ID RHOC_HUMAN Reviewed; 193 AA. AC P08134; B3KSW1; Q6ICN3; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 27-MAR-2024, entry version 237. DE RecName: Full=Rho-related GTP-binding protein RhoC; DE AltName: Full=Rho cDNA clone 9; DE Short=h9; DE Flags: Precursor; GN Name=RHOC; Synonyms=ARH9, ARHC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3283705; DOI=10.1093/nar/16.6.2717; RA Chardin P., Madaule P., Tavitian A.; RT "Coding sequence of human rho cDNAs clone 6 and clone 9."; RL Nucleic Acids Res. 16:2717-2717(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RA Fagan K.P., Oliveira L., Pittler S.J.; RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 [10] RP INTERACTION WITH ROCK1 AND ROCK2. RX PubMed=8816443; DOI=10.1128/mcb.16.10.5313; RA Leung T., Chen X.-Q., Manser E., Lim L.; RT "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and RT is involved in the reorganization of the cytoskeleton."; RL Mol. Cell. Biol. 16:5313-5327(1996). RN [11] RP INTERACTION WITH AKAP13. RX PubMed=11546812; DOI=10.1074/jbc.m106629200; RA Diviani D., Soderling J., Scott J.D.; RT "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho- RT mediated stress fiber formation."; RL J. Biol. Chem. 276:44247-44257(2001). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16236794; DOI=10.1091/mbc.e05-06-0569; RA Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.; RT "Dissecting the role of Rho-mediated signaling in contractile ring RT formation."; RL Mol. Biol. Cell 17:43-55(2006). RN [13] RP INTERACTION WITH ARHGDIA. RX PubMed=20400958; DOI=10.1038/ncb2049; RA Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G., RA Brennwald P.J., Burridge K.; RT "Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1."; RL Nat. Cell Biol. 12:477-483(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] 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). RN [16] RP GLYCOSYLATION AT TYR-34 (MICROBIAL INFECTION). RX PubMed=24141704; DOI=10.1038/nsmb.2688; RA Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E., RA Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C., RA Aktories K.; RT "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation RT of Gq and Gi proteins."; RL Nat. Struct. Mol. Biol. 20:1273-1280(2013). RN [17] RP GLYCOSYLATION AT THR-37 (MICROBIAL INFECTION). RX PubMed=24905543; DOI=10.1111/cmi.12321; RA Genth H., Pauillac S., Schelle I., Bouvet P., Bouchier C., RA Varela-Chavez C., Just I., Popoff M.R.; RT "Haemorrhagic toxin and lethal toxin from Clostridium sordellii strain RT vpi9048: molecular characterization and comparative analysis of substrate RT specificity of the large clostridial glucosylating toxins."; RL Cell. Microbiol. 16:1706-1721(2014). RN [18] RP INTERACTION WITH RIPOR1. RX PubMed=27807006; DOI=10.1242/jcs.198614; RA Mardakheh F.K., Self A., Marshall C.J.; RT "RHO binding to FAM65A regulates Golgi reorientation during cell RT migration."; RL J. Cell Sci. 129:4466-4479(2016). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH DIAPH1. RX PubMed=15864301; DOI=10.1038/nature03604; RA Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R., RA Wittinghofer A.; RT "Structural and mechanistic insights into the interaction between Rho and RT mammalian Dia."; RL Nature 435:513-518(2005). 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:16236794, ECO:0000269|PubMed:20974804}. CC -!