ID   GDIR2_BOVIN             Reviewed;         200 AA.
AC   Q9TU03; Q3ZCK4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Rho GDP-dissociation inhibitor 2;
DE            Short=Rho GDI 2;
DE   AltName: Full=D4-GDP-dissociation inhibitor;
DE            Short=D4-GDI;
DE   AltName: Full=Ly-GDI;
DE   AltName: Full=Rho-GDI beta;
GN   Name=ARHGDIB; Synonyms=GDID4;
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], AND SUBCELLULAR LOCATION.
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: Regulates the GDP/GTP exchange reaction of the Rho proteins
CC       by inhibiting the dissociation of GDP from them, and the subsequent
CC       binding of GTP to them. Regulates reorganization of the actin
CC       cytoskeleton mediated by Rho family members.
CC       {ECO:0000250|UniProtKB:P52566}.
CC   -!- SUBUNIT: Interacts with RHOA. Interacts with RAC1. Interacts with RAC2.
CC       Interacts with CDC42. {ECO:0000250|UniProtKB:P52566}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10802295}.
CC   -!- SIMILARITY: Belongs to the Rho GDI family. {ECO:0000305}.
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DR   EMBL; AF182001; AAF00938.1; -; mRNA.
DR   EMBL; BC102109; AAI02110.1; -; mRNA.
DR   RefSeq; NP_786991.1; NM_175797.2.
DR   AlphaFoldDB; Q9TU03; -.
DR   SMR; Q9TU03; -.
DR   STRING; 9913.ENSBTAP00000007933; -.
DR   PaxDb; Q9TU03; -.
DR   PeptideAtlas; Q9TU03; -.
DR   PRIDE; Q9TU03; -.
DR   GeneID; 327676; -.
DR   KEGG; bta:327676; -.
DR   CTD; 397; -.
DR   eggNOG; KOG3205; Eukaryota.
DR   HOGENOM; CLU_076228_1_1_1; -.
DR   InParanoid; Q9TU03; -.
DR   OrthoDB; 1265661at2759; -.
DR   TreeFam; TF105387; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR   Gene3D; 2.70.50.30; -; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR000406; Rho_GDI.
DR   InterPro; IPR024792; RhoGDI_dom_sf.
DR   PANTHER; PTHR10980; PTHR10980; 1.
DR   Pfam; PF02115; Rho_GDI; 1.
DR   PRINTS; PR00492; RHOGDI.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; GTPase activation; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   CHAIN           2..200
FT                   /note="Rho GDP-dissociation inhibitor 2"
FT                   /id="PRO_0000219015"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         20
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         23
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         39
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         46
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         101
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         123
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
FT   MOD_RES         174
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52566"
SQ   SEQUENCE   200 AA;  22794 MW;  EE8F1E38993AFDE5 CRC64;
     MTEKAPEPHV EEDDDELDGK LNYKPPPQKS LKELQEMDKD DESLTKYKKT LLGDGPVVAD
     PTAPNVTVTR LTLVCESAPG PITMDLTGDL EALKKETFVL KEGVEYRVKI NFKVNKDIVS
     GLKYVQHTYR TGVKVDKATF MVGSYGPRPE EYEFLTPIEE APKGMLARGT YHNKSFFTDD
     DKHDHLTWEW NLSIKKDWTE