GENTAUR Molecular Products.

 RAC1_MOUSE              Reviewed;         192 AA.
 P63001; O95501; P15154; Q9BTB4;
 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
 31-AUG-2004, sequence version 1.
 18-JUL-2018, entry version 166.
 RecName: Full=Ras-related C3 botulinum toxin substrate 1;
 AltName: Full=p21-Rac1;
 Flags: Precursor;
 Name=Rac1;
 Mus musculus (Mouse).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Mus; Mus.
 NCBI_TaxID=10090;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
 TISSUE=Thymus;
 PubMed=1905006;
 Moll J., Sansig G., Fattori E., van der Putten H.;
 "The murine rac1 gene: cDNA cloning, tissue distribution and regulated
 expression of rac1 mRNA by disassembly of actin microfilaments.";
 Oncogene 6:863-866(1991).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=C57BL/6J, and NOD; TISSUE=Head, Liver, Thymus, and Tongue;
 PubMed=16141072; DOI=10.1126/science.1112014;
 Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
 Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
 Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
 Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
 Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
 Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
 Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
 Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
 di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
 Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
 Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
 Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
 Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
 Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
 Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
 Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
 Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
 Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
 Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
 Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
 Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
 Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
 Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
 Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
 Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
 Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
 Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
 Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
 Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
 Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
 Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
 Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
 Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
 Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
 Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
 Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
 Hayashizaki Y.;
 "The transcriptional landscape of the mammalian genome.";
 Science 309:1559-1563(2005).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [4]
 INTERACTION WITH RASGRF2.
 PubMed=9707409; DOI=10.1016/S0960-9822(07)00376-4;
 Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.;
 "The exchange factor Ras-GRF2 activates Ras-dependent and Rac-
 dependent mitogen-activated protein kinase pathways.";
 Curr. Biol. 8:935-938(1998).
 [5]
 INTERACTION WITH PARD6A, AND MUTAGENESIS OF GLY-12.
 PubMed=10934474; DOI=10.1038/35019573;
 Joberty G., Petersen C., Gao L., Macara I.G.;
 "The cell-polarity protein Par6 links Par3 and atypical protein kinase
 C to Cdc42.";
 Nat. Cell Biol. 2:531-539(2000).
 [6]
 INTERACTION WITH PARD6B.
 PubMed=10934475; DOI=10.1038/35019582;
 Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.;
 "A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC
 signalling and cell polarity.";
 Nat. Cell Biol. 2:540-547(2000).
 [7]
 INTERACTION WITH PIP5K1A.
 PubMed=10679324; DOI=10.1016/S0960-9822(00)00315-8;
 Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C.,
 Carpenter C.L.;
 "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-
 dependent actin assembly.";
 Curr. Biol. 10:153-156(2000).
 [8]
 INTERACTION WITH MAP3K3; MAP2K3 AND CCM2.
 PubMed=14634666; DOI=10.1038/ncb1071;
 Uhlik M.T., Abell A.N., Johnson N.L., Sun W., Cuevas B.D.,
 Lobel-Rice K.E., Horne E.A., Dell'Acqua M.L., Johnson G.L.;
 "Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during
 hyperosmotic shock.";
 Nat. Cell Biol. 5:1104-1110(2003).
 [9]
 INTERACTION WITH NISCH.
 PubMed=16002401; DOI=10.1074/jbc.M502546200;
 Reddig P.J., Xu D., Juliano R.L.;
 "Regulation of p21-activated kinase-independent Rac1 signal
 transduction by Nischarin.";
 J. Biol. Chem. 280:30994-31002(2005).
 [10]
 INTERACTION WITH PKN2.
 PubMed=17403031; DOI=10.1111/j.1471-4159.2007.04485.x;
 Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.;
 "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma
 kinase activation leading to cytoskeleton function and cell migration
 in astrocytes.";
 J. Neurochem. 101:1002-1017(2007).
 [11]
 FUNCTION.
 PubMed=19029984; DOI=10.1038/nm.1879;
 Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H.,
 Tanaka H., Miyoshi J., Takai Y., Fujita T.;
 "Modification of mineralocorticoid receptor function by Rac1 GTPase:
 implication in proteinuric kidney disease.";
 Nat. Med. 14:1370-1376(2008).
