GDIR1_MACFA
ID GDIR1_MACFA Reviewed; 204 AA.
AC Q4R4J0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Rho GDP-dissociation inhibitor 1;
DE Short=Rho GDI 1;
DE AltName: Full=Rho-GDI alpha;
GN Name=ARHGDIA; ORFNames=QtrA-11619;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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 -!- 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 EMBL; AB169904; BAE01985.1; -; mRNA.
DR RefSeq; NP_001270796.1; NM_001283867.1.
DR AlphaFoldDB; Q4R4J0; -.
DR SMR; Q4R4J0; -.
DR STRING; 9541.XP_005585322.1; -.
DR PRIDE; Q4R4J0; -.
DR GeneID; 101866857; -.
DR CTD; 396; -.
DR VEuPathDB; HostDB:ENSMFAG00000041442; -.
DR eggNOG; KOG3205; Eukaryota.
DR OMA; DDDKRCH; -.
DR OrthoDB; 1265661at2759; -.
DR Proteomes; UP000233100; Chromosome 16.
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; -; 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; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CHAIN 2..204
FT /note="Rho GDP-dissociation inhibitor 1"
FT /id="PRO_0000318591"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PT1"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99PT1"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 141
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 141
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99PT1"
FT MOD_RES 178
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
SQ SEQUENCE 204 AA; 23207 MW; 59CB6F42E3B3BCCA CRC64;
MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK YKEALLGRVA
VSADPNVPNV VVTGLTLVCS SAPGPLELDL TGDLESFKKQ SFVLKEGVEY RIKISFRVNR
EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG PRAEEYEFLT PVEEAPKGML ARGSYSIKSR
FTDDDKTDHL SWEWNLTIKK DWKD
