RAC1_MOUSE
ID RAC1_MOUSE Reviewed; 192 AA.
AC P63001; O95501; P15154; Q9BTB4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Ras-related C3 botulinum toxin substrate 1 {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000269|PubMed:24352656, ECO:0000269|PubMed:26969129};
DE AltName: Full=p21-Rac1;
DE Flags: Precursor;
GN Name=Rac1 {ECO:0000312|MGI:MGI:97845};
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 TISSUE SPECIFICITY.
RC TISSUE=Thymus;
RX PubMed=1905006;
RA Moll J., Sansig G., Fattori E., van der Putten H.;
RT "The murine rac1 gene: cDNA cloning, tissue distribution and regulated
RT expression of rac1 mRNA by disassembly of actin microfilaments.";
RL Oncogene 6:863-866(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Liver, Thymus, and Tongue;
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=Czech II, and 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 RASGRF2.
RX PubMed=9707409; DOI=10.1016/s0960-9822(07)00376-4;
RA Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.;
RT "The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent
RT mitogen-activated protein kinase pathways.";
RL Curr. Biol. 8:935-938(1998).
RN [5]
RP INTERACTION WITH PARD6A, AND MUTAGENESIS OF GLY-12.
RX PubMed=10934474; DOI=10.1038/35019573;
RA Joberty G., Petersen C., Gao L., Macara I.G.;
RT "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to
RT Cdc42.";
RL Nat. Cell Biol. 2:531-539(2000).
RN [6]
RP INTERACTION WITH PARD6B.
RX PubMed=10934475; DOI=10.1038/35019582;
RA Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.;
RT "A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC
RT signalling and cell polarity.";
RL Nat. Cell Biol. 2:540-547(2000).
RN [7]
RP INTERACTION WITH PIP5K1A.
RX PubMed=10679324; DOI=10.1016/s0960-9822(00)00315-8;
RA Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C.,
RA Carpenter C.L.;
RT "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-
RT dependent actin assembly.";
RL Curr. Biol. 10:153-156(2000).
RN [8]
RP FUNCTION.
RX PubMed=12695502; DOI=10.1083/jcb.200211002;
RA Zhang H., Webb D.J., Asmussen H., Horwitz A.F.;
RT "Synapse formation is regulated by the signaling adaptor GIT1.";
RL J. Cell Biol. 161:131-142(2003).
RN [9]
RP INTERACTION WITH MAP3K3; MAP2K3 AND CCM2.
RX PubMed=14634666; DOI=10.1038/ncb1071;
RA Uhlik M.T., Abell A.N., Johnson N.L., Sun W., Cuevas B.D., Lobel-Rice K.E.,
RA Horne E.A., Dell'Acqua M.L., Johnson G.L.;
RT "Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic
RT shock.";
RL Nat. Cell Biol. 5:1104-1110(2003).
RN [10]
RP INTERACTION WITH NISCH.
RX PubMed=16002401; DOI=10.1074/jbc.m502546200;
RA Reddig P.J., Xu D., Juliano R.L.;
RT "Regulation of p21-activated kinase-independent Rac1 signal transduction by
RT Nischarin.";
RL J. Biol. Chem. 280:30994-31002(2005).
RN [11]
RP INTERACTION WITH PKN2.
RX PubMed=17403031; DOI=10.1111/j.1471-4159.2007.04485.x;
RA Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.;
RT "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase
RT activation leading to cytoskeleton function and cell migration in
RT astrocytes.";
RL J. Neurochem. 101:1002-1017(2007).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=17116687; DOI=10.1128/mcb.00756-06;
RA Cho Y.J., Cunnick J.M., Yi S.J., Kaartinen V., Groffen J., Heisterkamp N.;
RT "Abr and Bcr, two homologous Rac GTPase-activating proteins, control
RT multiple cellular functions of murine macrophages.";
RL Mol. Cell. Biol. 27:899-911(2007).
RN [13]
RP FUNCTION.
RX PubMed=19029984; DOI=10.1038/nm.1879;
RA Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H.,
RA Miyoshi J., Takai Y., Fujita T.;
RT "Modification of mineralocorticoid receptor function by Rac1 GTPase:
RT implication in proteinuric kidney disease.";
RL Nat. Med. 14:1370-1376(2008).
