ID U6IW87_ECHGR Unreviewed; 447 AA.
AC U6IW87;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN Name=EGR_07503 {ECO:0000313|WBParaSite:EgrG_000767200};
GN ORFNames=EGR_07503 {ECO:0000313|EMBL:EUB57627.1}, EgrG_000767200
GN {ECO:0000313|EMBL:CDS15277.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB57627.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB57627.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
RN [2] {ECO:0000313|EMBL:CDS15277.1, ECO:0000313|Proteomes:UP000492820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [3] {ECO:0000313|EMBL:CDS15277.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|WBParaSite:EgrG_000767200}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (OCT-2020) 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 EMBL; LK028576; CDS15277.1; -; Genomic_DNA.
DR EMBL; APAU02000079; EUB57627.1; -; Genomic_DNA.
DR AlphaFoldDB; U6IW87; -.
DR STRING; 6210.U6IW87; -.
DR EnsemblMetazoa; XM_024496752.1; XP_024348823.1; GeneID_36343218.
DR WBParaSite; EgrG_000767200; EgrG_000767200; EgrG_000767200.
DR OMA; FETKAKM; -.
DR OrthoDB; 8704at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR Proteomes; UP000492820; 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:UP000019149}.
SQ SEQUENCE 447 AA; 50210 MW; F804EE590AF7F021 CRC64;
MDEDYDIVIL GTGLKECILS GLMSVAGKKV LHMDRNSYYG GESTSITPLD ELFKRFNKTC
PGEQVYKRLR DWNVDLIPKF LMADGKLVKL LLHTGVTRYL EFKSVGGSYV YKGTVDSGRI
CKVPSNEREA LSSDLMGMFE KRRFRKLLIF TDGVDENKPD TWGELPLNKC TMQAVFDKFG
VDNNTQDFVG HAICLYRNDD YKRNLCALDA IRRMKLYSDS LSRYGSSPYL YPLYGLGELP
QGFARLSAVY GGTYMLNKPF EGFVMENGKV VGVKSEGEVA KCSKVICDPS YAPDLVRQVG
KVVRAICILD HPIDGTNGST SCQIIIPQNQ VGRKHDIYIS CVSHDHNVAA KPFFIALVAT
TVETQQPERE LVPGIRLLGH MMDCFVSVSN LYEPINDGKA NNIFVSSSYD ATTHFETTCD
DVLDIYERIM SEKFDFSKVK ANLDDEQ
//
