RHOC_MOUSE
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 03-AUG-2022, entry version 194.
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 iPTMnet; Q62159; -.
DR PhosphoSitePlus; Q62159; -.
DR SwissPalm; Q62159; -.
DR EPD; Q62159; -.
DR jPOST; Q62159; -.
DR MaxQB; Q62159; -.
DR PaxDb; Q62159; -.
DR PeptideAtlas; Q62159; -.
DR PRIDE; Q62159; -.
DR ProteomicsDB; 254877; -.
DR TopDownProteomics; Q62159; -.
DR DNASU; 11853; -.
DR Ensembl; ENSMUST00000002303; ENSMUSP00000002303; ENSMUSG00000002233.
DR Ensembl; ENSMUST00000106787; ENSMUSP00000102399; ENSMUSG00000002233.
DR Ensembl; ENSMUST00000196817; ENSMUSP00000142697; ENSMUSG00000002233.
DR GeneID; 11853; -.
DR KEGG; mmu:11853; -.
DR UCSC; uc008qul.2; mouse.
DR CTD; 389; -.
DR MGI; MGI:106028; Rhoc.
DR VEuPathDB; HostDB:ENSMUSG00000002233; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR InParanoid; Q62159; -.
DR OMA; APEVNHY; -.
DR OrthoDB; 1166960at2759; -.
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 74 CRISPR screens.
DR PRO; PR:Q62159; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q62159; protein.
DR Bgee; ENSMUSG00000002233; Expressed in decidua and 249 other tissues.
DR ExpressionAtlas; Q62159; baseline and differential.
DR Genevisible; Q62159; MM.
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; 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: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; ISO:MGI.
DR GO; GO:0060193; P:positive regulation of lipase activity; 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: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 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