- SUBUNIT: Interacts with RTKN (By similarity). Interacts with AKAP13 CC (PubMed:11546812). Interacts with DIAPH1 (PubMed:15864301). Interacts CC with PKN2 (PubMed:20974804). Interacts with ROCK1 and ROCK2 CC (PubMed:8816443). Interacts with ARHGDIA (PubMed:20400958). Interacts CC with RIPOR1 (PubMed:27807006). {ECO:0000250, CC ECO:0000250|UniProtKB:Q62159, ECO:0000269|PubMed:11546812, CC ECO:0000269|PubMed:15864301, ECO:0000269|PubMed:20400958, CC ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:27807006, CC ECO:0000269|PubMed:8816443}. CC -!- INTERACTION: CC P08134; Q9Y4F9: RIPOR2; NbExp=5; IntAct=EBI-747589, EBI-2798942; CC P08134; Q96MK2: RIPOR3; NbExp=3; IntAct=EBI-747589, EBI-12010512; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow CC {ECO:0000269|PubMed:16236794}. Note=Translocates to the equatorial CC region before furrow formation in a ECT2-dependent manner. CC -!- PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus CC asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits CC downstream signaling by an impaired interaction with diverse regulator CC and effector proteins of Rho and leads to actin disassembly. CC {ECO:0000269|PubMed:24141704}. CC -!- PTM: (Microbial infection) Glucosylated at Thr-37 by C.difficile toxins CC TcdA and TcdB in the colonic epithelium (PubMed:24905543). CC Monoglucosylation completely prevents the recognition of the downstream CC effector, blocking the GTPases in their inactive form, leading to actin CC cytoskeleton disruption (PubMed:24905543). CC {ECO:0000269|PubMed:24905543}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42110/RHOC"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X06821; CAA29969.1; -; mRNA. DR EMBL; L25081; AAC33179.1; -; mRNA. DR EMBL; AF498972; AAM21119.1; -; mRNA. DR EMBL; CR450360; CAG29356.1; -; mRNA. DR EMBL; BT019448; AAV38255.1; -; mRNA. DR EMBL; AK094474; BAG52873.1; -; mRNA. DR EMBL; AL603832; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471122; EAW56534.1; -; Genomic_DNA. DR EMBL; BC007245; AAH07245.1; -; mRNA. DR EMBL; BC009177; AAH09177.1; -; mRNA. DR EMBL; BC052808; AAH52808.1; -; mRNA. DR CCDS; CCDS854.1; -. DR PIR; S01029; TVHURC. DR RefSeq; NP_001036143.1; NM_001042678.1. DR RefSeq; NP_001036144.1; NM_001042679.1. DR RefSeq; NP_786886.1; NM_175744.4. DR PDB; 1Z2C; X-ray; 3.00 A; A/C=1-193. DR PDB; 2GCN; X-ray; 1.85 A; A=1-181. DR PDB; 2GCO; X-ray; 1.40 A; A/B=1-181. DR PDB; 2GCP; X-ray; 2.15 A; A=1-181. DR PDBsum; 1Z2C; -. DR PDBsum; 2GCN; -. DR PDBsum; 2GCO; -. DR PDBsum; 2GCP; -. DR AlphaFoldDB; P08134; -. DR SMR; P08134; -. DR BioGRID; 106882; 580. DR IntAct; P08134; 32. DR MINT; P08134; -. DR STRING; 9606.ENSP00000285735; -. DR BindingDB; P08134; -. DR ChEMBL; CHEMBL3883318; -. DR GlyCosmos; P08134; 2 sites, No reported glycans. DR GlyGen; P08134; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P08134; -. DR MetOSite; P08134; -. DR PhosphoSitePlus; P08134; -. DR SwissPalm; P08134; -. DR BioMuta; RHOC; -. DR DMDM; 132543; -. DR EPD; P08134; -. DR jPOST; P08134; -. DR MassIVE; P08134; -. DR MaxQB; P08134; -. DR PaxDb; 9606-ENSP00000285735; -. DR PeptideAtlas; P08134; -. DR ProteomicsDB; 52072; -. DR Pumba; P08134; -. DR TopDownProteomics; P08134; -. DR Antibodypedia; 33829; 426 antibodies from 31 providers. DR DNASU; 389; -. DR Ensembl; ENST00000285735.6; ENSP00000285735.2; ENSG00000155366.17. DR Ensembl; ENST00000339083.12; ENSP00000345236.8; ENSG00000155366.17. DR Ensembl; ENST00000369632.6; ENSP00000358646.2; ENSG00000155366.17. DR Ensembl; ENST00000369633.6; ENSP00000358647.2; ENSG00000155366.17. DR Ensembl; ENST00000369637.5; ENSP00000358651.1; ENSG00000155366.17. DR Ensembl; ENST00000369638.6; ENSP00000358652.2; ENSG00000155366.17. DR Ensembl; ENST00000369642.7; ENSP00000358656.3; ENSG00000155366.17. DR GeneID; 389; -. DR KEGG; hsa:389; -. DR MANE-Select; ENST00000339083.12; ENSP00000345236.8; NM_175744.5; NP_786886.1. DR