ID   A0A183TE44_SCHSO        Unreviewed;       306 AA.
AC   A0A183TE44;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001530001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0001530001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) 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; A0A183TE44; -.
DR   WBParaSite; SSLN_0001530001-mRNA-1; SSLN_0001530001-mRNA-1; SSLN_0001530001.
DR   Proteomes; UP000050788; 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   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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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}.
SQ   SEQUENCE   306 AA;  34011 MW;  3B14EEA8A64F4CAB CRC64;
     LSMDTLTISS KGTTTTTLAM RSFYLGPIDL FIPGASYHAD FIGHAICLHQ SEDYKTKCSA
     LDCIKRMQLY SNSLMRYGKS PYLYPLYGLG ELPQGFARLS AVYGGTYMLN KPFDGFVMEN
     GKVVGVKSEG EVARCKQVIC DPSYAPDLVR KVGRVVRAIC ILDHPIPNTA DALSCQIILP
     QNQIGRKHGI CAFRSHIYIS CVSFDHKVAA ERFFIAMVAT IVETDNPPRE LAAGIRLLGP
     MKECFVKDSD LYEPIGSGTD NQIFISSSYD ATTHFESTCD DVLNIYERLM GEKFDFSKVK
     ARLDDE
//