ID   D6R711_HYPMO            Unreviewed;       448 AA.
AC   D6R711;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
OS   Hypophthalmichthys molitrix (Silver carp) (Leuciscus molitrix).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Xenocyprididae; Xenocypridinae; Hypophthalmichthys.
OX   NCBI_TaxID=13095 {ECO:0000313|EMBL:ADF97610.1};
RN   [1] {ECO:0000313|EMBL:ADF97610.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang D.Q., Zhang Y., Luo X.S.;
RT   "Construction of cDNA library from liver and kidney and cloning of
RT   transferrin gene in Hemorrhagic silver carp (Hypophthalmichthys
RT   molitrix).";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most RAB proteins
CC       by inhibiting the dissociation of GDP from them, and the subsequent
CC       binding of GTP. {ECO:0000256|RuleBase:RU363124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363124}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
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DR   EMBL; HM124748; ADF97610.1; -; mRNA.
DR   AlphaFoldDB; D6R711; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR000806; RabGDI.
DR   PANTHER; PTHR11787:SF1; RAB GDP DISSOCIATION INHIBITOR BETA; 1.
DR   PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PRINTS; PR00892; RABGDI.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|RuleBase:RU363124};
KW   GTPase activation {ECO:0000256|RuleBase:RU363124};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
SQ   SEQUENCE   448 AA;  50581 MW;  4E399B324FE54F2D CRC64;
     MNEEYDVIVL GTGLTECILS GIMSVKGKKV LHMDRNSYYG GESASITPLE DLYKRFSLPG
     SPPESMGKGR DWNVDLIPKF LMANGQLVRM LLITQVTRYL DFKVIEGSFV YKKGSIYKVP
     STETEALASS LMGLFEKRRF RKFLVFVANF DENDPKTLEG VDPKKTTMRD VYKKFDLGQD
     VVDFTGHALA LYRTDDYLDQ PCIETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
     LSAIYGGTYM LNKPIEEIVV ENGKVVGVKS EGEIARCKQL ICDPSYVMDR VNKVGQVIRV
     ICIMSHPIKN TSDANSCQII IPQNQVNRKH DIYVCMISYA HNVAAQGKYV AIVSTTVETN
     DPEKEIKPAL DLLEPVEQKF VSISDQYAPT DLGSDSQVFI SRSYDATTHF ETTCDDIKDI
     YKRMTGTEFD FAEMERKKND IFGDCADQ
//