ID   GDIR1_CAVPO             Reviewed;         111 AA.
AC   P80237;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Rho GDP-dissociation inhibitor 1;
DE            Short=Rho GDI 1;
DE   AltName: Full=Rho-GDI alpha;
DE   Flags: Fragments;
GN   Name=ARHGDIA;
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   PROTEIN SEQUENCE, AND FUNCTION.
RC   STRAIN=Hartley; TISSUE=Macrophage;
RX   PubMed=8223583; DOI=10.1111/j.1432-1033.1993.tb18264.x;
RA   Pick E., Gorzalczany Y., Engel S.;
RT   "Role of the rac1 p21-GDP-dissociation inhibitor for rho heterodimer in the
RT   activation of the superoxide-forming NADPH oxidase of macrophages.";
RL   Eur. J. Biochem. 217:441-455(1993).
CC   -!- FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP
CC       exchange reaction of the Rho proteins by inhibiting the dissociation of
CC       GDP from them, and the subsequent binding of GTP to them. Retains Rho
CC       proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool,
CC       regulating their stability and protecting them from degradation.
CC       Actively involved in the recycling and distribution of activated Rho
CC       GTPases in the cell, mediates extraction from membranes of both
CC       inactive and activated molecules due its exceptionally high affinity
CC       for prenylated forms. Through the modulation of Rho proteins, may play
CC       a role in cell motility regulation. In glioma cells, inhibits cell
CC       migration and invasion by mediating the signals of SEMA5A and PLXNB3
CC       that lead to inactivation of RAC1. {ECO:0000250|UniProtKB:P52565,
CC       ECO:0000250|UniProtKB:Q99PT1, ECO:0000269|PubMed:8223583}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with FER (By similarity).
CC       Interacts with PLXNB3 (By similarity). Forms a heterodimer with RAC1.
CC       Interacts with RHOA, the affinity is increased by three orders of
CC       magnitude when RHOA is prenylated. Interacts with PSMD10; the
CC       interaction increases ARHGDIA association with RHOA, leading to
CC       ARHGDIA-mediated inactivation of RHOA and ROCK and prolonged AKT
CC       activation. Interacts with KANK2; the interaction is direct and may
CC       regulate the interaction of ARHGDIA with RHOA, RAC1 and CDC42.
CC       Interacts with RHOC. Interacts with CDC42 (By similarity). Interacts
CC       with NGFR (via death domain); NGFR binding decreases the affinity for
CC       RHOA (By similarity). {ECO:0000250|UniProtKB:P52565,
CC       ECO:0000250|UniProtKB:Q99PT1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52565}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the Rho GDI family. {ECO:0000305}.
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   PIR; S38768; S38768.
DR   AlphaFoldDB; P80237; -.
DR   SMR; P80237; -.
DR   InParanoid; P80237; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR   Gene3D; 2.70.50.30; -; 2.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR000406; Rho_GDI.
DR   InterPro; IPR024792; RhoGDI_dom_sf.
DR   PANTHER; PTHR10980; PTHR10980; 2.
DR   Pfam; PF02115; Rho_GDI; 1.
DR   PRINTS; PR00492; RHOGDI.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; GTPase activation;
KW   Isopeptide bond; Reference proteome; Ubl conjugation.
FT   CHAIN           <1..>111
FT                   /note="Rho GDP-dissociation inhibitor 1"
FT                   /id="PRO_0000219012"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52565"
FT   MOD_RES         60
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99PT1"
FT   CROSSLNK        57
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52565"
FT   CROSSLNK        57
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52565"
FT   CROSSLNK        60
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52565"
FT   CROSSLNK        60
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P52565"
FT   UNSURE          98
FT   UNSURE          100
FT   NON_CONS        40..41
FT                   /evidence="ECO:0000305"
FT   NON_CONS        46..47
FT                   /evidence="ECO:0000305"
FT   NON_CONS        86..87
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         111
SQ   SEQUENCE   111 AA;  12496 MW;  0FCE35BEA40FE951 CRC64;
     VAVSADPNEP NVIVTRLTLV CSTAPGPLEL DLTGDLESFK IKISFRYIQH TYRKGVKIDK
     TDYMVGSYGP RAEEYEFLTP MEEAPKGMLA RFTDDDKTDH LSGERNLTIK K