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Database: UniProt
Entry: A0A3Q3BNB2_KRYMA
LinkDB: A0A3Q3BNB2_KRYMA
Original site: A0A3Q3BNB2_KRYMA 
ID   A0A3Q3BNB2_KRYMA        Unreviewed;       157 AA.
AC   A0A3Q3BNB2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-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   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000027209.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000027209.1}
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}.
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DR   AlphaFoldDB; A0A3Q3BNB2; -.
DR   STRING; 37003.ENSKMAP00000027209; -.
DR   Ensembl; ENSKMAT00000027551.1; ENSKMAP00000027209.1; ENSKMAG00000020167.1.
DR   GeneTree; ENSGT00390000006233; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:UP000264800}.
SQ   SEQUENCE   157 AA;  18280 MW;  F20244E39FE8AC42 CRC64;
     STRLRTKTQT GDVLETLWGH FGDRNKNRTL RIGPAEQTII IRCLGDLEAF KKQAFVLKEG
     VEYKIKINFK VNTEIVSGLK YVQQTFRKGM KIDKSDYMVG SYGPRPTEYD FLTTMEEAPK
     GLLARGNYVI KSKFTDDDKH DHLSWEWNLN IKKDWND
//
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