(data stored in ACNUC4266 zone)

HOVERGEN: RAC2_BOVIN

ID   RAC2_BOVIN              Reviewed;         192 AA.
AC   Q9TU25; Q3T0U8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-OCT-2009, entry version 64.
DE   RecName: Full=Ras-related C3 botulinum toxin substrate 2;
DE   AltName: Full=p21-Rac2;
DE   Flags: Precursor;
GN   Name=RAC2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20264070; PubMed=10802295; DOI=10.1016/S0165-2427(00)00176-8;
RA   Davis A.R., Clements M.K., Bunger P.L., Siemsen D.W., Quinn M.T.;
RT   "Cloning of bovine low molecular weight GTPases (Rac1 and Rac2) and
RT   Rho GDP-dissociation inhibitor 2 (D4-GDI).";
RL   Vet. Immunol. Immunopathol. 74:285-301(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Seems to be
CC       involved in the regulation of the NADPH oxidase (By similarity).
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.
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CC   -!- GENE_FAMILY: HBG009351 [ FAMILY / ALN / TREE ]
DR   EMBL; AF175263; AAF00715.1; -; mRNA.
DR   EMBL; BC102255; AAI02256.1; -; mRNA.
DR   IPI; IPI00695702; -.
DR   RefSeq; NP_786986.1; -.
DR   UniGene; Bt.4946; -.
DR   HSSP; P15153; 1DS6.
DR   SMR; Q9TU25; 1-181.
DR   STRING; Q9TU25; -.
DR   PRIDE; Q9TU25; -.
DR   Ensembl; ENSBTAT00000014666; ENSBTAP00000014666; ENSBTAG00000011043; Bos taurus.
DR   GeneID; 327671; -.
DR   KEGG; bta:327671; -.
DR   CTD; 327671; -.
DR   HOVERGEN; Q9TU25; -.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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;
DR   PRODOM; Q9TU25.
DR   SWISS-2DPAGE; Q9TU25.
KW   Acetylation; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation.
FT   DOMAIN        4    179       PRODOM:2005.1:PD000015  2217
FT   CHAIN         1    189       Ras-related C3 botulinum toxin substrate
FT                                2.
FT                                /FTId=PRO_0000042042.
FT   PROPEP      190    192       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000042043.
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).
SQ   SEQUENCE   192 AA;  21424 MW;  2B5D6266AACC3210 CRC64;
     MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP VNLGLWDTAG
     QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE VRHHCPSTPI ILVGTKLDLR
     DDKDTIEKLK EKKLAPITYP QGLALAKEID SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ
     PTRPQKRPCS IL
//

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