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RHOC_BOVIN
ID   RHOC_BOVIN              Reviewed;         193 AA.
AC   Q1RMJ6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Rho-related GTP-binding protein RhoC;
DE   Flags: Precursor;
GN   Name=RHOC; Synonyms=ARHC;
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=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates a signal transduction pathway linking plasma
CC       membrane receptors to the assembly of focal adhesions and actin stress
CC       fibers. Serves as a microtubule-dependent signal that is required for
CC       the myosin contractile ring formation during cell cycle cytokinesis.
CC       Regulates apical junction formation in bronchial epithelial cells (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RTKN. Interacts with AKAP13. Interacts with
CC       DIAPH1. Interacts with PKN2. Interacts with ROCK1 and ROCK2. Interacts
CC       with ARHGDIA. Interacts with RIPOR1. {ECO:0000250|UniProtKB:P08134,
CC       ECO:0000250|UniProtKB:Q62159}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cleavage furrow
CC       {ECO:0000250}. Note=Translocates to the equatorial region before furrow
CC       formation in a ECT2-dependent manner. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; BC114859; AAI14860.1; -; mRNA.
DR   RefSeq; NP_001039603.1; NM_001046138.2.
DR   RefSeq; XP_005204165.1; XM_005204108.2.
DR   RefSeq; XP_010801464.1; XM_010803162.2.
DR   AlphaFoldDB; Q1RMJ6; -.
DR   SMR; Q1RMJ6; -.
DR   STRING; 9913.ENSBTAP00000018998; -.
DR   PaxDb; Q1RMJ6; -.
DR   PeptideAtlas; Q1RMJ6; -.
DR   PRIDE; Q1RMJ6; -.
DR   Ensembl; ENSBTAT00000018998; ENSBTAP00000018998; ENSBTAG00000014299.
DR   GeneID; 513152; -.
DR   KEGG; bta:513152; -.
DR   CTD; 389; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014299; -.
DR   VGNC; VGNC:55672; RHOC.
DR   eggNOG; KOG0393; Eukaryota.
DR   GeneTree; ENSGT00950000182945; -.
DR   HOGENOM; CLU_041217_21_2_1; -.
DR   InParanoid; Q1RMJ6; -.
DR   OMA; APEVNHY; -.
DR   OrthoDB; 1166960at2759; -.
DR   TreeFam; TF300837; -.
DR   Reactome; R-BTA-416482; G alpha (12/13) signalling events.
DR   Reactome; R-BTA-5625900; RHO GTPases activate CIT.
DR   Reactome; R-BTA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-BTA-9013106; RHOC GTPase cycle.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000014299; Expressed in corpus epididymis and 103 other tissues.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0043297; P:apical junction assembly; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0060193; P:positive regulation of lipase activity; IEA:Ensembl.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   PANTHER; PTHR24072; PTHR24072; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..190
FT                   /note="Rho-related GTP-binding protein RhoC"
FT                   /id="PRO_0000265728"
FT   PROPEP          191..193
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000265729"
FT   MOTIF           34..42
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         190
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           190
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  22006 MW;  A193DA581560F131 CRC64;
     MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG KQVELALWDT
     AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
     LRQDEHTRRE LAKMKQEPVR SEEGRDMANR ISAFGYLECS AKTKEGVREV FEMATRAGLQ
     VRKNKRRRGC PIL
 
 
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