CAV3_RAT
ID CAV3_RAT Reviewed; 151 AA.
AC P51638;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Caveolin-3;
GN Name=Cav3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart muscle;
RX PubMed=8567687; DOI=10.1074/jbc.271.4.2255;
RA Tang Z., Scherer P.E., Okamoto T., Song K., Chu K., Kohtz D.S.,
RA Nishimoto I., Lodish H.F., Lisanti M.P.;
RT "Molecular cloning of caveolin-3, a novel member of the caveolin gene
RT family expressed predominantly in muscle.";
RL J. Biol. Chem. 271:2255-2261(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP INTERACTION WITH DLG1 AND KCNA5.
RX PubMed=15277200; DOI=10.1152/ajpheart.00152.2004;
RA Folco E.J., Liu G.-X., Koren G.;
RT "Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the
RT voltage-gated potassium channel Kv1.5.";
RL Am. J. Physiol. 287:H681-H690(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=24567387; DOI=10.1073/pnas.1315359111;
RA Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T., Miyagawa K.,
RA Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H., Oh H., Ueyama T.;
RT "MURC/Cavin-4 facilitates recruitment of ERK to caveolae and concentric
RT cardiac hypertrophy induced by alpha1-adrenergic receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014).
RN [5]
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. Mediates the recruitment of
CC CAVIN2 and CAVIN3 proteins to the caveolae.
CC {ECO:0000250|UniProtKB:P51637, ECO:0000250|UniProtKB:P56539}.
CC -!- SUBUNIT: Homooligomer. Interacts with DYSF (By similarity). Interacts
CC with DLG1 and KCNA5; forms a ternary complex (PubMed:15277200).
CC Interacts with DAG1 (via its C-terminal); the interaction prevents
CC binding of DAG1 with DMD. Interacts with TRIM72. Interacts with MUSK;
CC may regulate MUSK signaling. Interacts with BVES. Interacts with
CC CAVIN1, CAVIN2 and CAVIN4 (By similarity).
CC {ECO:0000250|UniProtKB:P51637, ECO:0000250|UniProtKB:P56539,
CC ECO:0000269|PubMed:15277200}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:26497963}; Peripheral
CC membrane protein {ECO:0000250}. Membrane, caveola
CC {ECO:0000250|UniProtKB:P51637}; Peripheral membrane protein
CC {ECO:0000250}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P51637}. Note=Potential hairpin-like structure
CC in the membrane. Membrane protein of caveolae (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in muscle.
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; U31968; AAC52377.1; -; mRNA.
DR EMBL; BC084692; AAH84692.1; -; mRNA.
DR RefSeq; NP_062028.1; NM_019155.2.
DR AlphaFoldDB; P51638; -.
DR BioGRID; 247843; 4.
DR CORUM; P51638; -.
DR IntAct; P51638; 1.
DR MINT; P51638; -.
DR STRING; 10116.ENSRNOP00000007601; -.
DR iPTMnet; P51638; -.
DR PhosphoSitePlus; P51638; -.
DR SwissPalm; P51638; -.
DR jPOST; P51638; -.
DR PaxDb; P51638; -.
DR PRIDE; P51638; -.
DR Ensembl; ENSRNOT00000007601; ENSRNOP00000007601; ENSRNOG00000005798.
DR GeneID; 29161; -.
DR KEGG; rno:29161; -.
DR UCSC; RGD:2281; rat.
DR CTD; 859; -.
DR RGD; 2281; Cav3.
DR eggNOG; ENOG502RYU9; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_102582_0_0_1; -.
DR InParanoid; P51638; -.
DR OMA; QYNINEE; -.
DR OrthoDB; 1468974at2759; -.
DR PhylomeDB; P51638; -.
DR TreeFam; TF315736; -.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR PRO; PR:P51638; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000005798; Expressed in quadriceps femoris and 11 other tissues.
DR Genevisible; P51638; RN.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0071253; F:connexin binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:RGD.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
DR GO; GO:0019870; F:potassium channel inhibitor activity; IMP:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0017080; F:sodium channel regulator activity; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
DR GO; GO:0070836; P:caveola assembly; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; IEP:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:RGD.
DR GO; GO:0035995; P:detection of muscle stretch; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0060347; P:heart trabecula formation; ISO:RGD.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0031579; P:membrane raft organization; ISO:RGD.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:InterPro.
DR GO; GO:0007520; P:myoblast fusion; ISO:RGD.
DR GO; GO:0014902; P:myotube differentiation; ISO:RGD.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISO:RGD.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0045792; P:negative regulation of cell size; ISO:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:RGD.
DR GO; GO:1900826; P:negative regulation of membrane depolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISO:RGD.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0060299; P:negative regulation of sarcomere organization; ISO:RGD.
DR GO; GO:0051647; P:nucleus localization; ISO:RGD.
DR GO; GO:0007009; P:plasma membrane organization; ISO:RGD.
DR GO; GO:0001778; P:plasma membrane repair; ISO:RGD.
DR GO; GO:2001288; P:positive regulation of caveolin-mediated endocytosis; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:RGD.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; ISO:RGD.
DR GO; GO:0090279; P:regulation of calcium ion import; ISO:RGD.
DR GO; GO:1901019; P:regulation of calcium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISO:RGD.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0051394; P:regulation of nerve growth factor receptor activity; ISO:RGD.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0038009; P:regulation of signal transduction by receptor internalization; ISO:RGD.
DR GO; GO:0014819; P:regulation of skeletal muscle contraction; ISO:RGD.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; ISO:RGD.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
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_0000144142"
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 CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 151 AA; 17402 MW; A822A33EF9AA668F CRC64;
MMTEEHTDLE ARIIKDIHCK EIDLVNRDPK NINEDIVKVD FEDVIAEPEG TYSFDGVWRV
SYTTFTVSKY WCYRLLSTLL GVPLALLWGF LFACISFCHI WAVVPCIKSY LIEIQCISHI
YSLCIRTFCN PLFAALGQVC SNIKVVLRRE G
