ID A0A3B4WLS8_SERLL Unreviewed; 147 AA.
AC A0A3B4WLS8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Rho GDP-dissociation inhibitor 1 {ECO:0000256|ARBA:ARBA00040620};
DE AltName: Full=Rho-GDI alpha {ECO:0000256|ARBA:ARBA00041559};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000002388.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000002388.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037489}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Rho GDI family.
CC {ECO:0000256|ARBA:ARBA00009758}.
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 AlphaFoldDB; A0A3B4WLS8; -.
DR STRING; 1841481.ENSSLDP00000002388; -.
DR Ensembl; ENSSLDT00000002488.1; ENSSLDP00000002388.1; ENSSLDG00000001848.1.
DR GeneTree; ENSGT00390000006233; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR Gene3D; 2.70.50.30; Coagulation Factor XIII, subunit A, domain 1; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000406; Rho_GDI.
DR InterPro; IPR024792; RhoGDI_dom_sf.
DR PANTHER; PTHR10980; RHO GDP-DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR10980:SF9; RHO GDP-DISSOCIATION INHIBITOR 1; 1.
DR Pfam; PF02115; Rho_GDI; 1.
DR PRINTS; PR00492; RHOGDI.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499}.
SQ SEQUENCE 147 AA; 16551 MW; 7C83DFE071B48E86 CRC64;
DDESLRKYKE ALLGSTAVVA DPTAPNVQVT RMTLVCEAAP QPLVLDLQGD LEGFRKNPFV
LKEGVEYRIK INFKVRESGL CLCLFSQTLY LSWETAQQDD ACCFLQVNKE IVSGLKYIQQ
SFRKGVKGKT AKIISFNLCN SLGRFYM
//