RN [14]
RP INTERACTION WITH SRGAP2, AND ACTIVITY REGULATION.
RX PubMed=19737524; DOI=10.1016/j.cell.2009.06.047;
RA Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V., Chen K.,
RA Jin W.L., Frost A., Polleux F.;
RT "The F-BAR domain of srGAP2 induces membrane protrusions required for
RT neuronal migration and morphogenesis.";
RL Cell 138:990-1004(2009).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19007770; DOI=10.1016/j.ydbio.2008.10.023;
RA Chen L., Melendez J., Campbell K., Kuan C.Y., Zheng Y.;
RT "Rac1 deficiency in the forebrain results in neural progenitor reduction
RT and microcephaly.";
RL Dev. Biol. 325:162-170(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [17]
RP INTERACTION WITH PLXNB3.
RX PubMed=20696765; DOI=10.1074/jbc.m110.120451;
RA Li X., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through
RT RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
RL J. Biol. Chem. 285:32436-32445(2010).
RN [18]
RP 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 [19]
RP SUBCELLULAR LOCATION, INTERACTION WITH SH3RF1, AND DEVELOPMENTAL STAGE.
RX PubMed=22959435; DOI=10.1016/j.celrep.2012.08.007;
RA Yang T., Sun Y., Zhang F., Zhu Y., Shi L., Li H., Xu Z.;
RT "POSH localizes activated Rac1 to control the formation of cytoplasmic
RT dilation of the leading process and neuronal migration.";
RL Cell Rep. 2:640-651(2012).
RN [20]
RP IDENTIFICATION IN A COMPLEX WITH SH3RF1; MAP2K7; MAP3K11; MAPK8IP1 AND
RP MAPK8.
RX PubMed=23963642; DOI=10.1002/eji.201343635;
RA Cunningham C.A., Knudson K.M., Peng B.J., Teixeiro E., Daniels M.A.;
RT "The POSH/JIP-1 scaffold network regulates TCR-mediated JNK1 signals and
RT effector function in CD8(+) T cells.";
RL Eur. J. Immunol. 43:3361-3371(2013).
RN [21]
RP CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24352656; DOI=10.1074/jbc.m113.534636;
RA Raynaud F., Moutin E., Schmidt S., Dahl J., Bertaso F., Boeckers T.M.,
RA Homburger V., Fagni L.;
RT "Rho-GTPase-activating protein interacting with Cdc-42-interacting protein
RT 4 homolog 2 (Rich2): a new Ras-related C3 botulinum toxin substrate 1
RT (Rac1) GTPase-activating protein that controls dendritic spine
RT morphogenesis.";
RL J. Biol. Chem. 289:2600-2609(2014).
RN [22]
RP CATALYTIC ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=26969129; DOI=10.1186/s13041-016-0206-6;
RA Sarowar T., Grabrucker S., Foehr K., Mangus K., Eckert M., Bockmann J.,
RA Boeckers T.M., Grabrucker A.M.;
RT "Enlarged dendritic spines and pronounced neophobia in mice lacking the PSD
RT protein RICH2.";
RL Mol. Brain 9:28-28(2016).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC active GTP-bound and inactive GDP-bound states (PubMed:24352656). In
CC its active state, binds to a variety of effector proteins to regulate
CC cellular responses such as secretory processes, phagocytosis of
CC apoptotic cells, epithelial cell polarization, neurons adhesion,
CC migration and differentiation, and growth-factor induced formation of
CC membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component
CC of the cytosolic factor sigma 1, which is involved in stimulation of
CC the NADPH oxidase activity in macrophages. Essential for the SPATA13-
CC mediated regulation of cell migration and adhesion assembly and
CC disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A,
CC plays a role in regulating the formation of RBs (ruffled borders) in
CC osteoclasts. In glioma cells, promotes cell migration and invasion.
CC Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-
CC dependent phosphorylation of cofilin (CFL1) and for up-regulation of
CC ACKR2 from endosomal compartment to cell membrane, increasing its
CC efficiency in chemokine uptake and degradation. In podocytes, promotes
CC nuclear shuttling of NR3C2; this modulation is required for a proper
CC kidney functioning. In neurons, is involved in dendritic spine
CC formation and synaptic plasticity (PubMed:24352656, PubMed:26969129).
