ID   CAVN4_BOVIN             Reviewed;         361 AA.
AC   A5PJI6; A7YVI0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Caveolae-associated protein 4;
DE   AltName: Full=Muscle-related coiled-coil protein;
DE   AltName: Full=Muscle-restricted coiled-coil protein;
GN   Name=CAVIN4; Synonyms=MURC;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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. Induces RHOA activation and activates NPPA
CC       transcription and myofibrillar organization through the Rho/ROCK
CC       signaling pathway. {ECO:0000250|UniProtKB:A2AMM0}.
CC   -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC       CAVIN3 and CAVIN4. Interacts with CAVIN1, ADRA1A, ADRA1B, MAPK1 and
CC       MAPK3. Interacts with CAVIN2; this augments the transactivation of
CC       NPPA. {ECO:0000250|UniProtKB:A2AMM0, ECO:0000250|UniProtKB:B1PRL5,
CC       ECO:0000250|UniProtKB:Q5BKX8}.
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: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   -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI23730.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI23730.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAI42127.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC123729; AAI23730.1; ALT_SEQ; mRNA.
DR   EMBL; BC142126; AAI42127.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001096734.2; NM_001103264.1.
DR   AlphaFoldDB; A5PJI6; -.
DR   SMR; A5PJI6; -.
DR   STRING; 9913.ENSBTAP00000029327; -.
DR   PaxDb; A5PJI6; -.
DR   Ensembl; ENSBTAT00000029327; ENSBTAP00000029327; ENSBTAG00000021992.
DR   Ensembl; ENSBTAT00000073253; ENSBTAP00000066521; ENSBTAG00000021992.
DR   GeneID; 528386; -.
DR   KEGG; bta:528386; -.
DR   CTD; 347273; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021992; -.
DR   VGNC; VGNC:26805; CAVIN4.
DR   eggNOG; ENOG502QQ9A; Eukaryota.
DR   GeneTree; ENSGT00950000182910; -.
DR   HOGENOM; CLU_065589_1_0_1; -.
DR   InParanoid; A5PJI6; -.
DR   OMA; YYIEESR; -.
DR   OrthoDB; 991901at2759; -.
DR   TreeFam; TF331031; -.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000021992; Expressed in biceps femoris and 88 other tissues.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS: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; IEA:Ensembl.
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; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Activator; Cell membrane; Coiled coil; Cytoplasm; Developmental protein;
KW   Differentiation; Membrane; Myogenesis; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..361
FT                   /note="Caveolae-associated protein 4"
FT                   /id="PRO_0000325762"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..124
FT                   /evidence="ECO:0000255"
FT   COILED          204..248
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1PRL5"
FT   MOD_RES         171
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1PRL5"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1PRL5"
FT   MOD_RES         335
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AMM0"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AMM0"
SQ   SEQUENCE   361 AA;  41161 MW;  B4D416C612C69B7A CRC64;
     MEHNGSASNA DKIHQNRLSN VTEDEDQDAA LTIVTVLDKV AAIVDSVQAS QKRIEERHRV
     MENAIKSVQI DLLKFSQSHS NTGYVINKLF EKTRKVSAHI KDVKARVEKQ QTHVKKVEAK
     QEEIMKKNKF RVVIFQEEVQ CPTSLSVVKD RSLTESPEEV DEIFDTPVDL SSDEEYFVEE
     SRSARLKKSG KERIDNIKKA FSKENMQKTR QNFDKKVNRI RTRIVTPERR ERLRQSGERL
     RQSGERLKQS GERFKKSISN AAPSREAFKM RSLRKTKDRA VAEGPEEVRE MGVDIIARGE
     ALGPISELYP EALSETDPEE ASATHPPQEG GEVSTPEPLK VTFKPQVKVE DDESLLLDLK
     Q