 [12]
 INTERACTION WITH SRGAP2, AND ENZYME REGULATION.
 PubMed=19737524; DOI=10.1016/j.cell.2009.06.047;
 Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V.,
 Chen K., Jin W.L., Frost A., Polleux F.;
 "The F-BAR domain of srGAP2 induces membrane protrusions required for
 neuronal migration and morphogenesis.";
 Cell 138:990-1004(2009).
 [13]
 FUNCTION, AND DISRUPTION PHENOTYPE.
 PubMed=19007770; DOI=10.1016/j.ydbio.2008.10.023;
 Chen L., Melendez J., Campbell K., Kuan C.Y., Zheng Y.;
 "Rac1 deficiency in the forebrain results in neural progenitor
 reduction and microcephaly.";
 Dev. Biol. 325:162-170(2009).
 [14]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
 Pancreas, Spleen, and Testis;
 PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
 Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
 Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
 "A tissue-specific atlas of mouse protein phosphorylation and
 expression.";
 Cell 143:1174-1189(2010).
 [15]
 INTERACTION WITH PLXNB3.
 PubMed=20696765; DOI=10.1074/jbc.M110.120451;
 Li X., Lee A.Y.;
 "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility
 through RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
 J. Biol. Chem. 285:32436-32445(2010).
 [16]
 INTERACTION WITH PKN2.
 PubMed=20974804; DOI=10.1128/MCB.01001-10;
 Wallace S.W., Magalhaes A., Hall A.;
 "The Rho target PRK2 regulates apical junction formation in human
 bronchial epithelial cells.";
 Mol. Cell. Biol. 31:81-91(2011).
 [17]
 SUBCELLULAR LOCATION, INTERACTION WITH SH3RF1, AND DEVELOPMENTAL
 STAGE.
 PubMed=22959435; DOI=10.1016/j.celrep.2012.08.007;
 Yang T., Sun Y., Zhang F., Zhu Y., Shi L., Li H., Xu Z.;
 "POSH localizes activated Rac1 to control the formation of cytoplasmic
 dilation of the leading process and neuronal migration.";
 Cell Rep. 2:640-651(2012).
 [18]
 IDENTIFICATION IN A COMPLEX WITH SH3RF1; MAP2K7; MAP3K11; MAPK8IP1 AND
 MAPK8.
 PubMed=23963642; DOI=10.1002/eji.201343635;
 Cunningham C.A., Knudson K.M., Peng B.J., Teixeiro E., Daniels M.A.;
 "The POSH/JIP-1 scaffold network regulates TCR-mediated JNK1 signals
 and effector function in CD8(+) T cells.";
 Eur. J. Immunol. 43:3361-3371(2013).
 -!- FUNCTION: Plasma membrane-associated small GTPase which cycles
     between active GTP-bound and inactive GDP-bound states. In its
     active state, binds to a variety of effector proteins to regulate
     cellular responses such as secretory processes, phagocytosis of
     apoptotic cells, epithelial cell polarization, neurons adhesion,
     migration and differentiation, and growth-factor induced formation
     of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active
     component of the cytosolic factor sigma 1, which is involved in
     stimulation of the NADPH oxidase activity in macrophages.
     Essential for the SPATA13-mediated regulation of cell migration
     and adhesion assembly and disassembly. Stimulates PKN2 kinase
     activity. In concert with RAB7A, plays a role in regulating the
     formation of RBs (ruffled borders) in osteoclasts. In glioma
     cells, promotes cell migration and invasion. Required for atypical
     chemokine receptor ACKR2-induced LIMK1-PAK1-dependent
     phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2
     from endosomal compartment to cell membrane, increasing its
     efficiency in chemokine uptake and degradation. In podocytes,
     promotes nuclear shuttling of NR3C2; this modulation is required
     for a proper kidney functioning. In synapses, seems to mediate the
     regulation of F-actin cluster formation performed by SHANK3.
