CAV1_MOUSE
ID CAV1_MOUSE Reviewed; 178 AA.
AC P49817; Q8C1X7; Q8CBP4; Q9QYH3; Q9QYH4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Caveolin-1;
GN Name=Cav1; Synonyms=Cav;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=7926819; DOI=10.1016/0378-1119(94)90087-6;
RA Tang Z., Scherer P.E., Lisanti M.P.;
RT "The primary sequence of murine caveolin reveals a conserved consensus site
RT for phosphorylation by protein kinase C.";
RL Gene 147:299-300(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=10631317; DOI=10.1016/s0014-5793(99)01730-5;
RA Kogo H., Fujimoto T.;
RT "Caveolin-1 isoforms are encoded in distinct mRNAs: identification of mouse
RT caveolin-1 mRNA variants caused by alternative transcription initiation and
RT splicing.";
RL FEBS Lett. 465:119-123(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=SWR/J;
RA Zaffaroni D., Dragani T.A.;
RT "Met gene is a candidate for the mouse pulmonary adenoma resistance 4
RT (Par4) locus.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C3H/He; TISSUE=Mesenchymal cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 5-26; 47-77 AND 165-176.
RX PubMed=7608210; DOI=10.1074/jbc.270.27.16395;
RA Scherer P.E., Tang Z., Chun M., Sargiacomo M., Lodish H.F., Lisanti M.P.;
RT "Caveolin isoforms differ in their N-terminal protein sequence and
RT subcellular distribution. Identification and epitope mapping of an isoform-
RT specific monoclonal antibody probe.";
RL J. Biol. Chem. 270:16395-16401(1995).
RN [7]
RP FUNCTION.
RX PubMed=10816572; DOI=10.1074/jbc.m002020200;
RA Galbiati F., Volonte D., Brown A.M., Weinstein D.E., Ben-Ze'ev A.,
RA Pestell R.G., Lisanti M.P.;
RT "Caveolin-1 expression inhibits Wnt/beta-catenin/Lef-1 signaling by
RT recruiting beta-catenin to caveolae membrane domains.";
RL J. Biol. Chem. 275:23368-23377(2000).
RN [8]
RP PHOSPHORYLATION AT TYR-14.
RX PubMed=12036959; DOI=10.1074/jbc.m203375200;
RA Kimura A., Mora S., Shigematsu S., Pessin J.E., Saltiel A.R.;
RT "The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-
RT 1.";
RL J. Biol. Chem. 277:30153-30158(2002).
RN [9]
RP PHOSPHORYLATION AT TYR-14.
RX PubMed=12531427; DOI=10.1016/s0898-6568(02)00090-6;
RA Sanguinetti A.R., Mastick C.C.;
RT "c-Abl is required for oxidative stress-induced phosphorylation of
RT caveolin-1 on tyrosine 14.";
RL Cell. Signal. 15:289-298(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP INTERACTION WITH SPRY1; SPRY2; SPRY3 AND SPRY4.
RX PubMed=16877379; DOI=10.1074/jbc.m603921200;
RA Cabrita M.A., Jaeggi F., Widjaja S.P., Christofori G.;
RT "A functional interaction between sprouty proteins and caveolin-1.";
RL J. Biol. Chem. 281:29201-29212(2006).
RN [12]
RP FUNCTION, INTERACTION WITH CAVIN1, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19546242; DOI=10.1083/jcb.200903053;
RA Bastiani M., Liu L., Hill M.M., Jedrychowski M.P., Nixon S.J., Lo H.P.,
RA Abankwa D., Luetterforst R., Fernandez-Rojo M., Breen M.R., Gygi S.P.,
RA Vinten J., Walser P.J., North K.N., Hancock J.F., Pilch P.F., Parton R.G.;
RT "MURC/Cavin-4 and cavin family members form tissue-specific caveolar
RT complexes.";
RL J. Cell Biol. 185:1259-1273(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND TYR-14, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP INTERACTION WITH PACSIN2, AND SUBCELLULAR LOCATION.
RX PubMed=21610094; DOI=10.1242/jcs.086264;
RA Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.;
RT "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting.";
RL J. Cell Sci. 124:2032-2040(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-5, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [17]
RP FUNCTION.
