ID   CVN4A_DANRE             Reviewed;         329 AA.
AC   A1L260; Q0P480;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Caveolae-associated protein 4a;
DE   AltName: Full=Muscle-related coiled-coil protein a;
DE   AltName: Full=Muscle-restricted coiled-coil protein;
GN   Name=cavin4a; Synonyms=murca; ORFNames=zgc:158664;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Larva;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: Induces rhoa activation and activates nppa transcription and
CC       myofibrillar organization through the rho/rock signaling pathway.
CC       {ECO:0000250|UniProtKB:A2AMM0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC       {ECO:0000250|UniProtKB:A2AMM0}. Cytoplasm
CC       {ECO:0000250|UniProtKB:A2AMM0}. Membrane, caveola
CC       {ECO:0000250|UniProtKB:A2AMM0}. Note=Localizes in the caveolae in a
CC       caveolin-dependent manner. {ECO:0000250|UniProtKB:A2AMM0}.
CC   -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI22231.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC122230; AAI22231.1; ALT_INIT; mRNA.
DR   EMBL; BC129363; AAI29364.1; -; mRNA.
DR   RefSeq; NP_001073667.1; NM_001080198.2.
DR   RefSeq; XP_017213931.1; XM_017358442.1.
DR   PDB; 4QKW; X-ray; 1.70 A; A/B/C=16-123.
DR   PDBsum; 4QKW; -.
DR   AlphaFoldDB; A1L260; -.
DR   SMR; A1L260; -.
DR   STRING; 7955.ENSDARP00000121336; -.
DR   iPTMnet; A1L260; -.
DR   PaxDb; A1L260; -.
DR   PeptideAtlas; A1L260; -.
DR   PRIDE; A1L260; -.
DR   GeneID; 552940; -.
DR   KEGG; dre:552940; -.
DR   CTD; 552940; -.
DR   ZFIN; ZDB-GENE-050506-21; cavin4a.
DR   eggNOG; ENOG502QQ9A; Eukaryota.
DR   InParanoid; A1L260; -.
DR   OrthoDB; 991901at2759; -.
DR   PhylomeDB; A1L260; -.
DR   PRO; PR:A1L260; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
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   3D-structure; Activator; Coiled coil; Cytoplasm; Developmental protein;
KW   Differentiation; Membrane; Myogenesis; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..329
FT                   /note="Caveolae-associated protein 4a"
FT                   /id="PRO_0000325765"
FT   REGION          198..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          198..262
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        200..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         292
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   CONFLICT        23
FT                   /note="S -> P (in Ref. 1; AAI22231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="G -> A (in Ref. 1; AAI22231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="E -> K (in Ref. 1; AAI22231)"
FT                   /evidence="ECO:0000305"
FT   HELIX           21..117
FT                   /evidence="ECO:0007829|PDB:4QKW"
SQ   SEQUENCE   329 AA;  36534 MW;  A52AEE4368494E4D CRC64;
     MEKRGDVILG VEDESGQPVS ALSILSLLER VSTIIDGVQA SQQRMEERQQ QLEGSVSAVQ
     SELLKLARDH GATATTVDKL LQKARRVSTH VKEVRSRVEK QNVRVKKVET TQDELLTRNK
     FRVVIYQGEK EVPSVAVTKT PKGAGLAELE VEPDEYDIPA DLSSDEEYMV VEDAESSRGA
     RLKQSGLKGI ENIKAAFSKE NMNKTREKTR ENLSKTKESL SKTGQTLGTK FNTLGEKIVP
     PEQREKIKQS SERLKENIAK KAPTKESFKI KLKKERTVAE GQEGAEAEPA VTPPKGRKSS
     PDVTYTEVVT ENKREGPVSE EGATRIHED