LMP012522 UniProt Annotations
Gene Name Rab geranylgeranyltransferase, beta subunit
Protein Entry PGTB2_RAT
UniProt ID Q08603
Species Rat
Comment type Description
Catalytic Activity Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. {ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
Cofactor Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10745007, ECO:0000269|PubMed:12620235, ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10745007, ECO:0000269|PubMed:12620235, ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166};
Enzyme Regulation The enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM.
Function Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. {ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
Similarity Belongs to the protein prenyltransferase subunit beta family
Similarity Contains 6 PFTB repeats
Subunit Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding. The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp. Interaction of RABGGTB with prenylated PTP4A2 precludes its association with RABGGTA and inhibits enzyme activity. {ECO:0000269|PubMed:10745007, ECO:0000269|PubMed:11675392, ECO:0000269|PubMed:12620235, ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
Tissue Specificity Most abundant in the heart, brain, spleen and liver. Less in the lung, muscle, kidney and testis; in these tissues, more abundant than the subunit alpha.
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