CC In hippocampal neurons, involved in spine morphogenesis and synapse
CC formation, through local activation at synapses by guanine nucleotide
CC exchange factors (GEFs), such as ARHGEF6/ARHGEF7/PIX (PubMed:12695502).
CC In synapses, seems to mediate the regulation of F-actin cluster
CC formation performed by SHANK3. In neurons, plays a crucial role in
CC regulating GABA(A) receptor synaptic stability and hence GABAergic
CC inhibitory synaptic transmission through its role in PAK1 activation
CC and eventually F-actin stabilization (By similarity).
CC {ECO:0000250|UniProtKB:P63000, ECO:0000250|UniProtKB:Q6RUV5,
CC ECO:0000269|PubMed:12695502, ECO:0000269|PubMed:19007770,
CC ECO:0000269|PubMed:19029984, ECO:0000269|PubMed:24352656,
CC ECO:0000269|PubMed:26969129}.
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:0000269|PubMed:24352656, ECO:0000269|PubMed:26969129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:24352656, ECO:0000305|PubMed:26969129};
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. GTP hydrolysis is stimulated by ARHGAP30
CC and ARHGAP44. {ECO:0000269|PubMed:24352656,
CC ECO:0000269|PubMed:26969129}.
CC -!- SUBUNIT: Interacts with the GEF proteins PREX1, FARP1, FARP2, DOCK1,
CC DOCK2 and DOCK7, which promote the exchange between GDP and GTP, and
CC therefore activate it. Part of a quaternary complex containing PARD3,
CC some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC
CC protein (PRKCI or PRKCZ), which plays a central role in epithelial cell
CC polarization. Found in a trimeric complex composed of DOCK1 and ELMO1,
CC which plays a central role in phagocytosis of apoptotic cells.
CC Interacts with RALBP1 via its effector domain. Interacts with BAIAP2,
CC BAIAP2L1, PLXNB1, CYFIP1/SRA-1 and DEF6. Probably found in a ternary
CC complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM; the
CC interaction requires PAK1. Interacts with TBC1D2. Interacts with UNKL.
CC Interacts with USP6. Interacts with SPATA13. Interacts with ITGB4.
CC Interacts with the GTP-bound form of RAB7A. Interacts with ARHGEF2.
CC Interacts with ARHGEF16; mediates activation of RAC1 by EPHA2.
CC Interacts with NOXA1. Interacts with S100A8 and calprotectin
CC (S100A8/9). Interacts with ARHGDIA; the interaction is induced by
CC SEMA5A, mediated through PLXNB3 and inactivates and stabilizes RAC1.
CC Interacts with PACSIN2. Interacts with ITGB1BP1 (By similarity).
CC Interacts with the GEF protein RASGRF2, which promotes the exchange
CC between GDP and GTP, and therefore activates it. Interacts with PARD6A,
CC PARD6B and PARD6G in a GTP-dependent manner. Part of a complex with
CC MAP2K3, MAP3K3 and CCM2. Interacts with NISCH. Interacts with PIP5K1A.
CC Interacts (GTP-bound form preferentially) with PKN2 (via the REM
CC repeats); the interaction stimulates autophosphorylation and
CC phosphorylation of PKN2. Interacts with SRGAP2. Interacts with PLXNB3.
CC Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C
CC phosphatase activity and translocates PPP5C to the cell membrane.
CC Interacts with RAPH1 (via Ras associating and PH domains) (By
CC similarity). Interacts with MTSS2 (via IMD domain); this interaction
CC may be important to potentiate PDGF-induced RAC1 activation. Interacts
CC (GTP-bound form) with SH3RF3. Interacts with PAK2 (By similarity).
CC Interacts (GTP-bound form) with SH3RF1 (PubMed:22959435). Found in a
CC complex with SH3RF1, MAPK8IP1/JIP1, MAP3K11/MLK3, MAP2K7/MKK7 and
CC MAPK8/JNK1 (PubMed:23963642). Interacts (both active GTP- or inactive
CC GDP-bound forms) with SH3RF2 (By similarity). Interacts (GTP-bound form
CC preferentially) with CYRIB (By similarity). Interacts with DOCK4 (via
CC DOCKER domain); functions as a guanine nucleotide exchange factor (GEF)
CC for RAC1 (By similarity). Interacts with GARRE1 (By similarity).
