ID A0A0C2DC81_9BILA Unreviewed; 444 AA.
AC A0A0C2DC81;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN ORFNames=ANCDUO_02216 {ECO:0000313|EMBL:KIH67448.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH67448.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH67448.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH67448.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) 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 -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
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DR EMBL; KN726693; KIH67448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2DC81; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
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|RuleBase:RU363124};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047}.
SQ SEQUENCE 444 AA; 49945 MW; 3C3FC02CEDD4E2CF CRC64;
MDEEYDAIVL GTGLKECIIS GMLSVSGKKV LHIDRNNYYG GESASLTPLE QLYEKFMGPN
AKPPPEMGRG RDWNVDLIPK FLMANGSLVK LLIHTGVTRY LEFKSVEGSY VYKGGKVYKV
PADEMEALAT SLMGMFEKRR FKKFLCWVQA FDRVNKDTWQ GLDPDTHTMQ QVYEKFGLDD
NTADFTGHAL ALYRDDDYKQ QPFGPTVEKI RLYSDSLARY GKSPYLYPLY GLGELPQGFA
RLSAIYGGTY MLDKPVDSLI VENGKVVGVK CGEETVRGKQ VYCDPSYAMD RVKKVGQVVR
AICLLNHPIP GTNDAQSCQI IIPQKQVGRH FDIYISCCSN TNMVTPKGWF VAMVSTTVET
NNPEAEILPG LQLLGTITEK FISVSDVYEP TDLGHESQIF ISRSYDPTTH FETTCKDVLD
IFQRGTTQEF DFSKITHLSL EDNE
//