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0GDIB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGDI2
DescriptionRab gdp dissociation inhibitor beta (rab gdi beta) (gdi-2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0009986 cell surface (IEP)
0005093 Rab GDP-dissociation inhibitor activity (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Rab proteins constitute a family of small GTPases that serve a regulatoryrole in vesicular membrane traffic . C-terminal geranylgeranylation iscrucial for their membrane association and function. This post-translationalmodification is catalysed by Rab geranylgeranyl transferase (Rab-GGTase). multi-subunit enzyme that contains a catalytic heterodimer and an accessorycomponent.ermed Rab escort protein (REP)-1 . REP-1 presents newly-synthesised Rab proteins to the catalytic component.nd forms a stablecomplex with the prenylated proteins following the transfer reaction. The mechanism of REP-1-mediated membrane association of Rab5 is similarto that mediated by Rab GDP dissociation inhibitor (GDI). REP-1 and Rab GDI also share other functional properties.ncluding the ability to inhibit therelease of GDP and to remove Rab proteins from membranes.The crystal structure of the bovine alpha-isoform of Rab GDI has beendetermined to a resolution of 1.81A . The protein is composed of twomain structural units: a large complex multi-sheet domain I.nd a smalleralpha-helical domain II.The structural organisation of domain I is closely related to FAD-containingmonooxygenases and oxidases . Conserved regions common to GDI and thechoroideraemia gene product.hich delivers Rab to catalytic subunits ofRab geranylgeranyltransferase II.re clustered on one face of the domain. The two most conserved regions form a compact structure at the apex ofthe molecule; site-directed mutagenesis has shown these regions to play acritical role in the binding of Rab proteins .
  IPR002005:Rab GTPase activator
InterPro domains unassigned to SynO:
Rab proteins. family of small Ras-related GTP-binding proteins.re involved in regulation of intracellular vesicle trafficking . Rab GDP dissociation inhibitor (GDI) forms a soluble complex with Rab proteins.hereby preventing exchange of GDP for GTP. Rab GDI exists in several isoforms.nd belongs to the TCD/MRS6 family of GDP dissociation inhibitors. The crystal structure of the bovine alpha-isoform of Rab GDI has beendetermined to a resolution of 1.81A . The protein is composed of twomain structural units: a large complex multi-sheet domain I.nd a smalleralpha-helical domain II.The structural organisation of domain I is closely related to FAD-containingmonooxygenases and oxidases . Conserved regions common to GDI and thechoroideraemia gene product.hich delivers Rab to catalytic subunits ofRab geranylgeranyltransferase II.re clustered on one face of the domain. The two most conserved regions form a compact structure at the apex ofthe molecule; site-directed mutagenesis has shown these regions to play acritical role in the binding of Rab proteins .
  IPR000806:Rab GDI protein
IPR002005:GDI 
Evalue:-1e+125 
Location:1-438
SequencesProtein: GDIB_HUMAN (445 aa)
mRNA: NM_001494
Local Annotation
Synapse Ontology
Fusion of intracellular membrane-bound vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft.
sdb:0049 synaptic vesicle fusion  (Evidence:domains)
Penetrating at least one phospholipid bilayer of a synaptic vesicle membrane. May also refer to the state of being buried in the bilayer with no exposure outside the bilayer.
sdb:0078 integral to synaptic vesicle membrane proteins  (Evidence:domains)
proteins that help to traffick the vesicle, such as synaptobrevin/Vamp, synaptotagmin, Rab3-rabphilin complex.
sdb:0097 vesicle trafficking protein  (Evidence:domains)
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:domains)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 310 residues, 5847192-5848121Exon2: 20 residues, 5848209-5848264Exon3: 50 residues, 5848462-5848607Exon4: 59 residues, 5850181-5850353Exon5: 35 residues, 5855810-5855910Exon6: 46 residues, 5867110-5867242Exon7: 68 residues, 5867820-5868019Exon8: 47 residues, 5876853-5876988Exon9: 35 residues, 5878731-5878831Exon10: 38 residues, 5882566-5882674Exon11: 67 residues, 5895182-5895379Exon12: 2 residues, -Jump to GDIB_HUMAN  
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