ID A0A0V1LMP4_9BILA Unreviewed; 482 AA.
AC A0A0V1LMP4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN Name=Gdi1 {ECO:0000313|EMBL:KRZ60765.1};
GN ORFNames=T02_6024 {ECO:0000313|EMBL:KRZ60765.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60765.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ60765.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60765.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ60765.1}.
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DR EMBL; JYDW01000025; KRZ60765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LMP4; -.
DR STRING; 6335.A0A0V1LMP4; -.
DR Proteomes; UP000054721; 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:UP000054721}.
SQ SEQUENCE 482 AA; 54480 MW; 837309EF149DD261 CRC64;
MLLRIKHNQL DQSKHLRYHL DIDLTYKLQV ALVLYLAAMD EIYDCVILGT GLTECIVSGM
LSVSGKKILH MDRNNYYGGE SASITPLEDL FDKFMPGTKP LESMGRGRDW NVDLIPKFLM
ANGSELVKLL LSTGVTRYLE FKSIEGSFVY KGGKVYKVPA DEAEALTTSL MGIFEKRRFK
KFLVWAQNFD FDNKATWEGL DPYTNTMNDV YRKFDLDENT ADFTGHALAL YINDKYKNEP
FGETVKRVKL YSASLERYGK SPYLYPLYGL GELPQGFARL SAIYGGTYML DTPVDEIVME
NGCVIGVRCG NQTVRCRQVY CDPSYAPNFV RHVGKVIRAI CLLNHPIPNT NDSKSCQIII
PQRQVGRQHD IYISMVSYTN MVAAKDWYVA IVSTTVETNS PESELLPGLQ LLGSITQKFV
SISDLMEPIN DGRSSQVFIS KSYDATSHFK TTCDDVIDIF QRGTGEPFDF SKISHLTLED
TQ
//
