LIPID MAPS® Gene/Proteome Database (LMPD)

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LMPD Record

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LMP012667

UniProt Annotations

Entry Information
Gene NameRab geranylgeranyltransferase, alpha subunit
Protein EntryPGTA_RAT
UniProt IDQ08602
SpeciesRat
Comments
Comment typeDescription
Catalytic ActivityGeranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. {ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:21520375, ECO:0000269|PubMed:22963166}.
Enzyme RegulationThe enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM.
FunctionCatalyzes 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:21520375, ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
SimilarityBelongs to the protein prenyltransferase subunit alpha family
SimilarityContains 5 LRR (leucine-rich) repeats
SimilarityContains 6 PFTA repeats. {ECO:0000255|PROSITE- ProRule:PRU00488}.
SubunitHeterotrimer 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. {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:21520375, ECO:0000269|PubMed:22963166, ECO:0000269|PubMed:8505342}.
Tissue SpecificityMost abundant in the heart, brain, spleen and liver. Less in the lung, muscle, kidney and testis; in these tissues less abundant than the beta subunit.