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Ras-related C3 botulinum toxin substrate 2 (Protein EN-7) (p21-Rac2)

 RAC2_MOUSE              Reviewed;         192 AA.
Q05144; Q3TBC4; Q9D8X9;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
05-DEC-2018, entry version 160.
RecName: Full=Ras-related C3 botulinum toxin substrate 2;
AltName: Full=Protein EN-7;
AltName: Full=p21-Rac2;
Flags: Precursor;
Name=Rac2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2189110;
Shirsat N.V., Pignolo R.J., Kreider B.L., Rovera G.;
"A member of the ras gene superfamily is expressed specifically in T,
B and myeloid hemopoietic cells.";
Oncogene 5:769-772(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
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=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
IDENTIFICATION IN A COMPLEX WITH SH3RF1; MAP3K7; MAP2K7; MAPK8IP1;
MAPK8 AND MAPK9.
PubMed=27084103; DOI=10.4049/jimmunol.1501728;
Cunningham C.A., Cardwell L.N., Guan Y., Teixeiro E., Daniels M.A.;
"POSH regulates CD4+ T cell differentiation and survival.";
J. Immunol. 196:4003-4013(2016).
-!- FUNCTION: Plasma membrane-associated small GTPase which cycles
between an active GTP-bound and inactive GDP-bound state. In
active state binds to a variety of effector proteins to regulate
cellular responses, such as secretory processes, phagocytose of
apoptotic cells and epithelial cell polarization. Augments the
production of reactive oxygen species (ROS) by NADPH oxidase.
-!- ACTIVITY 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 DOCK2, which may activate it. Interacts
with S100A8 and calprotectin (S100A8/9) (By similarity). Found in
a complex with SH3RF1, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1,
MAPK8/JNK1 and MAPK9/JNK2 (PubMed:27084103).
{ECO:0000250|UniProtKB:P15153, ECO:0000269|PubMed:27084103}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Membrane-
associated when activated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X53247; CAA37337.1; -; mRNA.
EMBL; AK007561; BAB25109.1; -; mRNA.
EMBL; AK144136; BAE25721.1; -; mRNA.
EMBL; AK171321; BAE42390.1; -; mRNA.
EMBL; BC005455; AAH05455.1; -; mRNA.
CCDS; CCDS27619.1; -.
PIR; A60194; A60194.
RefSeq; NP_033034.1; NM_009008.3.
UniGene; Mm.1972; -.
ProteinModelPortal; Q05144; -.
SMR; Q05144; -.
BioGrid; 202557; 4.
DIP; DIP-41834N; -.
IntAct; Q05144; 4.
MINT; Q05144; -.
STRING; 10090.ENSMUSP00000036384; -.
iPTMnet; Q05144; -.
PhosphoSitePlus; Q05144; -.
SwissPalm; Q05144; -.
EPD; Q05144; -.
MaxQB; Q05144; -.
PaxDb; Q05144; -.
PeptideAtlas; Q05144; -.
PRIDE; Q05144; -.
Ensembl; ENSMUST00000043214; ENSMUSP00000036384; ENSMUSG00000033220.
GeneID; 19354; -.
KEGG; mmu:19354; -.
UCSC; uc007wpp.1; mouse.
CTD; 5880; -.
MGI; MGI:97846; Rac2.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00940000155205; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; Q05144; -.
KO; K07860; -.
OMA; LCPQPAK; -.
OrthoDB; EOG091G0KCM; -.
PhylomeDB; Q05144; -.
TreeFam; TF101109; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-194840; Rho GTPase cycle.
Reactome; R-MMU-4086400; PCP/CE pathway.
Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
ChiTaRS; Rac2; mouse.
PRO; PR:Q05144; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000033220; Expressed in 140 organ(s), highest expression level in spleen.
CleanEx; MM_RAC2; -.
Genevisible; Q05144; MM.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030027; C:lamellipodium; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005635; C:nuclear envelope; IDA:MGI.
GO; GO:0005525; F:GTP binding; ISO:MGI.
GO; GO:0003924; F:GTPase activity; IDA:MGI.
GO; GO:0019887; F:protein kinase regulator activity; IMP:CACAO.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
GO; GO:0007015; P:actin filament organization; ISO:MGI.
GO; GO:0045453; P:bone resorption; ISO:MGI.
GO; GO:0030031; P:cell projection assembly; IDA:MGI.
GO; GO:0006935; P:chemotaxis; IDA:MGI.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:MGI.
GO; GO:0071593; P:lymphocyte aggregation; ISO:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:UniProtKB.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
GO; GO:0016601; P:Rac protein signal transduction; IBA:GO_Central.
GO; GO:0010810; P:regulation of cell-substrate adhesion; ISO:MGI.
GO; GO:0060753; P:regulation of mast cell chemotaxis; IMP:CACAO.
GO; GO:0043304; P:regulation of mast cell degranulation; IMP:CACAO.
GO; GO:1902622; P:regulation of neutrophil migration; ISO:MGI.
GO; GO:0060263; P:regulation of respiratory burst; ISO:MGI.
GO; GO:0042129; P:regulation of T cell proliferation; IMP:CACAO.
GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; GTP-binding; Lipoprotein;
Membrane; Methylation; Nucleotide-binding; Prenylation;
Reference proteome.
CHAIN 1 189 Ras-related C3 botulinum toxin substrate
2.
/FTId=PRO_0000042048.
PROPEP 190 192 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000042049.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 115 118 GTP. {ECO:0000250}.
MOTIF 32 40 Effector region. {ECO:0000255}.
MOD_RES 147 147 N6-acetyllysine.
{ECO:0000250|UniProtKB:P15153}.
MOD_RES 189 189 Cysteine methyl ester. {ECO:0000250}.
LIPID 189 189 S-geranylgeranyl cysteine. {ECO:0000250}.
CONFLICT 60 60 G -> V (in Ref. 2; BAB25109).
{ECO:0000305}.
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


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