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Q08602 (PGTA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Geranylgeranyl transferase type-2 subunit alpha

EC=2.5.1.60
Alternative name(s):
Geranylgeranyl transferase type II subunit alpha
Rab geranyl-geranyltransferase subunit alpha
Short name=Rab GG transferase alpha
Short name=Rab GGTase alpha
Rab geranylgeranyltransferase subunit alpha
Gene names
Name:Rabggta
Synonyms:Ggta
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Catalytic activity

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. Ref.7 Ref.8 Ref.9 Ref.10

Enzyme regulation

The enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM.

Subunit structure

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. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Tissue specificity

Most 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.

Sequence similarities

Belongs to the protein prenyltransferase subunit alpha family.

Contains 5 LRR (leucine-rich) repeats.

Contains 6 PFTA repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Geranylgeranyl transferase type-2 subunit alpha
PRO_0000119759

Regions

Repeat44 – 7835PFTA 1
Repeat88 – 12235PFTA 2
Repeat124 – 15835PFTA 3
Repeat159 – 19335PFTA 4
Repeat207 – 24135PFTA 5
Repeat363 – 39735PFTA 6
Repeat442 – 46322LRR 1
Repeat464 – 48623LRR 2
Repeat487 – 50822LRR 3
Repeat509 – 53022LRR 4
Repeat534 – 55522LRR 5

Experimental info

Sequence conflict1691S → D AA sequence Ref.1
Sequence conflict2271S → Q AA sequence Ref.1

Secondary structure

..................................................................................... 567
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08602 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 1F9D235F973EABD5

FASTA56764,904
        10         20         30         40         50         60 
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE LTSQILGANP 

        70         80         90        100        110        120 
DFATLWNCRR EVLQHLETEK SPEESAALVK AELGFLESCL RVNPKSYGTW HHRCWLLSRL 

       130        140        150        160        170        180 
PEPNWARELE LCARFLEADE RNFHCWDYRR FVAAQAAVAP AEELAFTDSL ITRNFSNYSS 

       190        200        210        220        230        240 
WHYRSCLLPQ LHPQPDSGPQ GRLPENVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAE 

       250        260        270        280        290        300 
PHDVLCCVHV SREEACLSVC FSRPLTVGSR MGTLLLMVDE APLSVEWRTP DGRNRPSHVW 

       310        320        330        340        350        360 
LCDLPAASLN DQLPQHTFRV IWTGSDSQKE CVLLKDRPEC WCRDSATDEQ LFRCELSVEK 

       370        380        390        400        410        420 
STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY EKETLQYFST LKAVDPMRAA 

       430        440        450        460        470        480 
YLDDLRSKFL LENSVLKMEY ADVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRALPP 

       490        500        510        520        530        540 
ALAALRCLEV LQASDNALEN VDGVANLPRL QELLLCNNRL QQSAAIQPLV SCPRLVLLNL 