     {ECO:0000250|UniProtKB:P63000, ECO:0000269|PubMed:19007770,
     ECO:0000269|PubMed:19029984}.
 -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
     factors (GEFs) which promote the exchange of bound GDP for free
     GTP, GTPase activating proteins (GAPs) which increase the GTP
     hydrolysis activity, and GDP dissociation inhibitors which inhibit
     the dissociation of the nucleotide from the GTPase. GTP hydrolysis
     is stimulated by ARHGAP30 (By similarity). {ECO:0000250}.
 -!- SUBUNIT: Interacts with the GEF proteins PREX1, FARP1, FARP2,
     DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and
     GTP, and therefore activate it. Part of a quaternary complex
     containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G)
     and some atypical PKC protein (PRKCI or PRKCZ), which plays a
     central role in epithelial cell polarization. Found in a trimeric
     complex composed of DOCK1 and ELMO1, which plays a central role in
     phagocytosis of apoptotic cells. Interacts with RALBP1 via its
     effector domain. Interacts with BAIAP2, BAIAP2L1, PLXNB1,
     CYFIP1/SRA-1 and DEF6. Probably found in a ternary complex
     composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM; the
     interaction requires PAK1. Interacts with TBC1D2. Interacts with
     UNKL. Interacts with USP6. Interacts with SPATA13. Interacts with
     ITGB4. Interacts with the GTP-bound form of RAB7A. Interacts with
     ARHGEF2. Interacts with ARHGEF16; mediates activation of RAC1 by
     EPHA2. Interacts with NOXA1. Interacts with S100A8 and
     calprotectin (S100A8/9). Interacts with ARHGDIA; the interaction
     is induced by SEMA5A, mediated through PLXNB3 and inactivates and
     stabilizes RAC1. Interacts with PACSIN2. Interacts with ITGB1BP1
     (By similarity). Interacts with the GEF protein RASGRF2, which
     promotes the exchange between GDP and GTP, and therefore activates
     it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent
     manner. Part of a complex with MAP2K3, MAP3K3 and CCM2. Interacts
     with NISCH. Interacts with PIP5K1A. Interacts (GTP-bound form
     preferentially) with PKN2 (via the REM repeats); the interaction
     stimulates autophosphorylation and phosphorylation of PKN2.
     Interacts with SRGAP2. Interacts with PLXNB3. Interacts (when
     active) with PPP5C (via TPR repeats); activates PPP5C phosphatase
     activity and translocates PPP5C to the cell membrane. Interacts
     with RAPH1 (via Ras associating and PH domains) (By similarity).
     Interacts with MTSS1L (via IMD domain); this interaction may be
     important to potentiate PDGF-induced RAC1 activation. Interacts
     (GTP-bound form) with SH3RF3. Interacts with PAK2 (By similarity).
     Interacts (GTP-bound form) with SH3RF1 (PubMed:22959435). Found in
     a complex with SH3RF1, MAPK8IP1/JIP1, MAP3K11/MLK3, MAP2K7/MKK7
     and MAPK8/JNK1 (PubMed:23963642). Interacts (both active GTP- or
     inactive GDP-bound forms) with SH3RF2 (By similarity).
     {ECO:0000250|UniProtKB:P63000, ECO:0000250|UniProtKB:Q6RUV5,
     ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:10934474,
     ECO:0000269|PubMed:10934475, ECO:0000269|PubMed:14634666,
     ECO:0000269|PubMed:16002401, ECO:0000269|PubMed:17403031,
     ECO:0000269|PubMed:19737524, ECO:0000269|PubMed:20696765,
     ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:22959435,
     ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:9707409}.
