ID   RAC2_CAVPO              Reviewed;         192 AA.
AC   O88931;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Ras-related C3 botulinum toxin substrate 2;
DE   AltName: Full=p21-Rac2;
DE   Flags: Precursor;
GN   Name=RAC2;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Dunkin-Hartley;
RX   PubMed=10540223; DOI=10.1046/j.1365-2567.1999.00873.x;
RA   Lacy P., Mahmudi-Azer S., Bablitz B., Gilchrist M., Fitzharris P.,
RA   Cheng D., Man S.F.P., Bokoch G.M., Moqbel R.;
RT   "Expression and translocation of Rac2 in eosinophils during superoxide
RT   generation.";
RL   Immunology 98:244-252(1999).
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; AF085341; AAC35359.1; -; mRNA.
DR   AlphaFoldDB; O88931; -.
DR   SMR; O88931; -.
DR   STRING; 10141.ENSCPOP00000014775; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   InParanoid; O88931; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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_0000042044"
FT   PROPEP          190..192
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042045"
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;  21408 MW;  2AE790A32A1BD986 CRC64;
     MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP VNLGLWDTAG
     QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVHANWYPK VRHHCPSTPI ILLGTKLDLR
     DDKETIEKLK EKKLAPITYP QGLALAKEID SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ
     PTRPQKRACS LL