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P63001 (RAC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related C3 botulinum toxin substrate 1
Alternative name(s):
p21-Rac1
Gene names
Name:Rac1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. 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 By similarity.

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.

Subunit structure

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. Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM; the interaction requires PAK1 By similarity. Interacts with TBC1D2 By similarity. Part of a complex with MAP2K3, MAP3K3 and CCM2. Interacts with NISCH. Interacts with UNKL By similarity. Interacts with USP6 By similarity. Interacts with SPATA13 By similarity. Interacts with ARHGEF16; mediates activation of RAC1 by EPHA2. Interacts with ITGB4 By similarity. Interacts with PIP5K1A. Interacts (GTP-bound form preferentially) with PKN2 (via the REM repeats); the interaction stimulates autophosphorylation and phosphorylation of PKN2. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

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. Ref.1

Domain

The effector region mediates interaction with DEF6 By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMIsopeptide bond
Lipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processWnt receptor signaling pathway, planar cell polarity pathway

Inferred from genetic interaction. Source: MGI

anatomical structure arrangement

Inferred from mutant phenotype. Source: MGI

auditory receptor cell morphogenesis

Inferred from mutant phenotype. Source: MGI

axon guidance

Inferred from mutant phenotype. Source: MGI

cell-cell junction organization

Inferred from mutant phenotype. Source: MGI

cerebral cortex radially oriented cell migration

Inferred from mutant phenotype. Source: MGI

cochlea morphogenesis

Inferred from mutant phenotype. Source: MGI

cytoskeleton organization

Inferred from direct assay. Source: MGI

dendrite development

Inferred from direct assay. Source: MGI

dopaminergic neuron differentiation

Inferred from genetic interaction. Source: MGI

embryonic olfactory bulb interneuron precursor migration

Inferred from mutant phenotype. Source: MGI

engulfment of apoptotic cell

Inferred from direct assay. Source: BHF-UCL

epithelial cell morphogenesis

Inferred from mutant phenotype. Source: MGI

hyperosmotic response

Inferred from direct assay. Source: MGI

lamellipodium assembly

Inferred from direct assay. Source: MGI

positive regulation of actin filament polymerization

Inferred from direct assay. Source: MGI

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype. Source: MGI

regulation of cell migration

Inferred from mutant phenotype. Source: MGI

small GTPase mediated signal transduction

Inferred from direct assay. Source: MGI

substrate adhesion-dependent cell spreading

Inferred from direct assay. Source: MGI

   Cellular componentcytosol

Traceable author statement. Source: Reactome

extrinsic to plasma membrane

Inferred from direct assay. Source: MGI

lamellipodium

Inferred from direct assay. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane fraction

Inferred from direct assay. Source: MGI

   Molecular functionGTP binding

Inferred from direct assay. Source: MGI

GTP-dependent protein binding

Inferred from physical interaction. Source: UniProtKB

GTPase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg4Q621082EBI-413646,EBI-300895

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Ras-related C3 botulinum toxin substrate 1
PRO_0000042038
Propeptide190 – 1923Removed in mature form By similarity
PRO_0000042039

Regions

Nucleotide binding10 – 178GTP By similarity
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding115 – 1184GTP By similarity
Motif32 – 409Effector region Potential

Amino acid modifications

Modified residue711Phosphoserine By similarity
Modified residue1891Cysteine methyl ester By similarity
Lipidation1891S-geranylgeranyl cysteine By similarity
Cross-link147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis121G → V: Constitutively active. Interacts with PARD6 proteins. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P63001 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: ACEDF83A45E5EA67

FASTA19221,450
        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 

« Hide

References

« Hide 'large scale' references
[1]"The murine rac1 gene: cDNA cloning, tissue distribution and regulated expression of rac1 mRNA by disassembly of actin microfilaments."
Moll J., Sansig G., Fattori E., van der Putten H.
Oncogene 6:863-866(1991) [PubMed: 1905006] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Thymus.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head, Liver, Thymus and Tongue.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[4]"The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
Joberty G., Petersen C., Gao L., Macara I.G.
Nat. Cell Biol. 2:531-539(2000) [PubMed: 10934474] [Abstract]
Cited for: INTERACTION WITH PARD6A, MUTAGENESIS OF GLY-12.
[5]"A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity."
Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.
Nat. Cell Biol. 2:540-547(2000) [PubMed: 10934475] [Abstract]
Cited for: INTERACTION WITH PARD6B.
[6]"The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways."
Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.
Curr. Biol. 8:935-938(1998) [PubMed: 9707409] [Abstract]
Cited for: INTERACTION WITH RASGRF2.
[7]"Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly."
Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C., Carpenter C.L.
Curr. Biol. 10:153-156(2000) [PubMed: 10679324] [Abstract]
Cited for: INTERACTION WITH PIP5K1A.
[8]"Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock."
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.
Nat. Cell Biol. 5:1104-1110(2003) [PubMed: 14634666] [Abstract]
Cited for: INTERACTION WITH MAP3K3; MAP2K3 AND CCM2.
[9]"Regulation of p21-activated kinase-independent Rac1 signal transduction by Nischarin."
Reddig P.J., Xu D., Juliano R.L.
J. Biol. Chem. 280:30994-31002(2005) [PubMed: 16002401] [Abstract]
Cited for: INTERACTION WITH NISCH.
[10]"Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes."
Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.
J. Neurochem. 101:1002-1017(2007) [PubMed: 17403031] [Abstract]
Cited for: INTERACTION WITH PKN2.
[11]"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
Wallace S.W., Magalhaes A., Hall A.
Mol. Cell. Biol. 31:81-91(2011) [PubMed: 20974804] [Abstract]
Cited for: INTERACTION WITH PKN2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57277 mRNA. Translation: CAA40545.1.
AK009017 mRNA. Translation: BAB26027.1.
AK011072 mRNA. Translation: BAB69451.1.
AK034601 mRNA. Translation: BAC28767.1.
AK047969 mRNA. Translation: BAC33203.1.
AK088825 mRNA. Translation: BAC40596.1.
BC003828 mRNA. Translation: AAH03828.1.
BC051053 mRNA. Translation: AAH51053.1.
IPIIPI00761613.
PIRA60347.
RefSeqNP_033033.1. NM_009007.2.
UniGeneMm.292510.
Mm.342177.

3D structure databases

ProteinModelPortalP63001.
SMRP63001. Positions 1-177.
ModBaseSearch...

Protein-protein interaction databases

IntActP63001. 17 interactions.
MINTMINT-1602774.
STRINGP63001.

PTM databases

PhosphoSiteP63001.

Proteomic databases

PRIDEP63001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847.
GeneID19353.
KEGGmmu:19353.
UCSCuc007mug.1. mouse.

Organism-specific databases

CTD5879.
MGIMGI:97845. Rac1.

Phylogenomic databases

eggNOGroNOG06989.
HOVERGENHBG009351.
OrthoDBEOG466VN1.
PhylomeDBP63001.

Enzyme and pathway databases

ReactomeREACT_115492. Developmental Biology.

Gene expression databases

ArrayExpressP63001.
BgeeP63001.
CleanExMM_RAC1.
GenevestigatorP63001.
GermOnlineENSMUSG00000001847. Mus musculus.

Family and domain databases

InterProIPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
KOK04392.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. Small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296387.
SOURCESearch...

Entry information

Entry nameRAC1_MOUSE
AccessionPrimary (citable) accession number: P63001
Secondary accession number(s): O95501, P15154, Q9BTB4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families