CAV3_MOUSE
ID CAV3_MOUSE Reviewed; 151 AA.
AC P51637;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Caveolin-3 {ECO:0000312|MGI:MGI:107570};
DE AltName: Full=M-caveolin;
GN Name=Cav3 {ECO:0000312|MGI:MGI:107570};
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=8521953; DOI=10.1016/0014-5793(95)01256-7;
RA Way M., Parton R.G.;
RT "M-caveolin, a muscle-specific caveolin-related protein.";
RL FEBS Lett. 376:108-112(1995).
RN [2]
RP ERRATUM OF PUBMED:8521953.
RX PubMed=8549793; DOI=10.1016/0014-5793(96)82884-5;
RA Way M., Parton R.G.;
RL FEBS Lett. 378:108-112(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP FUNCTION, INTERACTION WITH TRIM72, AND MUTAGENESIS OF ARG-27 AND PRO-105.
RX PubMed=19380584; DOI=10.1074/jbc.m109.009589;
RA Cai C., Weisleder N., Ko J.-K., Komazaki S., Sunada Y., Nishi M.,
RA Takeshima H., Ma J.;
RT "Membrane repair defects in muscular dystrophy are linked to altered
RT interaction between MG53, caveolin-3, and dysferlin.";
RL J. Biol. Chem. 284:15894-15902(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
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 [6]
RP INTERACTION WITH MUSK.
RX PubMed=19940021; DOI=10.1091/mbc.e09-05-0381;
RA Hezel M., de Groat W.C., Galbiati F.;
RT "Caveolin-3 promotes nicotinic acetylcholine receptor clustering and
RT regulates neuromuscular junction activity.";
RL Mol. Biol. Cell 21:302-310(2010).
RN [7]
RP INTERACTION WITH BVES, AND SUBCELLULAR LOCATION.
RX PubMed=24066022; DOI=10.1371/journal.pone.0071100;
RA Alcalay Y., Hochhauser E., Kliminski V., Dick J., Zahalka M.A., Parnes D.,
RA Schlesinger H., Abassi Z., Shainberg A., Schindler R.F., Brand T.,
RA Kessler-Icekson G.;
RT "Popeye domain containing 1 (Popdc1/Bves) is a caveolae-associated protein
RT involved in ischemia tolerance.";
RL PLoS ONE 8:E71100-E71100(2013).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=26497963; DOI=10.1152/ajpheart.00446.2015;
RA Naito D., Ogata T., Hamaoka T., Nakanishi N., Miyagawa K., Maruyama N.,
RA Kasahara T., Taniguchi T., Nishi M., Matoba S., Ueyama T.;
RT "The coiled-coil domain of MURC/cavin-4 is involved in membrane trafficking
RT of caveolin-3 in cardiomyocytes.";
RL Am. J. Physiol. 309:H2127-H2136(2015).
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes.
CC Interacts directly with G-protein alpha subunits and can functionally
CC regulate their activity. May also regulate voltage-gated potassium
CC channels. Plays a role in the sarcolemma repair mechanism of both
CC skeletal muscle and cardiomyocytes that permits rapid resealing of
CC membranes disrupted by mechanical stress (PubMed:19380584). Mediates
CC the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae (By
CC similarity). {ECO:0000250|UniProtKB:P56539,
CC ECO:0000269|PubMed:19380584}.
CC -!- SUBUNIT: Homooligomer. Interacts with DYSF. Interacts with DLG1 and
CC KCNA5; forms a ternary complex. Interacts with DAG1 (via its C-
CC terminal); the interaction prevents binding of DAG1 with DMD (By
CC similarity). Interacts with TRIM72 (PubMed:19380584). Interacts with
CC MUSK; may regulate MUSK signaling (PubMed:19940021). Interacts with
CC BVES (PubMed:24066022). Interacts with CAVIN1, CAVIN2 and CAVIN4 (By
CC similarity). {ECO:0000250|UniProtKB:P51638,
CC ECO:0000250|UniProtKB:P56539, ECO:0000269|PubMed:19380584,
CC ECO:0000269|PubMed:19940021, ECO:0000269|PubMed:24066022}.
CC -!- INTERACTION:
CC P51637; P18762: Adrb2; NbExp=2; IntAct=EBI-298576, EBI-491143;
CC P51637; Q01815: Cacna1c; NbExp=4; IntAct=EBI-298576, EBI-644904;
CC P51637; Q5SUG4: Cacna1g; NbExp=3; IntAct=EBI-298576, EBI-6918583;
CC P51637; Q6PE92: Cacna1h; NbExp=5; IntAct=EBI-298576, EBI-6918775;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:26497963}; Peripheral membrane protein
CC {ECO:0000250}. Membrane, caveola {ECO:0000269|PubMed:24066022};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:24066022}. Note=Potential hairpin-like structure in
CC the membrane. Membrane protein of caveolae (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in muscle.
CC {ECO:0000269|PubMed:8521953}.
CC -!- PTM: Sumoylation with SUMO3 by PIAS4 may reduce agonist-induced
CC internalization and desensitization of adrenergic receptor ABRD2.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR EMBL; U36579; AAC52352.1; -; mRNA.
DR EMBL; BC024383; AAH24383.1; -; mRNA.
