):17,090
Checksum:iF1D1A06351AF6C3C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701I → F in BAC29118 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform 2. 2 PublicationsVSP_018693Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19924.1. [P49817-1]
CCDS57410.1. [P49817-2]
PIRiI48976.
RefSeqiNP_001229993.1. NM_001243064.1. [P49817-2]
NP_031642.1. NM_007616.4. [P49817-1]
XP_006505037.1. XM_006504974.1. [P49817-1]
XP_006505038.1. XM_006504975.1. [P49817-2]
XP_006505039.1. XM_006504976.1. [P49817-2]
UniGeneiMm.28278.

Genome annotation databases

EnsembliENSMUST00000007799; ENSMUSP00000007799; ENSMUSG00000007655. [P49817-1]
ENSMUST00000115453; ENSMUSP00000111113; ENSMUSG00000007655. [P49817-2]
ENSMUST00000115454; ENSMUSP00000111114; ENSMUSG00000007655. [P49817-2]
ENSMUST00000115456; ENSMUSP00000111116; ENSMUSG00000007655. [P49817-1]
GeneIDi12389.
KEGGimmu:12389.
UCSCiuc009azo.2. mouse. [P49817-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19924.1. [P49817-1]
CCDS57410.1. [P49817-2]
PIRiI48976.
RefSeqiNP_001229993.1. NM_001243064.1. [P49817-2]
NP_031642.1. NM_007616.4. [P49817-1]
XP_006505037.1. XM_006504974.1. [P49817-1]
XP_006505038.1. XM_006504975.1. [P49817-2]
XP_006505039.1. XM_006504976.1. [P49817-2]
UniGeneiMm.28278.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198514. 9 interactions.
DIPiDIP-35140N.
IntActiP49817. 11 interactions.
MINTiMINT-1542313.
STRINGi10090.ENSMUSP00000007799.

PTM databases

PhosphoSiteiP49817.

Proteomic databases

MaxQBiP49817.
PaxDbiP49817.
PRIDEiP49817.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007799; ENSMUSP00000007799; ENSMUSG00000007655. [P49817-1]
ENSMUST00000115453; ENSMUSP00000111113; ENSMUSG00000007655. [P49817-2]
ENSMUST00000115454; ENSMUSP00000111114; ENSMUSG00000007655. [P49817-2]
ENSMUST00000115456; ENSMUSP00000111116; ENSMUSG00000007655. [P49817-1]
GeneIDi12389.
KEGGimmu:12389.
UCSCiuc009azo.2. mouse. [P49817-1]

Organism-specific databases

CTDi857.
MGIiMGI:102709. Cav1.

Phylogenomic databases

eggNOGiNOG86001.
GeneTreeiENSGT00390000014924.
HOGENOMiHOG000036550.
HOVERGENiHBG003422.
InParanoidiP49817.
KOiK06278.
OMAiIYVHTFC.
OrthoDBiEOG7V1FSD.
PhylomeDBiP49817.
TreeFamiTF315736.

Enzyme and pathway databases

ReactomeiREACT_316390. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_321965. VEGFR2 mediated vascular permeability.
REACT_323105. Basigin interactions.
REACT_342348. eNOS activation.
REACT_351979. NOSTRIN mediated eNOS trafficking.

Miscellaneous databases

NextBioi281122.
PROiP49817.
SOURCEiSearch...

Gene expression databases

BgeeiP49817.
CleanExiMM_CAV1.
ExpressionAtlasiP49817. baseline and differential.
GenevisibleiP49817. MM.

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. "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 1).
    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 1 AND 2).
  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 1).
    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.
    , 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 1 AND 2).
    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 1).
    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.

Entry informationi

Entry nameiCAV1_MOUSE
AccessioniPrimary (citable) accession number: P49817
Secondary accession number(s): Q8C1X7
, Q8CBP4, Q9QYH3, Q9QYH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 164 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.