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UniProtKB/Swiss-Prot entry P63001


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RAC1_MOUSE
Primary accession number P63001
Secondary accession numbers O95501 P15154 Q9BTB4
Integrated into Swiss-Prot on August 31, 2004
Sequence was last modified on August 31, 2004 (Sequence version 1)
Annotations were last modified on    May 26, 2009 (Entry version 66)
Name and origin of the protein
Protein name Ras-related C3 botulinum toxin substrate 1 [Precursor]
Synonym p21-Rac1
Gene name
Name: Rac1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Thymus;
PubMed=1905006 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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 PARD6A, AND MUTAGENESIS OF GLY-12.
DOI=10.1038/35019573; PubMed=10934474 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
INTERACTION WITH PARD6B.
DOI=10.1038/35019592; PubMed=10934475 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
INTERACTION WITH RASGRF2.
DOI=10.1016/S0960-9822(07)00376-4; PubMed=9707409 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
INTERACTION WITH MAP3K3; MAP2K3 AND CCM2.
DOI=10.1038/ncb1071; PubMed=14634666 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
INTERACTION WITH NISCH.
DOI=10.1074/jbc.M502546200; PubMed=16002401 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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 and growth-factor induced formation of membrane ruffles.
  • 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.
  • SUBUNIT: Interacts with the GEF proteins PREX1, RASGRF2, DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and GTP, and therefore activate it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent manner. 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. Interacts with NOXA1. Interacts with ARHGEF2 (By similarity). Part of a complex with MAP2K3, MAP3K3 and CCM2. Interacts with NISCH.
  • INTERACTION:
    Q13153:PAK1 (xeno); NbExp=1; IntAct=EBI-413646, EBI-1307;
  • SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity). Melanosome (By similarity). Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine (By similarity).
  • TISSUE SPECIFICITY: Widely expressed.
  • DOMAIN: The effector region mediates interaction with DEF6 (By similarity).
  • SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X57277; CAA40545.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK009017; BAB26027.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011072; BAB69451.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK034601; BAC28767.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK047969; BAC33203.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088825; BAC40596.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003828; AAH03828.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC051053; AAH51053.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00761613; -.
PIR A60347; A60347.
RefSeq NP_033033.1; -.
UniGene Mm.292510
3D structure databases
SMR P63001; 2-189.
ModBase P63001.
Protein-protein interaction databases
IntAct P63001; 16.
PTM databases
PhosphoSite P63001; -.
Organism-specific databases
MGI MGI:97845; Rac1.
Gene expression databases
ArrayExpress P63001; -.
Bgee P63001; -.
CleanEx MM_RAC1; -.
GermOnline ENSMUSG00000001847; Mus musculus.
Ontologies
GO
GO:0019897; Cellular component: extrinsic to plasma membrane (inferred from direct assay from MGI).
GO:0030027; Cellular component: lamellipodium (inferred from direct assay from MGI).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005624; Cellular component: membrane fraction (inferred from direct assay from MGI).
GO:0005525; Molecular function: GTP binding (inferred from direct assay from MGI).
GO:0003924; Molecular function: GTPase activity (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007411; Biological process: axon guidance (inferred from mutant phenotype from MGI).
GO:0007155; Biological process: cell adhesion (inferred from direct assay from MGI).
GO:0021799; Biological process: cerebral cortex radially oriented cell migration (inferred from mutant phenotype from MGI).
GO:0016358; Biological process: dendrite development (inferred from direct assay from MGI).
GO:0021831; Biological process: embryonic olfactory bulb interneuron precursor migration (inferred from mutant phenotype from MGI).
GO:0006897; Biological process: endocytosis (inferred from direct assay from MGI).
GO:0006972; Biological process: hyperosmotic response (inferred from direct assay from MGI).
GO:0030032; Biological process: lamellipodium assembly (inferred from direct assay from MGI).
GO:0030838; Biological process: positive regulation of actin filament polymerization (inferred from direct assay from MGI).
GO:0043552; Biological process: positive regulation of phosphoinositide 3-kinase activity (inferred from mutant phenotype from MGI).
GO:0030334; Biological process: regulation of cell migration (inferred from mutant phenotype from MGI).
GO:0007264; Biological process: small GTPase mediated signal transduction (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR003578; GTPase_Rho.
IPR013753; Ras.
IPR001806; Ras_GTPase.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.
Pfam PF00071; Ras; 1.
Pfam graphical view of domain structure.
PRINTS PR00449; RASTRNSFRMNG.
SMART SM00174; RHO; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS51420; RHO; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P63001; -.
Genome annotation databases
Ensembl ENSMUSG00000001847; Mus musculus. [Contig view]
GeneID 19353; -.
KEGG mmu:19353; -.
Phylogenomic databases
HOVERGEN P63001; -.
Other
NextBio 296387; -.
SOURCE Rac1; Mus musculus.
ProtoNet P63001.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   189  189     Ras-related C3 botulinum toxin substrate 1. PRO_0000042038
PROPEP   190   192  3     Removed in mature form (By similarity). PRO_0000042039
NP_BIND   10    17  8     GTP (By similarity). 
NP_BIND   57    61  5     GTP (By similarity). 
NP_BIND   115   118  4     GTP (By similarity). 
MOTIF   32    40  9     Effector region (Potential). 
MOD_RES   71    71        Phosphoserine (By similarity). 
MOD_RES   189   189        Cysteine methyl ester (By similarity). 
LIPID   189   189        S-geranylgeranyl cysteine (By similarity). 
MUTAGEN   12    12        G->V: Constitutively active. Interacts with PARD6 proteins. 
Sequence information
Length: 192 AA [This is the length of the unprocessed precursor] Molecular weight: 21450 Da [This is the MW of the unprocessed precursor] CRC64: ACEDF83A45E5EA67 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG 

        70         80         90        100        110        120 
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR 

       130        140        150        160        170        180 
DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP 

       190 
PVKKRKRKCL LL 

P63001 in FASTA format

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