CC Interacts with RAP1GDS1 (By similarity). {ECO:0000250|UniProtKB:P63000,
CC ECO:0000250|UniProtKB:Q6RUV5, ECO:0000269|PubMed:10679324,
CC ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:10934475,
CC ECO:0000269|PubMed:14634666, ECO:0000269|PubMed:16002401,
CC ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:19737524,
CC ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:20974804,
CC ECO:0000269|PubMed:22959435, ECO:0000269|PubMed:23963642,
CC ECO:0000269|PubMed:9707409}.
CC -!- INTERACTION:
CC P63001; Q62108: Dlg4; NbExp=3; IntAct=EBI-413646, EBI-300895;
CC P63001; P08228: Sod1; NbExp=4; IntAct=EBI-413646, EBI-1635090;
CC P63001; Q13153: PAK1; Xeno; NbExp=3; IntAct=EBI-413646, EBI-1307;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63000};
CC Lipid-anchor {ECO:0000250|UniProtKB:P63000}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P63000}. Melanosome
CC {ECO:0000250|UniProtKB:P63000}. Cytoplasm
CC {ECO:0000269|PubMed:17116687}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:22959435}. Cell projection, dendrite
CC {ECO:0000269|PubMed:24352656}. Synapse {ECO:0000250|UniProtKB:Q6RUV5}.
CC Nucleus {ECO:0000250|UniProtKB:P63000}. Note=Inner surface of plasma
CC membrane possibly with attachment requiring prenylation of the C-
CC terminal cysteine (By similarity). Found in the ruffled border (a late
CC endosomal-like compartment in the plasma membrane) of bone-resorbing
CC osteoclasts (By similarity). Localizes to the lamellipodium in a
CC SH3RF1-dependent manner. In macrophages, cytoplasmic location increases
CC upon CSF1 stimulation (PubMed:17116687). Activation by GTP-binding
CC promotes nuclear localization (By similarity).
CC {ECO:0000250|UniProtKB:P63000, ECO:0000269|PubMed:17116687,
CC ECO:0000269|PubMed:22959435}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:1905006}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the neocortical neurons in the
CC developing brain. {ECO:0000269|PubMed:22959435}.
CC -!- DOMAIN: The effector region mediates interaction with DEF6.
CC {ECO:0000250|UniProtKB:P63000}.
CC -!- PTM: GTP-bound active form is ubiquitinated by HACE1, leading to its
CC degradation by the proteasome. {ECO:0000250|UniProtKB:P63000}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout of Rac1 in the telencephalic
CC ventricular zone of embryos leads to primary microcephaly. Self-
CC renewal, survival, and differentiation of telencephalic neural
CC progenitor cells is affected. {ECO:0000269|PubMed:19007770}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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; X57277; CAA40545.1; -; mRNA.
DR EMBL; AK009017; BAB26027.1; -; mRNA.
DR EMBL; AK011072; BAB69451.1; -; mRNA.
DR EMBL; AK034601; BAC28767.1; -; mRNA.
DR EMBL; AK047969; BAC33203.1; -; mRNA.
DR EMBL; AK088825; BAC40596.1; -; mRNA.
DR EMBL; BC003828; AAH03828.1; -; mRNA.
DR EMBL; BC051053; AAH51053.1; -; mRNA.
DR CCDS; CCDS19843.1; -.
DR PIR; A60347; A60347.
DR RefSeq; NP_033033.1; NM_009007.2.
DR AlphaFoldDB; P63001; -.
DR BMRB; P63001; -.
DR SMR; P63001; -.
DR BioGRID; 202556; 81.
DR CORUM; P63001; -.
DR DIP; DIP-31545N; -.
DR IntAct; P63001; 50.
DR MINT; P63001; -.
DR STRING; 10090.ENSMUSP00000079380; -.
DR BindingDB; P63001; -.
DR ChEMBL; CHEMBL5628; -.
DR iPTMnet; P63001; -.