DR CCDS; CCDS20406.1; -.
DR PIR; S68222; S68222.
DR RefSeq; NP_031643.1; NM_007617.3.
DR AlphaFoldDB; P51637; -.
DR SMR; P51637; -.
DR BioGRID; 198516; 8.
DR CORUM; P51637; -.
DR DIP; DIP-31069N; -.
DR IntAct; P51637; 343.
DR MINT; P51637; -.
DR STRING; 10090.ENSMUSP00000074922; -.
DR iPTMnet; P51637; -.
DR PhosphoSitePlus; P51637; -.
DR MaxQB; P51637; -.
DR PaxDb; P51637; -.
DR PeptideAtlas; P51637; -.
DR PRIDE; P51637; -.
DR ProteomicsDB; 265669; -.
DR Antibodypedia; 4305; 293 antibodies from 39 providers.
DR DNASU; 12391; -.
DR Ensembl; ENSMUST00000075477; ENSMUSP00000074922; ENSMUSG00000062694.
DR GeneID; 12391; -.
DR KEGG; mmu:12391; -.
DR UCSC; uc009dea.1; mouse.
DR CTD; 859; -.
DR MGI; MGI:107570; Cav3.
DR VEuPathDB; HostDB:ENSMUSG00000062694; -.
DR eggNOG; ENOG502RYU9; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_102582_0_0_1; -.
DR InParanoid; P51637; -.
DR OMA; QYNINEE; -.
DR OrthoDB; 1468974at2759; -.
DR PhylomeDB; P51637; -.
DR TreeFam; TF315736; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 12391; 3 hits in 71 CRISPR screens.
DR PRO; PR:P51637; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P51637; protein.
DR Bgee; ENSMUSG00000062694; Expressed in cardiac muscle of left ventricle and 92 other tissues.
DR Genevisible; P51637; MM.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IDA:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:MGI.
DR GO; GO:0071253; F:connexin binding; IPI:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
DR GO; GO:0019870; F:potassium channel inhibitor activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0017080; F:sodium channel regulator activity; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:MGI.
DR GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; IMP:MGI.
DR GO; GO:0070836; P:caveola assembly; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.
DR GO; GO:0035995; P:detection of muscle stretch; IMP:BHF-UCL.
DR GO; GO:0006897; P:endocytosis; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0060347; P:heart trabecula formation; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0031579; P:membrane raft organization; IMP:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:InterPro.
DR GO; GO:0007520; P:myoblast fusion; IMP:MGI.
DR GO; GO:0014902; P:myotube differentiation; IMP:MGI.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:MGI.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:MGI.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0045792; P:negative regulation of cell size; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
DR GO; GO:1900826; P:negative regulation of membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IMP:MGI.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
DR GO; GO:0060299; P:negative regulation of sarcomere organization; ISO:MGI.
DR GO; GO:0051647; P:nucleus localization; IMP:MGI.
DR GO; GO:0007009; P:plasma membrane organization; IMP:MGI.
DR GO; GO:0001778; P:plasma membrane repair; IMP:MGI.
DR GO; GO:2001288; P:positive regulation of caveolin-mediated endocytosis; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0090279; P:regulation of calcium ion import; ISO:MGI.
DR GO; GO:1901019; P:regulation of calcium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:MGI.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISO:MGI.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0008016; P:regulation of heart contraction; ISO:MGI.
DR GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR GO; GO:0051394; P:regulation of nerve growth factor receptor activity; ISO:MGI.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; IMP:MGI.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IMP:MGI.
DR GO; GO:0038009; P:regulation of signal transduction by receptor internalization; ISO:MGI.
DR GO; GO:0014819; P:regulation of skeletal muscle contraction; ISO:MGI.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; ISO:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
DR InterPro; IPR031091; CAV-3.
DR InterPro; IPR001612; Caveolin.
DR InterPro; IPR018361; Caveolin_CS.
DR PANTHER; PTHR10844; PTHR10844; 1.
DR PANTHER; PTHR10844:SF16; PTHR10844:SF16; 1.
DR Pfam; PF01146; Caveolin; 1.
DR PROSITE; PS01210; CAVEOLIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Golgi apparatus; Isopeptide bond; Membrane;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..151
FT /note="Caveolin-3"
FT /id="PRO_0000144141"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 64..114
FT /note="Required for interaction with DAG1"
FT /evidence="ECO:0000250"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3)"
FT /evidence="ECO:0000250"
FT MUTAGEN 27
FT /note="R->Q: Results in aberrent localization of TRIM72 and
FT defects in membrane repair."
FT /evidence="ECO:0000269|PubMed:19380584"
FT MUTAGEN 105
FT /note="P->L: Dominant-negative mutant that induces defects
FT in membrane repair."
FT /evidence="ECO:0000269|PubMed:19380584"
SQ SEQUENCE 151 AA; 17358 MW; 7C1A181010CC60F1 CRC64;
MMTEEHTDLE ARIIKDIHCK EIDLVNRDPK NINEDIVKVD FEDVIAEPEG TYSFDGVWKV
SFTTFTVSKY WCYRLLSTLL GVPLALLWGF LFACISFCHI WAVVPCIKSY LIEIQCISHI
YSLCIRTFCN PLFAALGQVC SNIKVVLRRE G