UCSC; uc001ecp.1; human. DR AGR; HGNC:669; -. DR CTD; 389; -. DR DisGeNET; 389; -. DR GeneCards; RHOC; -. DR HGNC; HGNC:669; RHOC. DR HPA; ENSG00000155366; Low tissue specificity. DR MIM; 165380; gene. DR neXtProt; NX_P08134; -. DR OpenTargets; ENSG00000155366; -. DR PharmGKB; PA24951; -. DR VEuPathDB; HostDB:ENSG00000155366; -. DR eggNOG; KOG0393; Eukaryota. DR GeneTree; ENSGT00950000182945; -. DR InParanoid; P08134; -. DR OMA; QADWINH; -. DR OrthoDB; 20499at2759; -. DR PhylomeDB; P08134; -. DR TreeFam; TF300837; -. DR BRENDA; 3.6.5.2; 2681. DR PathwayCommons; P08134; -. DR Reactome; R-HSA-416482; G alpha (12/13) signalling events. DR Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse. DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs. DR Reactome; R-HSA-5625900; RHO GTPases activate CIT. DR Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins. DR Reactome; R-HSA-9013106; RHOC GTPase cycle. DR SignaLink; P08134; -. DR SIGNOR; P08134; -. DR BioGRID-ORCS; 389; 22 hits in 1158 CRISPR screens. DR ChiTaRS; RHOC; human. DR EvolutionaryTrace; P08134; -. DR GeneWiki; RhoC; -. DR GenomeRNAi; 389; -. DR Pharos; P08134; Tbio. DR PRO; PR:P08134; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P08134; Protein. DR Bgee; ENSG00000155366; Expressed in mucosa of transverse colon and 109 other cell types or tissues. DR ExpressionAtlas; P08134; baseline and differential. DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0000281; P:mitotic cytokinesis; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL. DR GO; GO:0060193; P:positive regulation of lipase activity; IDA:AgBase. 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; IMP:BHF-UCL. 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; P08134; HS. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Cell membrane; Glycoprotein; GTP-binding; KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation; KW Reference proteome. FT CHAIN 1..190 FT /note="Rho-related GTP-binding protein RhoC" FT /id="PRO_0000042022" FT PROPEP 191..193 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000042023" 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 41 FT /note="ADP-ribosylasparagine; by botulinum toxin" FT /evidence="ECO:0000250" FT MOD_RES 190 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250|UniProtKB:P62745" FT LIPID 190 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62745" FT CARBOHYD 34 FT /note="O-linked (GlcNAc) tyrosine; by Photorhabdus FT PAU_02230" FT /evidence="ECO:0000269|PubMed:24141704" FT CARBOHYD 37 FT /note="(Microbial infection) O-linked (Glc) threonine; by FT C.difficile toxins TcdA and TcdB" FT /evidence="ECO:0000269|PubMed:24905543" FT VARIANT 120 FT /note="D -> H (in dbSNP:rs11538959)" FT /id="VAR_051974" FT STRAND 4..13 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 18..27 FT /evidence="ECO:0007829|PDB:2GCO" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:2GCO" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:2GCO" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:2GCO" FT STRAND 78..85 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 89..97 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 99..106 FT /evidence="ECO:0007829|PDB:2GCO" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 125..132 FT /evidence="ECO:0007829|PDB:2GCO" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 141..150 FT /evidence="ECO:0007829|PDB:2GCO" FT STRAND 154..158 FT /evidence="ECO:0007829|PDB:2GCO" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:2GCO" FT HELIX 167..179 FT /evidence="ECO:0007829|PDB:2GCO" 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 //