ID   RHOC_MOUSE              Reviewed;         193 AA.
AC   Q62159; Q3TUN0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Rho-related GTP-binding protein RhoC;
DE   AltName: Full=Silica-induced gene 61 protein;
DE            Short=SIG-61;
DE   Flags: Precursor;
GN   Name=Rhoc; Synonyms=Arhc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   TISSUE=Macrophage;
RX   PubMed=7868905;
RA   Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S.;
RT   "Isolation of nine gene sequences induced by silica in murine
RT   macrophages.";
RL   J. Immunol. 154:2384-2392(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH RTKN.
RX   PubMed=8662891; DOI=10.1074/jbc.271.23.13556;
RA   Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N.,
RA   Fujisawa K., Morii N., Madaule P., Narumiya S.;
RT   "Rhotekin, a new putative target for Rho bearing homology to a
RT   serine/threonine kinase, PKN, and rhophilin in the rho-binding domain.";
RL   J. Biol. Chem. 271:13556-13560(1996).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH PKN2.
RX   PubMed=20974804; DOI=10.1128/mcb.01001-10;
RA   Wallace S.W., Magalhaes A., Hall A.;
RT   "The Rho target PRK2 regulates apical junction formation in human bronchial
RT   epithelial cells.";
RL   Mol. Cell. Biol. 31:81-91(2011).
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.
CC       {ECO:0000269|PubMed:20974804}.
CC   -!- SUBUNIT: Interacts with RTKN (PubMed:8662891). Interacts with AKAP13.
CC       Interacts with DIAPH1 (By similarity). Interacts with PKN2
CC       (PubMed:20974804). Interacts with ROCK1 and ROCK2. Interacts with
CC       ARHGDIA. Interacts with RIPOR1 (By similarity).
CC       {ECO:0000250|UniProtKB:P08134, ECO:0000269|PubMed:20974804,
CC       ECO:0000269|PubMed:8662891}.
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   -!- INDUCTION: Up-regulated in silica-treated macrophages.
CC       {ECO:0000269|PubMed:7868905}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; X80638; CAA56682.1; -; mRNA.
DR   EMBL; AK011599; BAB27724.1; -; mRNA.
DR   EMBL; AK152802; BAE31507.1; -; mRNA.
DR   EMBL; AK160650; BAE35941.1; -; mRNA.
DR   EMBL; BC004627; AAH04627.1; -; mRNA.
DR   CCDS; CCDS17704.1; -.
DR   RefSeq; NP_001278788.1; NM_001291859.1.
DR   RefSeq; NP_031510.2; NM_007484.2.
DR   AlphaFoldDB; Q62159; -.
DR   SMR; Q62159; -.
DR   BioGRID; 198197; 4.
DR   IntAct; Q62159; 3.
DR   MINT; Q62159; -.
DR   STRING; 10090.ENSMUSP00000002303; -.
DR   GlyGen; Q62159; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q62159; -.
DR   PhosphoSitePlus; Q62159; -.
DR   SwissPalm; Q62159; -.
DR   EPD; Q62159; -.
DR   jPOST; Q62159; -.
DR   MaxQB; Q62159; -.
DR   PaxDb; 10090-ENSMUSP00000002303; -.
DR   PeptideAtlas; Q62159; -.
DR   ProteomicsDB; 254877; -.
DR   Pumba; Q62159; -.
DR   TopDownProteomics; Q62159; -.
DR   DNASU; 11853; -.
DR   Ensembl; ENSMUST00000002303.12; ENSMUSP00000002303.6; ENSMUSG00000002233.14.
DR   Ensembl; ENSMUST00000106787.8; ENSMUSP00000102399.2; ENSMUSG00000002233.14.
DR   Ensembl; ENSMUST00000196817.5; ENSMUSP00000142697.2; ENSMUSG00000002233.14.
DR   GeneID; 11853; -.
DR   KEGG; mmu:11853; -.
DR   UCSC; uc008qul.2; mouse.
DR   AGR; MGI:106028; -.
DR   CTD; 389; -.
DR   MGI; MGI:106028; Rhoc.
DR   VEuPathDB; HostDB:ENSMUSG00000002233; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   GeneTree; ENSGT00950000182945; -.
DR   InParanoid; Q62159; -.
DR   OMA; GAVECVH; -.
DR   OrthoDB; 20499at2759; -.
DR   PhylomeDB; Q62159; -.
DR   TreeFam; TF300837; -.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
DR   Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-MMU-5625900; RHO GTPases activate CIT.
DR   Reactome; R-MMU-5627117; RHO GTPases Activate ROCKs.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR   BioGRID-ORCS; 11853; 3 hits in 79 CRISPR screens.
DR   PRO; PR:Q62159; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q62159; Protein.
DR   Bgee; ENSMUSG00000002233; Expressed in decidua and 252 other cell types or tissues.
DR   ExpressionAtlas; Q62159; baseline and differential.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0032420; C:stereocilium; IDA: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; IDA:UniProtKB.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:UniProtKB.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; 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   CDD; cd01870; RhoA_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR   PANTHER; PTHR24072:SF100; RHO-RELATED GTP-BINDING PROTEIN RHOC; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51420; RHO; 1.
DR   Genevisible; Q62159; MM.
PE   1: Evidence at protein 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_0000042024"
FT   PROPEP          191..193
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042025"
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"
FT   CONFLICT        102
FT                   /note="E -> Q (in Ref. 1; CAA56682)"
FT                   /evidence="ECO:0000305"
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
//