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   30-NOV-2010, entry version 97.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90265620; 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,
RT   B and 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles
CC       between an active GTP-bound and inactive GDP-bound state. In
CC       active state binds to a variety of effector proteins to regulate
CC       cellular responses, such as secretory processes, phagocytose of
CC       apoptotic cells and epithelial cell polarization. Augments the
CC       production of reactive oxygen species (ROS) by NADPH oxidase.
CC   -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
CC       factors (GEFs) which promote the exchange of bound GDP for free
CC       GTP, GTPase activating proteins (GAPs) which increase the GTP
CC       hydrolysis activity, and GDP dissociation inhibitors which inhibit
CC       the dissociation of the nucleotide from the GTPase.
CC   -!- SUBUNIT: Interacts with DOCK2, which may activate it (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; Lipid-
CC       anchor (By similarity). Note=Membrane-associated when activated
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   IPI; IPI00137618; -.
DR   PIR; A60194; A60194.
DR   RefSeq; NP_033034.1; NM_009008.3.
DR   UniGene; Mm.1972; -.
DR   ProteinModelPortal; Q05144; -.
DR   SMR; Q05144; 1-181.
DR   IntAct; Q05144; 1.
DR   STRING; Q05144; -.
DR   PhosphoSite; Q05144; -.
DR   PRIDE; Q05144; -.
DR   Ensembl; ENSMUST00000043214; ENSMUSP00000036384; ENSMUSG00000033220.
DR   GeneID; 19354; -.
DR   KEGG; mmu:19354; -.
DR   UCSC; uc007wpp.1; mouse.
DR   CTD; 19354; -.
DR   MGI; MGI:97846; Rac2.
DR   eggNOG; roNOG06989; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q05144; -.
DR   OMA; CPQPTRT; -.
DR   OrthoDB; EOG9X0QC9; -.
DR   PhylomeDB; Q05144; -.
DR   NextBio; 296391; -.
DR   ArrayExpress; Q05144; -.
DR   Bgee; Q05144; -.
DR   CleanEx; MM_RAC2; -.
DR   Genevestigator; Q05144; -.
DR   GermOnline; ENSMUSG00000033220; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR   GO; GO:0030031; P:cell projection assembly; IDA:MGI.
DR   GO; GO:0006935; P:chemotaxis; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003578; GTPase_Rho.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00174; RHO; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation.
FT   CHAIN         1    189       Ras-related C3 botulinum toxin substrate
FT                                2.
FT                                /FTId=PRO_0000042048.
FT   PROPEP      190    192       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000042049.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     115    118       GTP (By similarity).
FT   MOTIF        32     40       Effector region (Potential).
FT   MOD_RES     147    147       N6-acetyllysine (By similarity).
FT   MOD_RES     189    189       Cysteine methyl ester (By similarity).
FT   LIPID       189    189       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT     60     60       G -> V (in Ref. 2; BAB25109).
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
//