GDIR1_BOVIN
ID GDIR1_BOVIN Reviewed; 204 AA.
AC P19803; Q3ZBA9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Rho GDP-dissociation inhibitor 1;
DE Short=Rho GDI 1;
DE AltName: Full=Rho-GDI alpha;
GN Name=ARHGDIA;
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], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=2120668;
RA Fukumoto Y., Kaibuchi K., Hori Y., Fujioka H., Araki S., Ueda T.,
RA Kikuchi A., Takai Y.;
RT "Molecular cloning and characterization of a novel type of regulatory
RT protein (GDI) for the rho proteins, ras p21-like small GTP-binding
RT proteins.";
RL Oncogene 5:1321-1328(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE BY NMR OF 60-204, AND FUNCTION.
RX PubMed=9194563; DOI=10.1038/42961;
RA Gosser Y.Q., Nomanbhoy T.K., Aghazadeh B., Manor D., Combs C.,
RA Cerione R.A., Rosen M.K.;
RT "C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-
RT terminal inhibitory peptide to GTPases.";
RL Nature 387:814-819(1997).
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:2120668,
CC ECO:0000269|PubMed:9194563}.
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 -!- TISSUE SPECIFICITY: Brain, lung, thymus, spleen, small intestine, and
CC kidney, and weakly in heart and liver.
CC -!- SIMILARITY: Belongs to the Rho GDI family. {ECO:0000305}.
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DR EMBL; X52689; CAA36916.1; -; mRNA.
DR EMBL; BC103465; AAI03466.1; -; mRNA.
DR PIR; S12121; S12121.
DR RefSeq; NP_788823.1; NM_176650.3.
DR RefSeq; XP_005221068.2; XM_005221011.3.
DR PDB; 1AJW; NMR; -; A=60-204.
DR PDB; 1DOA; X-ray; 2.60 A; B=1-204.
DR PDB; 1GDF; NMR; -; A=60-204.
DR PDB; 5FR1; X-ray; 2.75 A; B=1-204.
DR PDB; 5FR2; X-ray; 3.35 A; B=1-204.
DR PDBsum; 1AJW; -.
DR PDBsum; 1DOA; -.
DR PDBsum; 1GDF; -.
DR PDBsum; 5FR1; -.
DR PDBsum; 5FR2; -.
DR AlphaFoldDB; P19803; -.
DR SMR; P19803; -.
DR MINT; P19803; -.
DR STRING; 9913.ENSBTAP00000040280; -.
DR PaxDb; P19803; -.
DR PeptideAtlas; P19803; -.
DR PRIDE; P19803; -.
DR GeneID; 338054; -.
DR KEGG; bta:338054; -.
DR CTD; 396; -.
DR eggNOG; KOG3205; Eukaryota.
DR HOGENOM; CLU_076228_1_1_1; -.
DR InParanoid; P19803; -.
DR OrthoDB; 1265661at2759; -.
DR TreeFam; TF105387; -.
DR EvolutionaryTrace; P19803; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0001772; C:immunological synapse; ISS:AgBase.
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:AgBase.
DR GO; GO:0007266; P:Rho protein signal transduction; ISS:AgBase.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.70.50.30; -; 1.
DR IDEAL; IID50041; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW GTPase activation; Isopeptide bond; Phosphoprotein; Reference proteome;
KW 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_0000219011"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..83
FT /note="Hydrophobic"
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 101
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 115
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
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"
FT TURN 10..14
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1DOA"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:1DOA"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:1DOA"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1AJW"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1DOA"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 123..134
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 137..149
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1GDF"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5FR1"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:1DOA"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1AJW"
FT STRAND 190..201
FT /evidence="ECO:0007829|PDB:1DOA"
SQ SEQUENCE 204 AA; 23421 MW; 49CE7DEB05D271CA CRC64;
MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK YKEALLGRVA
VSADPNVPNV VVTRLTLVCS TAPGPLELDL TGDLESFKKQ SFVLKEGVEY RIKISFRVNR
EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG PRAEEYEFLT PMEEAPKGML ARGSYNIKSR
FTDDDRTDHL SWEWNLTIKK EWKD
