ID   RHOC_PONAB              Reviewed;         193 AA.
AC   Q5RCK9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Rho-related GTP-binding protein RhoC;
DE   Flags: Precursor;
GN   Name=RHOC; Synonyms=ARHC;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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; CR858261; CAH90498.1; -; mRNA.
DR   RefSeq; NP_001125261.1; NM_001131789.1.
DR   AlphaFoldDB; Q5RCK9; -.
DR   SMR; Q5RCK9; -.
DR   STRING; 9601.ENSPPYP00000011947; -.
DR   Ensembl; ENSPPYT00000001226; ENSPPYP00000001186; ENSPPYG00000001018.
DR   GeneID; 100172158; -.
DR   KEGG; pon:100172158; -.
DR   CTD; 389; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   GeneTree; ENSGT00940000160965; -.
DR   InParanoid; Q5RCK9; -.
DR   OrthoDB; 1166960at2759; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0043297; P:apical junction assembly; ISS:UniProtKB.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
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_0000265730"
FT   PROPEP          191..193
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000265731"
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