RAC2_MOUSE
ID RAC2_MOUSE Reviewed; 192 AA.
AC Q05144; Q3TBC4; Q9D8X9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ras-related C3 botulinum toxin substrate 2;
DE AltName: Full=Protein EN-7;
DE AltName: Full=p21-Rac2;
DE Flags: Precursor;
GN Name=Rac2;
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].
RX PubMed=2189110;
RA Shirsat N.V., Pignolo R.J., Kreider B.L., Rovera G.;
RT "A member of the ras gene superfamily is expressed specifically in T, B and
RT myeloid hemopoietic cells.";
RL Oncogene 5:769-772(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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=C57BL/6J; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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 [5]
RP IDENTIFICATION IN A COMPLEX WITH SH3RF1; MAP3K7; MAP2K7; MAPK8IP1; MAPK8
RP AND MAPK9.
RX PubMed=27084103; DOI=10.4049/jimmunol.1501728;
RA Cunningham C.A., Cardwell L.N., Guan Y., Teixeiro E., Daniels M.A.;
RT "POSH regulates CD4+ T cell differentiation and survival.";
RL J. Immunol. 196:4003-4013(2016).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC an active GTP-bound and inactive GDP-bound state. In active state binds
CC to a variety of effector proteins to regulate cellular responses, such
CC as secretory processes, phagocytose of apoptotic cells and epithelial
CC cell polarization. Augments the production of reactive oxygen species
CC (ROS) by NADPH oxidase.
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.
CC -!- SUBUNIT: Interacts with DOCK2, which may activate it. Interacts with
CC S100A8 and calprotectin (S100A8/9) (By similarity). Found in a complex
CC with SH3RF1, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and
CC MAPK9/JNK2 (PubMed:27084103). Interacts with PAK1 (By similarity).
CC {ECO:0000250|UniProtKB:P15153, ECO:0000269|PubMed:27084103}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Lipid-anchor {ECO:0000250}. Note=Membrane-associated when activated.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; X53247; CAA37337.1; -; mRNA.
DR EMBL; AK007561; BAB25109.1; -; mRNA.
DR EMBL; AK144136; BAE25721.1; -; mRNA.
DR EMBL; AK171321; BAE42390.1; -; mRNA.
DR EMBL; BC005455; AAH05455.1; -; mRNA.
DR CCDS; CCDS27619.1; -.
DR PIR; A60194; A60194.
DR RefSeq; NP_033034.1; NM_009008.3.
DR AlphaFoldDB; Q05144; -.
DR SMR; Q05144; -.
DR BioGRID; 202557; 5.
DR DIP; DIP-41834N; -.
DR IntAct; Q05144; 4.
DR MINT; Q05144; -.
DR STRING; 10090.ENSMUSP00000036384; -.
DR ChEMBL; CHEMBL4523277; -.
DR iPTMnet; Q05144; -.
DR PhosphoSitePlus; Q05144; -.
DR SwissPalm; Q05144; -.
DR EPD; Q05144; -.
DR jPOST; Q05144; -.
DR MaxQB; Q05144; -.
DR PaxDb; Q05144; -.
DR PeptideAtlas; Q05144; -.
DR PRIDE; Q05144; -.
DR ProteomicsDB; 300294; -.
DR Antibodypedia; 25898; 412 antibodies from 35 providers.
DR DNASU; 19354; -.
DR Ensembl; ENSMUST00000043214; ENSMUSP00000036384; ENSMUSG00000033220.
DR GeneID; 19354; -.
DR KEGG; mmu:19354; -.
DR UCSC; uc007wpp.1; mouse.
DR CTD; 5880; -.
DR MGI; MGI:97846; Rac2.
DR VEuPathDB; HostDB:ENSMUSG00000033220; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000155205; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q05144; -.
DR OMA; LICYSIM; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q05144; -.
DR TreeFam; TF101109; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR BioGRID-ORCS; 19354; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Rac2; mouse.
DR PRO; PR:Q05144; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q05144; protein.
DR Bgee; ENSMUSG00000033220; Expressed in granulocyte and 128 other tissues.
DR ExpressionAtlas; Q05144; baseline and differential.
DR Genevisible; Q05144; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IMP:CACAO.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0045453; P:bone resorption; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0030031; P:cell projection assembly; IDA:MGI.
DR GO; GO:0006935; P:chemotaxis; IDA:MGI.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:MGI.
DR GO; GO:0071593; P:lymphocyte aggregation; ISO:MGI.
DR GO; GO:0070662; P:mast cell proliferation; IMP:MGI.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0070668; P:positive regulation of mast cell proliferation; IMP:MGI.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0010810; P:regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0060753; P:regulation of mast cell chemotaxis; IMP:CACAO.
DR GO; GO:0043304; P:regulation of mast cell degranulation; IMP:CACAO.
DR GO; GO:1902622; P:regulation of neutrophil migration; ISO:MGI.
DR GO; GO:0060263; P:regulation of respiratory burst; ISO:MGI.
DR GO; GO:0042129; P:regulation of T cell proliferation; IMP:CACAO.
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 Acetylation; Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..189
FT /note="Ras-related C3 botulinum toxin substrate 2"
FT /id="PRO_0000042048"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042049"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15153"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 60
FT /note="G -> V (in Ref. 2; BAB25109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21441 MW; 2A1F1266AB9D7705 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP VNLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE VRHHCPSTPI ILVGTKLDLR
DDKDTIEKLK EKKLAPITYP QGLALAKDID SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ
PTRQQKRPCS LL
