CAVN4_RAT
ID CAVN4_RAT Reviewed; 362 AA.
AC B1PRL5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Caveolae-associated protein 4 {ECO:0000312|RGD:1310395};
DE AltName: Full=Muscle-related coiled-coil protein {ECO:0000250|UniProtKB:Q5BKX8};
DE AltName: Full=Muscle-restricted coiled-coil protein {ECO:0000312|EMBL:ACA62937.1};
GN Name=Cavin4 {ECO:0000312|RGD:1310395};
GN Synonyms=Murc {ECO:0000312|EMBL:ACA62937.1};
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] {ECO:0000305, ECO:0000312|EMBL:ACA62937.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:ACA62937.1};
RC TISSUE=Cardiac myocyte {ECO:0000269|PubMed:18332105};
RX PubMed=18332105; DOI=10.1128/mcb.02186-07;
RA Ogata T., Ueyama T., Isodono K., Tagawa M., Takehara N., Kawashima T.,
RA Harada K., Takahashi T., Shioi T., Matsubara H., Oh H.;
RT "MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK
RT pathway, induces cardiac dysfunction and conduction disturbance.";
RL Mol. Cell. Biol. 28:3424-3436(2008).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-171; SER-172 AND
RP THR-334, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, AND 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).
CC -!- FUNCTION: Modulates the morphology of formed caveolae in
CC cardiomyocytes, but is not required for caveolar formation. Facilitates
CC the recruitment of MAPK1/3 to caveolae within cardiomyocytes and
CC regulates alpha-1 adrenergic receptor-induced hypertrophic responses in
CC cardiomyocytes through MAPK1/3 activation. Contributes to proper
CC membrane localization and stabilization of caveolin-3 (CAV3) in
CC cardiomyocytes (By similarity). Induces RHOA activation and activates
CC NPPA transcription and myofibrillar organization through the Rho/ROCK
CC signaling pathway (PubMed:18332105). {ECO:0000250|UniProtKB:A2AMM0,
CC ECO:0000269|PubMed:18332105}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN4. Interacts with CAVIN1, CAV3, ADRA1A and ADRA1B.
CC Interacts with CAVIN2; this augments the transactivation of NPPA (By
CC similarity). Interacts with MAPK1 and MAPK3 (PubMed:24567387).
CC {ECO:0000250|UniProtKB:A2AMM0, ECO:0000250|UniProtKB:Q5BKX8,
CC ECO:0000269|PubMed:24567387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm
CC {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:A2AMM0}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:A2AMM0}. Membrane, caveola
CC {ECO:0000269|PubMed:24567387}. Cell membrane
CC {ECO:0000250|UniProtKB:A2AMM0}. Note=In cardiomyocytes, accumulates in
CC the Z-line of the sarcomere. In vascular smooth muscle cells, detected
CC diffusely throughout the cytoplasm. Localizes in the caveolae in a
CC caveolin-dependent manner. {ECO:0000250|UniProtKB:A2AMM0}.
CC -!- TISSUE SPECIFICITY: Expressed at much higher levels in cardiomyocytes
CC than in non-cardiomyocytes. {ECO:0000269|PubMed:18332105}.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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DR EMBL; EU487255; ACA62937.1; -; mRNA.
DR RefSeq; NP_001101401.1; NM_001107931.2.
DR AlphaFoldDB; B1PRL5; -.
DR SMR; B1PRL5; -.
DR BioGRID; 260358; 1.
DR STRING; 10116.ENSRNOP00000010561; -.
DR iPTMnet; B1PRL5; -.
DR PhosphoSitePlus; B1PRL5; -.
DR PaxDb; B1PRL5; -.
DR PeptideAtlas; B1PRL5; -.
DR PRIDE; B1PRL5; -.
DR Ensembl; ENSRNOT00000010561; ENSRNOP00000010561; ENSRNOG00000008027.
DR GeneID; 313225; -.
DR KEGG; rno:313225; -.
DR UCSC; RGD:1310395; rat.
DR CTD; 347273; -.
DR RGD; 1310395; Cavin4.
DR eggNOG; ENOG502QQ9A; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR HOGENOM; CLU_065589_1_0_1; -.
DR InParanoid; B1PRL5; -.
DR OMA; YYIEESR; -.
DR OrthoDB; 991901at2759; -.
DR PhylomeDB; B1PRL5; -.
DR TreeFam; TF331031; -.
DR PRO; PR:B1PRL5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008027; Expressed in quadriceps femoris and 8 other tissues.
DR Genevisible; B1PRL5; RN.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR InterPro; IPR033299; Cavin4.
DR InterPro; IPR026752; Cavin_fam.
DR PANTHER; PTHR15240; PTHR15240; 1.
DR PANTHER; PTHR15240:SF4; PTHR15240:SF4; 1.
DR Pfam; PF15237; PTRF_SDPR; 1.
PE 1: Evidence at protein level;
KW Activator; Cell membrane; Coiled coil; Cytoplasm; Developmental protein;
KW Differentiation; Membrane; Myogenesis; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..362
FT /note="Caveolae-associated protein 4"
FT /id="PRO_0000370221"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..120
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 324
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A2AMM0"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AMM0"
SQ SEQUENCE 362 AA; 41093 MW; C3FB53E5D7D9C154 CRC64;
MEHNGSASNA GKIHQNRLSS VTEDEDQDAA LTIVTVLDRV ATVVDSVQAS QKRIEERHRE
MGNAIKSVQI DLLKLSQSHS NTGYVVNKLF EKTRKVSAHI KDVKARVEKQ QVRVTKVETK
QEEIMKKNKF RVVIFQEDVP CPASLSVVKD RSLPENEEEA EEVFDPPIDL SSDEEYYVEE
SRSARLRKSG KEHIDHIKKA FSKENMQKTR QNFDKKVSGI RTRIVTPERR ERLRQSGERL
RQSGERLRQS GERFKKSISN ATPSKEAFKI RSLRKPKDPK AEGQEVDRGM GVDIISGSLA
LGPIHEFHSD GFSETEKEVT KVGYIPQEGG DPPTPEPLKV TFKPQVRVED DESLLLELKQ
SS
