ID A0A0N5C903_STREA Unreviewed; 444 AA.
AC A0A0N5C903;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001438600.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001438600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
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DR AlphaFoldDB; A0A0N5C903; -.
DR STRING; 174720.A0A0N5C903; -.
DR WBParaSite; SPAL_0001438600.1; SPAL_0001438600.1; SPAL_0001438600.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005737; C:cytoplasm; 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:SF8; RAB GDP DISSOCIATION INHIBITOR; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU363124};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468,
KW ECO:0000256|RuleBase:RU363124}.
SQ SEQUENCE 444 AA; 50135 MW; C57A13AC28655F84 CRC64;
MNDEYDAIVL GTGLKECILS GMLSVSGKKV LHIDRNNYYG GESASLSPLN QLYEIFHGKD
AQAPEFMGRG RDWNVDLIPK FLMANGQLVK LLIHTGVTRY LEFKSIEGSY VYKGGKVYKV
PADEVEALST SLMGMFEKRR FKKFLVWVQG FDINDQDTYE GMDPTKDTMQ QVYDKFGLDE
NTADFTGHAL ALYRDDAYKN ELFVKTVQKI RLYSDSLARY GKSPYLYPLY GLGELPQGFA
RLSAIYGGTY MLDKQVDEIV IENNKVVGVK SGNEIAKCKQ LYCDPSYVLD RCKQNSQVVR
AICILDHPIP DTKEAASCQI IIPQKQVNRG SDIYISCVSN ANQTAPKGWY IAMVSTTVET
GNPELEIQPG LQLLGQIKEK FIRVYDIYEP VDMGHESQIF ISRGYDATTH FETVCTDVLD
IFARGTGEQF DFSKITHLTM EEQD
//