 -!- INTERACTION:
     Q62108:Dlg4; NbExp=3; IntAct=EBI-413646, EBI-300895;
     Q13153:PAK1 (xeno); NbExp=3; IntAct=EBI-413646, EBI-1307;
     Q8BTI9:Pik3cb; NbExp=3; IntAct=EBI-413646, EBI-644672;
     P08228:Sod1; NbExp=4; IntAct=EBI-413646, EBI-1635090;
 -!- SUBCELLULAR LOCATION: Cell membrane
     {ECO:0000250|UniProtKB:P63000}; Lipid-anchor
     {ECO:0000250|UniProtKB:P63000}; Cytoplasmic side
     {ECO:0000250|UniProtKB:P63000}. Melanosome
     {ECO:0000250|UniProtKB:P63000}. Cytoplasm
     {ECO:0000250|UniProtKB:P63000}. Cell projection, lamellipodium
     {ECO:0000269|PubMed:22959435}. Note=Inner surface of plasma
     membrane possibly with attachment requiring prenylation of the C-
     terminal cysteine (By similarity). Found in the ruffled border (a
     late endosomal-like compartment in the plasma membrane) of bone-
     resorbing osteoclasts (By similarity). Localizes to the
     lamellipodium in a SH3RF1-dependent manner.
     {ECO:0000250|UniProtKB:P63000, ECO:0000269|PubMed:22959435}.
 -!- TISSUE SPECIFICITY: Widely expressed.
     {ECO:0000269|PubMed:1905006}.
 -!- DEVELOPMENTAL STAGE: Expressed in the neocortical neurons in the
     developing brain. {ECO:0000269|PubMed:22959435}.
 -!- DOMAIN: The effector region mediates interaction with DEF6.
     {ECO:0000250}.
 -!- PTM: GTP-bound active form is ubiquitinated by HACE1, leading to
     its degradation by the proteasome. {ECO:0000250}.
 -!- DISRUPTION PHENOTYPE: Conditional knockout of Rac1 in the
     telencephalic ventricular zone of embryos leads to primary
     microcephaly. Self-renewal, survival, and differentiation of
     telencephalic neural progenitor cells is affected.
     {ECO:0000269|PubMed:19007770}.
 -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
     {ECO:0000305}.
 -----------------------------------------------------------------------
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 EMBL; X57277; CAA40545.1; -; mRNA.
 EMBL; AK009017; BAB26027.1; -; mRNA.
 EMBL; AK011072; BAB69451.1; -; mRNA.
 EMBL; AK034601; BAC28767.1; -; mRNA.
 EMBL; AK047969; BAC33203.1; -; mRNA.
 EMBL; AK088825; BAC40596.1; -; mRNA.
 EMBL; BC003828; AAH03828.1; -; mRNA.
 EMBL; BC051053; AAH51053.1; -; mRNA.
 CCDS; CCDS19843.1; -.
 PIR; A60347; A60347.
 RefSeq; NP_033033.1; NM_009007.2.
 UniGene; Mm.292510; -.
 UniGene; Mm.469963; -.
 UniGene; Mm.475073; -.
 ProteinModelPortal; P63001; -.
 SMR; P63001; -.
 BioGrid; 202556; 32.
 CORUM; P63001; -.
 DIP; DIP-31545N; -.
 IntAct; P63001; 36.
 MINT; P63001; -.
 STRING; 10090.ENSMUSP00000079380; -.
 BindingDB; P63001; -.
 ChEMBL; CHEMBL5628; -.
 iPTMnet; P63001; -.
 PhosphoSitePlus; P63001; -.
 SwissPalm; P63001; -.
 EPD; P63001; -.
 MaxQB; P63001; -.
 PaxDb; P63001; -.
 PRIDE; P63001; -.
 Ensembl; ENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847.
 GeneID; 19353; -.
 KEGG; mmu:19353; -.
 UCSC; uc009akk.1; mouse.
 CTD; 5879; -.
 MGI; MGI:97845; Rac1.
 eggNOG; KOG0393; Eukaryota.
 eggNOG; COG1100; LUCA.
 GeneTree; ENSGT00760000118978; -.
 HOGENOM; HOG000233974; -.
 HOVERGEN; HBG009351; -.
 InParanoid; P63001; -.
 KO; K04392; -.
 PhylomeDB; P63001; -.
 TreeFam; TF101109; -.
 Reactome; R-MMU-114604; GPVI-mediated activation cascade.
 Reactome; R-MMU-1433557; Signaling by SCF-KIT.
 Reactome; R-MMU-193648; NRAGE signals death through JNK.
