ID   A0A1S3PX71_SALSA        Unreviewed;       237 AA.
AC   A0A1S3PX71;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Rho GDP-dissociation inhibitor 1 {ECO:0000256|ARBA:ARBA00040620};
DE   AltName: Full=Rho-GDI alpha {ECO:0000256|ARBA:ARBA00041559};
GN   Name=LOC106588090 {ECO:0000313|RefSeq:XP_014032236.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014032236.1};
RN   [1] {ECO:0000313|RefSeq:XP_014032236.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014032236.1};
RG   RefSeq;
RL   Submitted (NOV-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}.
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DR   RefSeq; XP_014032236.1; XM_014176761.1.
DR   AlphaFoldDB; A0A1S3PX71; -.
DR   STRING; 8030.ENSSSAP00000045149; -.
DR   PaxDb; 8030-ENSSSAP00000045149; -.
DR   Ensembl; ENSSSAT00000071957; ENSSSAP00000045149; ENSSSAG00000046941.
DR   GeneID; 106588090; -.
DR   KEGG; sasa:106588090; -.
DR   OMA; HPDHHDE; -.
DR   OrthoDB; 21211at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa02.
DR   Bgee; ENSSSAG00000046941; Expressed in spleen and 16 other cell types or tissues.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
SQ   SEQUENCE   237 AA;  26795 MW;  3ACBDAF9E4E68FA3 CRC64;
     MGRRRSLFAI LAQGRATEAL ILQAPGRKQQ ENDMAEDDLT PEQLAAIAAE NDVGETVNYK
     PPAQKTLQEI QELDQDDESL RKYKEVLLGA GAAAVADPSV PNVQVTRLTL MCETAPNPLT
     LDLQGDLEAF KKQSFILKEG VEYRIKISFK VNKEIVSGLK YVQQTHRKGV RIDKSDYMVG
     SYGPRPNEYD FLTPLEEAPK GMLARGTYNI KSKFTDDDKH DHLSWEWNLN IKKDWKD
//