RX PubMed=30188967; DOI=10.1093/abbs/gmy105;
RA Wei Z., Liu T., Lei J., Wu Y., Wang S., Liao K.;
RT "Fam198a, a member of secreted kinase, secrets through caveolae biogenesis
RT pathway.";
RL Acta Biochim. Biophys. Sin. 50:968-975(2018).
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes
CC (By similarity). Forms a stable heterooligomeric complex with CAV2 that
CC targets to lipid rafts and drives caveolae formation. Mediates the
CC recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae
CC (PubMed:19546242). Interacts directly with G-protein alpha subunits and
CC can functionally regulate their activity (By similarity). Involved in
CC the costimulatory signal essential for T-cell receptor (TCR)-mediated
CC T-cell activation. Its binding to DPP4 induces T-cell proliferation and
CC NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By
CC similarity). Recruits CTNNB1 to caveolar membranes and may regulate
CC CTNNB1-mediated signaling through the Wnt pathway (PubMed:10816572).
CC Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating
CC the internalization of TGFBR1 from membrane rafts leading to its
CC subsequent degradation (By similarity). {ECO:0000250|UniProtKB:Q03135,
CC ECO:0000269|PubMed:10816572, ECO:0000269|PubMed:19546242}.
CC -!- SUBUNIT: Homooligomer. Interacts (via the N-terminus) with DPP4; the
CC interaction is direct. Forms a stable heterooligomeric complex with
CC CAV2 that targets to lipid rafts and drives caveolae formation.
CC Interacts with BMX, BTK, CTNNB1, CDH1, GLIPR2, JUP, NOSTRIN, SNAP25 and
CC STX1A. Interacts with SLC7A9. Interacts with TGFBR1 (By similarity).
CC Interacts with CTNNB1, CDH1 and JUP. Interacts with PACSIN2; this
CC interaction induces membrane tubulation (PubMed:21610094). Interacts
CC with CAVIN3 (via leucine-zipper domain) in a cholesterol-sensitive
CC manner. Interacts with EHD2 in a cholesterol-dependent manner (By
CC similarity). Interacts with CAVIN1 (PubMed:19546242). Forms a ternary
CC complex with UBXN6 and VCP; mediates CAV1 targeting to lysosomes for
CC degradation (By similarity). Interacts with ABCG1; this interaction
CC regulates ABCG1-mediated cholesterol efflux (By similarity). Interacts
CC with NEU3; this interaction enhances NEU3 sialidase activity within
CC caveola. Interacts (via C-terminus) with SPRY1, SPRY2 (via C-terminus),
CC SPRY3, and SPRY4 (PubMed:16877379). {ECO:0000250|UniProtKB:P41350,
CC ECO:0000250|UniProtKB:Q03135, ECO:0000250|UniProtKB:Q2IBA5,
CC ECO:0000269|PubMed:16877379, ECO:0000269|PubMed:19546242,
CC ECO:0000269|PubMed:21610094}.
CC -!- INTERACTION:
CC P49817; P15208: Insr; NbExp=2; IntAct=EBI-1161338, EBI-6999015;
CC P49817; Q64729: Tgfbr1; NbExp=4; IntAct=EBI-1161338, EBI-2899393;
CC P49817; Q07820: MCL1; Xeno; NbExp=3; IntAct=EBI-1161338, EBI-1003422;
CC P49817; P22307: SCP2; Xeno; NbExp=3; IntAct=EBI-1161338, EBI-1050999;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Membrane, caveola
CC {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:21610094}; Peripheral
CC membrane protein {ECO:0000269|PubMed:21610094}. Membrane raft
CC {ECO:0000250|UniProtKB:Q03135}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:P33724}. Note=Colocalized with DPP4 in membrane
CC rafts. Potential hairpin-like structure in the membrane. Membrane
CC protein of caveolae (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P49817-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49817-2; Sequence=VSP_018693;
CC -!- TISSUE SPECIFICITY: Adipose tissue, lung, heart, skeletal muscle,
CC stomach, small bowel, kidney, spleen and testis (at protein level).
CC {ECO:0000269|PubMed:19546242}.
CC -!- PTM: The N-terminus of both isoforms are blocked.
CC -!- PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress.
CC {ECO:0000269|PubMed:12036959, ECO:0000269|PubMed:12531427}.