 Reactome; R-MMU-194840; Rho GTPase cycle.
 Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
 Reactome; R-MMU-2424491; DAP12 signaling.
 Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
 Reactome; R-MMU-376172; DSCAM interactions.
 Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
 Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
 Reactome; R-MMU-3928664; Ephrin signaling.
 Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
 Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
 Reactome; R-MMU-4086400; PCP/CE pathway.
 Reactome; R-MMU-416482; G alpha (12/13) signalling events.
 Reactome; R-MMU-416550; Sema4D mediated inhibition of cell attachment and migration.
 Reactome; R-MMU-418885; DCC mediated attractive signaling.
 Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
 Reactome; R-MMU-445144; Signal transduction by L1.
 Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
 Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
 Reactome; R-MMU-5625900; RHO GTPases activate CIT.
 Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
 Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
 Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
 Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
 Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
 Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
 Reactome; R-MMU-6798695; Neutrophil degranulation.
 Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
 Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
 Reactome; R-MMU-9032759; NTRK2 activates RAC1.
 Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
 ChiTaRS; Rac1; mouse.
 PRO; PR:P63001; -.
 Proteomes; UP000000589; Chromosome 5.
 Bgee; ENSMUSG00000001847; -.
 CleanEx; MM_RAC1; -.
 ExpressionAtlas; P63001; baseline and differential.
 Genevisible; P63001; MM.
 GO; GO:0042995; C:cell projection; IDA:MGI.
 GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
 GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
 GO; GO:0005829; C:cytosol; ISS:UniProtKB.
 GO; GO:0043197; C:dendritic spine; ISO:MGI.
 GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
 GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
 GO; GO:0000139; C:Golgi membrane; ISO:MGI.
 GO; GO:0060091; C:kinocilium; IDA:MGI.
 GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO; GO:0016020; C:membrane; IDA:MGI.
 GO; GO:0005634; C:nucleus; IDA:UniProtKB.
 GO; GO:0000242; C:pericentriolar material; IDA:MGI.
 GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
 GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
 GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
 GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
 GO; GO:0051117; F:ATPase binding; ISO:MGI.
 GO; GO:0019899; F:enzyme binding; ISO:MGI.
 GO; GO:0005525; F:GTP binding; IDA:MGI.
 GO; GO:0030742; F:GTP-dependent protein binding; IPI:UniProtKB.
 GO; GO:0003924; F:GTPase activity; IDA:MGI.
 GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
 GO; GO:0019901; F:protein kinase binding; ISO:MGI.
 GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
 GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; ISS:UniProtKB.
 GO; GO:0031996; F:thioesterase binding; ISO:MGI.
 GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
 GO; GO:0007015; P:actin filament organization; ISO:MGI.
 GO; GO:0030041; P:actin filament polymerization; IDA:MGI.
 GO; GO:0048532; P:anatomical structure arrangement; IMP:MGI.
 GO; GO:0002093; P:auditory receptor cell morphogenesis; IMP:MGI.
 GO; GO:0007411; P:axon guidance; IMP:MGI.
 GO; GO:0045453; P:bone resorption; ISO:MGI.
 GO; GO:0007155; P:cell adhesion; IDA:MGI.
 GO; GO:0016477; P:cell migration; IDA:MGI.
 GO; GO:0048870; P:cell motility; ISS:UniProtKB.
 GO; GO:0008283; P:cell proliferation; ISO:MGI.
 GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
 GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
 GO; GO:0021894; P:cerebral cortex GABAergic interneuron development; IGI:MGI.
 GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
 GO; GO:0006935; P:chemotaxis; ISO:MGI.
 GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
 GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
 GO; GO:0016358; P:dendrite development; IDA:MGI.
 GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
 GO; GO:0071542; P:dopaminergic neuron differentiation; IGI:MGI.
 GO; GO:0021831; P:embryonic olfactory bulb interneuron precursor migration; IMP:MGI.
 GO; GO:0006897; P:endocytosis; IDA:MGI.
 GO; GO:0043652; P:engulfment of apoptotic cell; IDA:BHF-UCL.
 GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
 GO; GO:0030900; P:forebrain development; IDA:UniProtKB.
 GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IGI:MGI.
 GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:MGI.
 GO; GO:0048873; P:homeostasis of number of cells within a tissue; IGI:MGI.
 GO; GO:0006972; P:hyperosmotic response; IDA:MGI.
 GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
 GO; GO:0051668; P:localization within membrane; ISO:MGI.
 GO; GO:0002551; P:mast cell chemotaxis; ISO:MGI.
 GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IMP:ParkinsonsUK-UCL.
 GO; GO:0032707; P:negative regulation of interleukin-23 production; ISO:MGI.
 GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
 GO; GO:0048812; P:neuron projection morphogenesis; IGI:ParkinsonsUK-UCL.
 GO; GO:0035567; P:non-canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
 GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
 GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
 GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
 GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:MGI.
 GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
 GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
 GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
 GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
 GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
 GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:MGI.
 GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
 GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
 GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
 GO; GO:0072659; P:protein localization to plasma membrane; IDA:MGI.
 GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
 GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
 GO; GO:0022604; P:regulation of cell morphogenesis; IGI:MGI.
 GO; GO:0008361; P:regulation of cell size; ISO:MGI.
 GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
 GO; GO:0010591; P:regulation of lamellipodium assembly; ISO:MGI.
 GO; GO:0014041; P:regulation of neuron maturation; IGI:MGI.
 GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
 GO; GO:0060263; P:regulation of respiratory burst; ISO:MGI.
 GO; GO:0051492; P:regulation of stress fiber assembly; ISO:MGI.
 GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
 GO; GO:0031529; P:ruffle organization; ISO:MGI.
 GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
 GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
 GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
 GO; GO:0051932; P:synaptic transmission, GABAergic; IGI:MGI.
 GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IGI:MGI.
 InterPro; IPR027417; P-loop_NTPase.
 InterPro; IPR005225; Small_GTP-bd_dom.
 InterPro; IPR001806; Small_GTPase.
 InterPro; IPR003578; Small_GTPase_Rho.
 Pfam; PF00071; Ras; 1.
 SUPFAM; SSF52540; SSF52540; 1.
 TIGRFAMs; TIGR00231; small_GTP; 1.
 PROSITE; PS51420; RHO; 1.
 1: Evidence at protein level;
 Cell membrane; Cell projection; Complete proteome; Cytoplasm;
 GTP-binding; Isopeptide bond; Lipoprotein; Membrane; Methylation;
 Nucleotide-binding; Prenylation; Reference proteome; Ubl conjugation.
 CHAIN         1    189       Ras-related C3 botulinum toxin substrate
                              1.
                              /FTId=PRO_0000042038.
 PROPEP      190    192       Removed in mature form. {ECO:0000250}.
                              /FTId=PRO_0000042039.
 NP_BIND      13     18       GTP. {ECO:0000250|UniProtKB:P63000}.
 NP_BIND      30     35       GTP. {ECO:0000250|UniProtKB:P63000}.
 NP_BIND     116    118       GTP. {ECO:0000250|UniProtKB:P63000}.
 NP_BIND     159    160       GTP. {ECO:0000250|UniProtKB:P63000}.
 MOTIF        32     40       Effector region. {ECO:0000255}.
 BINDING      60     60       GTP; via amide nitrogen.
                              {ECO:0000250|UniProtKB:P63000}.
 MOD_RES     189    189       Cysteine methyl ester. {ECO:0000250}.
 LIPID       189    189       S-geranylgeranyl cysteine.
                              {ECO:0000250|UniProtKB:P63000}.
 CROSSLNK    147    147       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in ubiquitin).
                              {ECO:0000250|UniProtKB:P63000}.
 MUTAGEN      12     12       G->V: Constitutively active. Interacts
                              with PARD6 proteins.
                              {ECO:0000269|PubMed:10934474}.
 SEQUENCE   192 AA;  21450 MW;  ACEDF83A45E5EA67 CRC64;
 MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG
 QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR
 DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP
 PVKKRKRKCL LL

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