LIPID MAPS® Gene/Proteome Database (LMPD)

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LMPD Record

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LMP012522

UniProt Annotations

Entry Information

Gene Name	Rab geranylgeranyltransferase, beta subunit
Protein Entry	PGTB2_RAT
UniProt ID	Q08603
Species	Rat

Comments

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.