CC -!- PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or
CC polyubiquitination. Monoubiquitination of N-terminal lysines promotes
CC integration in a ternary complex with UBXN6 and VCP which promotes
CC oligomeric CAV1 targeting to lysosomes for degradation.
CC {ECO:0000250|UniProtKB:Q03135}.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR EMBL; U07645; AAA85784.1; -; mRNA.
DR EMBL; AB029929; BAA89461.1; -; mRNA.
DR EMBL; AB029930; BAA89462.1; -; mRNA.
DR EMBL; AB029931; BAA89463.1; -; Genomic_DNA.
DR EMBL; AY439333; AAR99702.1; -; mRNA.
DR EMBL; AK003489; BAB22817.1; -; mRNA.
DR EMBL; AK028738; BAC26091.1; -; mRNA.
DR EMBL; AK035592; BAC29118.1; -; mRNA.
DR EMBL; AK090074; BAC41079.1; -; mRNA.
DR EMBL; BC038280; AAH38280.1; -; mRNA.
DR EMBL; BC052859; AAH52859.1; -; mRNA.
DR CCDS; CCDS19924.1; -. [P49817-1]
DR CCDS; CCDS57410.1; -. [P49817-2]
DR PIR; I48976; I48976.
DR RefSeq; NP_001229993.1; NM_001243064.1. [P49817-2]
DR RefSeq; NP_031642.1; NM_007616.4. [P49817-1]
DR RefSeq; XP_006505037.1; XM_006504974.1. [P49817-1]
DR RefSeq; XP_006505038.1; XM_006504975.1. [P49817-2]
DR RefSeq; XP_006505039.1; XM_006504976.1. [P49817-2]
DR AlphaFoldDB; P49817; -.
DR BioGRID; 198514; 12.
DR CORUM; P49817; -.
DR DIP; DIP-35140N; -.
DR IntAct; P49817; 18.
DR MINT; P49817; -.
DR STRING; 10090.ENSMUSP00000007799; -.
DR iPTMnet; P49817; -.
DR PhosphoSitePlus; P49817; -.
DR SwissPalm; P49817; -.
DR jPOST; P49817; -.
DR MaxQB; P49817; -.
DR PaxDb; P49817; -.
DR PeptideAtlas; P49817; -.
DR PRIDE; P49817; -.
DR ProteomicsDB; 265553; -. [P49817-1]
DR ProteomicsDB; 265554; -. [P49817-2]
DR Antibodypedia; 3530; 1199 antibodies from 47 providers.
DR DNASU; 12389; -.
DR Ensembl; ENSMUST00000007799; ENSMUSP00000007799; ENSMUSG00000007655. [P49817-1]
DR Ensembl; ENSMUST00000115453; ENSMUSP00000111113; ENSMUSG00000007655. [P49817-2]
DR Ensembl; ENSMUST00000115454; ENSMUSP00000111114; ENSMUSG00000007655. [P49817-2]
DR Ensembl; ENSMUST00000115456; ENSMUSP00000111116; ENSMUSG00000007655. [P49817-1]
DR GeneID; 12389; -.
DR KEGG; mmu:12389; -.
DR UCSC; uc009azo.2; mouse. [P49817-1]
DR CTD; 857; -.
DR MGI; MGI:102709; Cav1.
DR VEuPathDB; HostDB:ENSMUSG00000007655; -.
DR eggNOG; ENOG502QUK5; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_102582_0_0_1; -.
DR InParanoid; P49817; -.
DR OMA; SIRINMQ; -.
DR OrthoDB; 1468974at2759; -.
DR PhylomeDB; P49817; -.
DR TreeFam; TF315736; -.
DR Reactome; R-MMU-203615; eNOS activation.
DR Reactome; R-MMU-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 12389; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Cav1; mouse.
DR PRO; PR:P49817; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P49817; protein.
DR Bgee; ENSMUSG00000007655; Expressed in left lung lobe and 232 other tissues.
DR ExpressionAtlas; P49817; baseline and differential.
DR Genevisible; P49817; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR GO; GO:0002095; C:caveolar macromolecular signaling complex; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:HGNC-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0070320; F:inward rectifier potassium channel inhibitor activity; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:BHF-UCL.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
DR GO; GO:0016504; F:peptidase activator activity; IMP:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; IGI:BHF-UCL.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0070836; P:caveola assembly; IDA:MGI.
