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 03-AUG-2022, entry version 147.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 Rho
RT 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 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 (By similarity). {ECO:0000250}.
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). Found in a complex with SH3RF1,
CC MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2.
CC Interacts with PAK1 (By similarity). {ECO:0000250|UniProtKB:P15153,
CC ECO:0000250|UniProtKB:Q05144}.
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; AF175263; AAF00715.1; -; mRNA.
DR EMBL; BC102255; AAI02256.1; -; mRNA.
DR RefSeq; NP_786986.1; NM_175792.2.
DR AlphaFoldDB; Q9TU25; -.
DR SMR; Q9TU25; -.
DR STRING; 9913.ENSBTAP00000014666; -.
DR PaxDb; Q9TU25; -.
DR PeptideAtlas; Q9TU25; -.
DR PRIDE; Q9TU25; -.
DR Ensembl; ENSBTAT00000014666; ENSBTAP00000014666; ENSBTAG00000011043.
DR GeneID; 327671; -.
DR KEGG; bta:327671; -.
DR CTD; 5880; -.
DR VEuPathDB; HostDB:ENSBTAG00000011043; -.
DR VGNC; VGNC:49061; RAC2.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000155205; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q9TU25; -.
DR OMA; LICYSIM; -.
DR OrthoDB; 1091615at2759; -.
DR TreeFam; TF101109; -.
DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-BTA-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-BTA-9013404; RAC2 GTPase cycle.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000011043; Expressed in blood and 103 other tissues.
DR ExpressionAtlas; Q9TU25; baseline and differential.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0071593; P:lymphocyte aggregation; IEA:Ensembl.
DR GO; GO:0070662; P:mast cell proliferation; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0070668; P:positive regulation of mast cell proliferation; IEA:Ensembl.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0060753; P:regulation of mast cell chemotaxis; IEA:Ensembl.
DR GO; GO:0043304; P:regulation of mast cell degranulation; IEA:Ensembl.
DR GO; GO:1902622; P:regulation of neutrophil migration; IBA:GO_Central.
DR GO; GO:0060263; P:regulation of respiratory burst; IEA:Ensembl.
DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
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 2: Evidence at transcript 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_0000042042"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042043"
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"
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