       550        560 
QGNSLCQEEG IQERLAEMLP SVSSILT 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of the alpha and beta subunits of rat Rab geranylgeranyl transferase."
Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S.
J. Biol. Chem. 268:12221-12229(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[3]"Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase with REP-1."
Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K.
J. Biol. Chem. 276:48637-48643(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[4]"Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution."
Zhang H., Seabra M.C., Deisenhofer J.
Structure 8:241-251(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RABGGTB, SUBUNIT.
[5]"Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase."
Pylypenko O., Rak A., Reents R., Niculae A., Sidorovitch V., Cioaca M.D., Bessolitsyna E., Thomae N.H., Waldmann H., Schlichting I., Goody R.S., Alexandrov K.
Mol. Cell 11:483-494(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH GERANYGERANYL PHOSHATE ANALOG; RABGGTB AND CHM/REP1, SUBUNIT.
[6]"Development of selective RabGGTase inhibitors and crystal structure of a RabGGTase-inhibitor complex."
Guo Z., Wu Y.W., Tan K.T., Bon R.S., Guiu-Rozas E., Delon C., Nguyen T.U., Wetzel S., Arndt S., Goody R.S., Blankenfeldt W., Alexandrov K., Waldmann H.
Angew. Chem. Int. Ed. Engl. 47:3747-3750(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-441 IN COMPLEX WITH INHIBITOR, FUNCTION, SUBUNIT.
[7]"Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation."
Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S., Lupilova N., Waldmann H., Brunsveld L., Goody R.S., Alexandrov K., Blankenfeldt W.
EMBO J. 27:2444-2456(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[8]"Design, synthesis, and characterization of peptide-based rab geranylgeranyl transferase inhibitors."
Tan K.T., Guiu-Rozas E., Bon R.S., Guo Z., Delon C., Wetzel S., Arndt S., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W., Blankenfeldt W.
J. Med. Chem. 52:8025-8037(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[9]"Structure-guided development of selective RabGGTase inhibitors."
Bon R.S., Guo Z., Stigter E.A., Wetzel S., Menninger S., Wolf A., Choidas A., Alexandrov K., Blankenfeldt W., Goody R.S., Waldmann H.
Angew. Chem. Int. Ed. Engl. 50:4957-4961(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[10]"Development of selective, potent RabGGTase inhibitors."
Stigter E.A., Guo Z., Bon R.S., Wu Y.W., Choidas A., Wolf A., Menninger S., Waldmann H., Blankenfeldt W., Goody R.S.
J. Med. Chem. 55:8330-8340(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10415 mRNA. Translation: AAA41998.1.
S62096 mRNA. Translation: AAB27018.1.
BC086547 mRNA. Translation: AAH86547.1.
PIRA45977.
RefSeqNP_113842.1. NM_031654.2.
XP_006252071.1. XM_006252009.1.
XP_006252072.1. XM_006252010.1.
UniGeneRn.29434.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCEX-ray2.00A/C1-567[»]
1LTXX-ray2.70A1-567[»]
3C72X-ray2.30A1-236[»]
A353-441[»]
3DSSX-ray1.80A1-237[»]
A353-441[»]
3DSTX-ray1.90A1-237[»]
A353-441[»]
3DSUX-ray1.90A1-237[»]
A353-441[»]
3DSVX-ray2.10A1-237[»]
A353-441[»]
3DSWX-ray2.15A1-237[»]
A353-441[»]
3DSXX-ray2.10A1-237[»]
A353-441[»]
3HXBX-ray2.25A1-237[»]
A353-441[»]
3HXCX-ray1.95A1-237[»]
A353-441[»]
3HXDX-ray1.95A1-237[»]
A353-441[»]
3HXEX-ray1.95A1-237[»]
A353-441[»]
3HXFX-ray1.90A1-237[»]
A353-441[»]
3PZ1X-ray1.95A1-237[»]
A353-441[»]
3PZ2X-ray2.35A1-237[»]
A353-441[»]
3PZ3X-ray2.00A1-237[»]
A353-441[»]
4EHMX-ray2.20A1-237[»]
A353-441[»]
4GTSX-ray2.45A1-237[»]
A353-441[»]
4GTTX-ray2.05A1-237[»]
A353-441[»]
4GTVX-ray1.95A1-237[»]
A353-441[»]
ProteinModelPortalQ08602.
SMRQ08602. Positions 2-567.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6137N.
STRING10116.ENSRNOP00000049261.

Proteomic databases

PRIDEQ08602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000048455; ENSRNOP00000049261; ENSRNOG00000030483.
GeneID58983.
KEGGrno:58983.
UCSCRGD:621697. rat.

Organism-specific databases

CTD5875.
RGD621697. Rabggta.

Phylogenomic databases

eggNOGCOG5536.
GeneTreeENSGT00550000075121.
HOGENOMHOG000007845.
HOVERGENHBG002171.
InParanoidQ08602.
KOK14050.
OMAWNCRREV.
OrthoDBEOG7PP56C.
PhylomeDBQ08602.
TreeFamTF315057.

Gene expression databases

GenevestigatorQ08602.

Family and domain databases

Gene3D2.60.40.1130. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF01239. PPTA. 5 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view]
ProDomPD331837. RabGG_trans_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF49594. SSF49594. 1 hit.
PROSITEPS51147. PFTA. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ08602.
NextBio611680.
PROQ08602.

Entry information

Entry namePGTA_RAT
AccessionPrimary (citable) accession number: Q08602
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references