DR GO; GO:0072584; P:caveolin-mediated endocytosis; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISO:MGI.
DR GO; GO:0071455; P:cellular response to hyperoxia; ISO:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IGI:BHF-UCL.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:MGI.
DR GO; GO:0090398; P:cellular senescence; ISO:MGI.
DR GO; GO:0033344; P:cholesterol efflux; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; TAS:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0002067; P:glandular epithelial cell differentiation; IMP:MGI.
DR GO; GO:0038016; P:insulin receptor internalization; IMP:CACAO.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0019915; P:lipid storage; IMP:MGI.
DR GO; GO:0032507; P:maintenance of protein location in cell; ISO:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:0060056; P:mammary gland involution; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR GO; GO:0046785; P:microtubule polymerization; ISO:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:2001258; P:negative regulation of cation channel activity; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IMP:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:1903609; P:negative regulation of inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IMP:CACAO.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IMP:MGI.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IMP:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:1900085; P:negative regulation of peptidyl-tyrosine autophosphorylation; IMP:BHF-UCL.
DR GO; GO:0048550; P:negative regulation of pinocytosis; ISO:MGI.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IMP:BHF-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; IDA:MGI.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IDA:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI.
DR GO; GO:0033484; P:nitric oxide homeostasis; IMP:MGI.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:BHF-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:MGI.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0009967; P:positive regulation of signal transduction; ISO:MGI.
DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:MGI.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IMP:MGI.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:MGI.
DR GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; ISO:MGI.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:MGI.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISO:MGI.
DR GO; GO:0052547; P:regulation of peptidase activity; IMP:MGI.
DR GO; GO:1900027; P:regulation of ruffle assembly; ISO:MGI.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IMP:MGI.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR GO; GO:0003057; P:regulation of the force of heart contraction by chemical signal; IGI:MGI.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0009617; P:response to bacterium; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
DR GO; GO:0043627; P:response to estrogen; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0002931; P:response to ischemia; IMP:MGI.
DR GO; GO:0009612; P:response to mechanical stimulus; ISO:MGI.
DR GO; GO:0032570; P:response to progesterone; ISO:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IMP:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0042310; P:vasoconstriction; IMP:MGI.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
DR InterPro; IPR015504; CAV-1.
DR InterPro; IPR001612; Caveolin.
DR InterPro; IPR018361; Caveolin_CS.
DR PANTHER; PTHR10844; PTHR10844; 1.
DR PANTHER; PTHR10844:SF18; PTHR10844:SF18; 1.
DR Pfam; PF01146; Caveolin; 1.
DR PROSITE; PS01210; CAVEOLIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Cell membrane;
KW Direct protein sequencing; Golgi apparatus; Isopeptide bond; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..178
FT /note="Caveolin-1"
FT /id="PRO_0000004766"
FT TOPO_DOM 2..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..94
FT /note="Required for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT REGION 82..94
FT /note="Interaction with CAVIN3"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT REGION 131..142
FT /note="Interacts with SPRY1, SPRY2, SPRY3 and SPRY4"
FT /evidence="ECO:0000269|PubMed:16877379"
FT REGION 149..160
FT /note="Interacts with SPRY1, SPRY2, and SPRY4"
FT /evidence="ECO:0000269|PubMed:16877379"
FT REGION 167..178
FT /note="Interacts with SPRY1, SPRY2, SPRY3 and SPRY4"
FT /evidence="ECO:0000269|PubMed:16877379"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41350"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 6
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 14
FT /note="Phosphotyrosine; by ABL1 and INSR"
FT /evidence="ECO:0000269|PubMed:12036959,
FT ECO:0000269|PubMed:12531427, ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT LIPID 133
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 143
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 156
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 47
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10631317,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018693"
FT CONFLICT 170
FT /note="I -> F (in Ref. 4; BAC29118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20539 MW; CF88FE9B1D3D67AE CRC64;
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADEVTEKQ VYDAHTKEID LVNRDPKHLN
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSTIFGIP MALIWGIYFA
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTFCDPLF EAIGKIFSNI RISTQKEI
