RAC3_MOUSE
ID RAC3_MOUSE Reviewed; 192 AA.
AC P60764; O14658;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ras-related C3 botulinum toxin substrate 3;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P60763};
DE AltName: Full=p21-Rac3;
DE Flags: Precursor;
GN Name=Rac3 {ECO:0000312|MGI:MGI:2180784};
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].
RA Koga H., Sumimoto H.;
RT "Mouse Rac3.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Swiss Webster; TISSUE=Submandibular gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC an active GTP-bound and inactive GDP-bound state. In active state binds
CC to a variety of effector proteins to regulate cellular responses, such
CC as cell spreading and the formation of actin-based protusions including
CC lamellipodia and membrane ruffles. Promotes cell adhesion and spreading
CC on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner.
CC {ECO:0000250|UniProtKB:P60763}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P60763};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. Regulated by the GEF protein DOCK7.
CC {ECO:0000250|UniProtKB:P60763}.
CC -!- SUBUNIT: Interacts with the GEF protein DOCK7, which promotes the
CC exchange between GDP and GTP, and therefore activates it. Interacts
CC with C1D. Interacts (via C-terminal region) with CIB1; the interaction
CC induces their association with the cytoskeleton upon alpha-IIb/beta3
CC integrin-mediated adhesion. Interacts with NRBP.
CC {ECO:0000250|UniProtKB:P60763}.
CC -!- INTERACTION:
CC P60764; Q99PT1: Arhgdia; NbExp=3; IntAct=EBI-644949, EBI-494354;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P60763}.
CC Endomembrane system {ECO:0000250|UniProtKB:P60763}. Cell projection,
CC lamellipodium {ECO:0000250|UniProtKB:P60763}. Cytoplasm, perinuclear
CC region {ECO:0000250|UniProtKB:P60763}. Cell membrane
CC {ECO:0000250|UniProtKB:P60763}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P60763}. Note=Membrane-associated when
CC activated. Colocalizes with NRBP to endomembranes and at the cell
CC periphery in lamellipodia. Colocalized with CIB1 in the perinuclear
CC area and at the cell periphery. {ECO:0000250|UniProtKB:P60763}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AB040819; BAB40573.1; -; mRNA.
DR EMBL; AK089930; BAC41001.1; -; mRNA.
DR CCDS; CCDS25754.1; -.
DR RefSeq; NP_573486.1; NM_133223.4.
DR AlphaFoldDB; P60764; -.
DR SMR; P60764; -.
DR BioGRID; 228420; 2.
DR IntAct; P60764; 4.
DR MINT; P60764; -.
DR STRING; 10090.ENSMUSP00000018156; -.
DR iPTMnet; P60764; -.
DR PhosphoSitePlus; P60764; -.
DR SwissPalm; P60764; -.
DR jPOST; P60764; -.
DR PaxDb; P60764; -.
DR PeptideAtlas; P60764; -.
DR PRIDE; P60764; -.
DR ProteomicsDB; 300388; -.
DR Antibodypedia; 32958; 94 antibodies from 24 providers.
DR DNASU; 170758; -.
DR Ensembl; ENSMUST00000018156; ENSMUSP00000018156; ENSMUSG00000018012.
DR GeneID; 170758; -.
DR KEGG; mmu:170758; -.
DR UCSC; uc007mug.1; mouse.
DR CTD; 5881; -.
DR MGI; MGI:2180784; Rac3.
DR VEuPathDB; HostDB:ENSMUSG00000018012; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153500; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P60764; -.
DR OMA; DRRMQPI; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P60764; -.
DR TreeFam; TF101109; -.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 170758; 2 hits in 73 CRISPR screens.
DR PRO; PR:P60764; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P60764; protein.
DR Bgee; ENSMUSG00000018012; Expressed in embryonic brain and 193 other tissues.
DR ExpressionAtlas; P60764; baseline and differential.
DR Genevisible; P60764; MM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; ISS:UniProtKB.
DR GO; GO:0021894; P:cerebral cortex GABAergic interneuron development; IGI:MGI.
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:0048873; P:homeostasis of number of cells within a tissue; IGI:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IGI:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0014041; P:regulation of neuron maturation; IGI:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IGI:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:MGI.
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; Cell projection; Cytoplasm; Cytoskeleton; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Reference proteome.
FT CHAIN 1..189
FT /note="Ras-related C3 botulinum toxin substrate 3"
FT /id="PRO_0000198890"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281241"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 192 AA; 21379 MW; 560BBC26BB7CDF4A CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPHTPI LLVGTKLDLR
DDKDTIERLR DKKLAPITYP QGLAMAREIG SVKYLECSAL TQRGLKTVFD EAIRAVLCPP
PVKKPGKKCT VF
