RHOC_HUMAN
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 03-AUG-2022, entry version 228.
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="http://atlasgeneticsoncology.org/Genes/RHOCID42110ch1p13.html";
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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; 566.
DR IntAct; P08134; 29.
DR MINT; P08134; -.
DR STRING; 9606.ENSP00000285735; -.
DR BindingDB; P08134; -.
DR ChEMBL; CHEMBL3883318; -.
DR GlyGen; P08134; 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; P08134; -.
DR PeptideAtlas; P08134; -.
DR PRIDE; P08134; -.
DR ProteomicsDB; 52072; -.
DR TopDownProteomics; P08134; -.
DR Antibodypedia; 33829; 374 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 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; KINACAY; -.
DR OrthoDB; 1166960at2759; -.
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; 21 hits in 1080 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 107 other tissues.
DR ExpressionAtlas; P08134; baseline and differential.
DR Genevisible; P08134; HS.
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; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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: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; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
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: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 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