DR PhosphoSitePlus; P63001; -.
DR SwissPalm; P63001; -.
DR EPD; P63001; -.
DR jPOST; P63001; -.
DR MaxQB; P63001; -.
DR PaxDb; P63001; -.
DR PRIDE; P63001; -.
DR ProteomicsDB; 300344; -.
DR Antibodypedia; 4545; 719 antibodies from 41 providers.
DR DNASU; 19353; -.
DR Ensembl; ENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847.
DR GeneID; 19353; -.
DR KEGG; mmu:19353; -.
DR UCSC; uc009akk.1; mouse.
DR CTD; 5879; -.
DR MGI; MGI:97845; Rac1.
DR VEuPathDB; HostDB:ENSMUSG00000001847; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153500; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P63001; -.
DR PhylomeDB; P63001; -.
DR TreeFam; TF101109; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2424491; DAP12 signaling.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-376172; DSCAM interactions.
DR Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-3928664; Ephrin signaling.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-MMU-418885; DCC mediated attractive signaling.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5625900; RHO GTPases activate CIT.
DR Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9032759; NTRK2 activates RAC1.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 19353; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Rac1; mouse.
DR PRO; PR:P63001; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P63001; protein.
DR Bgee; ENSMUSG00000001847; Expressed in metanephric loop of Henle and 281 other tissues.
DR ExpressionAtlas; P63001; baseline and differential.
DR Genevisible; P63001; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0060091; C:kinocilium; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IDA:MGI.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0031996; F:thioesterase binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0030041; P:actin filament polymerization; IDA:MGI.
DR GO; GO:0048532; P:anatomical structure arrangement; IMP:MGI.
DR GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; IDA:MGI.
DR GO; GO:0002093; P:auditory receptor cell morphogenesis; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0045453; P:bone resorption; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0016477; P:cell migration; IDA:MGI.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR GO; GO:0021894; P:cerebral cortex GABAergic interneuron development; IGI:MGI.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
DR GO; GO:0006935; P:chemotaxis; ISO:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR GO; GO:0016358; P:dendrite development; IDA:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IGI:MGI.
DR GO; GO:0021831; P:embryonic olfactory bulb interneuron precursor migration; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IDA:BHF-UCL.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0030900; P:forebrain development; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:MGI.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IGI:MGI.
DR GO; GO:0006972; P:hyperosmotic response; IDA:MGI.
DR GO; GO:1904936; P:interneuron migration; IMP:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR GO; GO:0051668; P:localization within membrane; ISO:MGI.
DR GO; GO:0002551; P:mast cell chemotaxis; ISO:MGI.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; ISO:MGI.
DR GO; GO:0032707; P:negative regulation of interleukin-23 production; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IGI:ParkinsonsUK-UCL.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:CACAO.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
DR GO; GO:2000386; P:positive regulation of ovarian follicle development; IMP:CACAO.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061344; P:regulation of cell adhesion involved in heart morphogenesis; IMP:CACAO.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
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:0008361; P:regulation of cell size; ISO:MGI.
DR GO; GO:0070376; P:regulation of ERK5 cascade; IDA:MGI.
DR GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0014041; P:regulation of neuron maturation; IGI:MGI.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:1902622; P:regulation of neutrophil migration; IBA:GO_Central.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IMP:CACAO.
DR GO; GO:0060263; P:regulation of respiratory burst; ISO:MGI.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
DR GO; GO:0031529; P:ruffle organization; ISO:MGI.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; ISO:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IGI:MGI.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IGI: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; GTP-binding; Hydrolase;
KW Isopeptide bond; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Nucleus; Prenylation; Reference proteome; Synapse; Ubl conjugation.
FT CHAIN 1..189
FT /note="Ras-related C3 botulinum toxin substrate 1"
FT /id="PRO_0000042038"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT /id="PRO_0000042039"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT MOTIF 179..188
FT /note="Polybasic region; required for nuclear import"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 13..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 30..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 116..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT BINDING 159..160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P63000"
FT MUTAGEN 12
FT /note="G->V: Constitutively active. Interacts with PARD6
FT proteins."
FT /evidence="ECO:0000269|PubMed:10934474"
SQ 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
