P63001 (RAC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related C3 botulinum toxin substrate 1

Alternative name(s):
p21-Rac1

Gene names

Name:

Rac1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Isopeptide bond Lipoprotein Methylation Phosphoprotein Prenylation Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Wnt 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 component	cytosol 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 function	GTP 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
Dlg4	Q62108	2	EBI-413646,EBI-300895

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 189	189	Ras-related C3 botulinum toxin substrate 1		PRO_0000042038
	Propeptide	190 – 192	3	Removed in mature form By similarity		PRO_0000042039
Regions
	Nucleotide binding	10 – 17	8	GTP By similarity
	Nucleotide binding	57 – 61	5	GTP By similarity
	Nucleotide binding	115 – 118	4	GTP By similarity
	Motif	32 – 40	9	Effector region Potential
Amino acid modifications
	Modified residue	71	1	Phosphoserine By similarity
	Modified residue	189	1	Cysteine methyl ester By similarity
	Lipidation	189	1	S-geranylgeranyl cysteine By similarity
	Cross-link	147		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Mutagenesis	12	1	G → V: Constitutively active. Interacts with PARD6 proteins. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P63001 [UniParc]. Last modified August 31, 2004. Version 1. Checksum: ACEDF83A45E5EA67	FASTA	192	21,450
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00761613.
PIR	A60347.
RefSeq	NP_033033.1. NM_009007.2.
UniGene	Mm.292510. Mm.342177.
3D structure databases
ProteinModelPortal	P63001.
SMR	P63001. Positions 1-177.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63001. 17 interactions.
MINT	MINT-1602774.
STRING	P63001.
PTM databases
PhosphoSite	P63001.
Proteomic databases
PRIDE	P63001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847.
GeneID	19353.
KEGG	mmu:19353.
UCSC	uc007mug.1. mouse.
Organism-specific databases
CTD	5879.
MGI	MGI:97845. Rac1.
Phylogenomic databases
eggNOG	roNOG06989.
HOVERGEN	HBG009351.
OrthoDB	EOG466VN1.
PhylomeDB	P63001.
Enzyme and pathway databases
Reactome	REACT_115492. Developmental Biology.
Gene expression databases
ArrayExpress	P63001.
Bgee	P63001.
CleanEx	MM_RAC1.
Genevestigator	P63001.
GermOnline	ENSMUSG00000001847. Mus musculus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003578. Small_GTPase_Rho. [Graphical view]
KO	K04392.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00174. RHO. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. Small_GTP. 1 hit.
PROSITE	PS51420. RHO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	296387.
SOURCE	Search...

Entry information

Entry name

RAC1_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program