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Q08603 (PGTB2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. 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 beta

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

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.5 Ref.6 Ref.7 Ref.8 Ref.9

Catalytic activity

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Cofactor

Binds 1 zinc ion per subunit. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

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. Interaction of RABGGTB with prenylated PTP4A2 precludes its association with RABGGTA and inhibits enzyme activity. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

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.

Sequence similarities

Belongs to the protein prenyltransferase subunit beta family.

Contains 6 PFTB repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 331330Geranylgeranyl transferase type-2 subunit beta
PRO_0000119774

Regions

Repeat20 – 6142PFTB 1
Repeat68 – 10942PFTB 2
Repeat116 – 15742PFTB 3
Repeat164 – 20542PFTB 4
Repeat212 – 25342PFTB 5
Repeat260 – 30243PFTB 6
Region190 – 1923Geranylgeranyl diphosphate binding
Region232 – 24413Geranylgeranyl diphosphate binding

Sites

Metal binding2381Zinc; catalytic
Metal binding2401Zinc; catalytic
Metal binding2901Zinc; via tele nitrogen; catalytic

Amino acid modifications

Modified residue21N-acetylglycine By similarity
Modified residue31Phosphothreonine By similarity

Secondary structure

...................................................... 331
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08603 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 4B12DEC0245979D6

FASTA33136,856
        10         20         30         40         50         60 
MGTQQKDVTI KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGV YWGLTVMDLM 

        70         80         90        100        110        120 
GQLHRMNKEE ILVFIKSCQH ECGGVSASIG HDPHLLYTLS AVQILTLYDS IHVINVDKVV 

       130        140        150        160        170        180 
AYVQSLQKED GSFAGDIWGE IDTRFSFCAV ATLALLGKLD AINVEKAIEF VLSCMNFDGG 

       190        200        210        220        230        240 
FGCRPGSESH AGQIYCCTGF LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC 

       250        260        270        280        290        300 
YSWWVLASLK IIGRLHWIDR EKLRSFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL 

       310        320        330 
LGEEQIKPVS PVFCMPEEVL QRVNVQPELV S 

« Hide

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, CATALYTIC ACTIVITY.
Tissue: Brain.
[2]"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.
[3]"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 RABGGTA AND ZINC IONS, SUBUNIT, COFACTOR.
[4]"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 (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS; GERANYGERANYL PHOSHATE ANALOG; RAB7A; RABGGTA AND CHM, SUBUNIT, COFACTOR.
[5]"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) IN COMPLEX WITH RABGGTA; INHIBITOR AND ZINC IONS, FUNCTION, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY.
[6]"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) IN COMPLEXES WITH RABGGTA; RAB7A; GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
[7]"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) IN COMPLEX WITH RABGGTA; ZINC IONS AND INHIBITOR, SUBUNIT, COFACTOR, FUNCTION, CATALYTIC ACTIVITY.
[8]"Psoromic acid is a selective and covalent Rab-prenylation inhibitor targeting autoinhibited RabGGTase."
Deraeve C., Guo Z., Bon R.S., Blankenfeldt W., DiLucrezia R., Wolf A., Menninger S., Stigter E.A., Wetzel S., Choidas A., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W.
J. Am. Chem. Soc. 134:7384-7391(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH RABGGTA; ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
[9]"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) IN COMPLEX WITH RABGGTA; ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10416 mRNA. Translation: AAA41999.1.
S62097 mRNA. Translation: AAB27019.1.
PIRB45977.
RefSeqNP_619715.1. NM_138708.2.
UniGeneRn.107818.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCEX-ray2.00B/D1-331[»]
1LTXX-ray2.70B1-331[»]
3C72X-ray2.30B1-331[»]
3DSSX-ray1.80B1-331[»]
3DSTX-ray1.90B1-331[»]
3DSUX-ray1.90B1-331[»]
3DSVX-ray2.10B1-331[»]
3DSWX-ray2.15B1-331[»]
3DSXX-ray2.10B1-331[»]
3HXBX-ray2.25B1-331[»]
3HXCX-ray1.95B1-331[»]
3HXDX-ray1.95B1-331[»]
3HXEX-ray1.95B1-331[»]
3HXFX-ray1.90B1-331[»]
4EHMX-ray2.20B2-331[»]
4GTSX-ray2.45B2-331[»]
4GTTX-ray2.05B2-331[»]
4GTVX-ray1.95B2-331[»]
ProteinModelPortalQ08603.
SMRQ08603. Positions 3-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6138N.

Proteomic databases

PaxDbQ08603.
PRIDEQ08603.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25533.
KEGGrno:25533.

Organism-specific databases

CTD5876.
RGD3530. Rabggtb.

Phylogenomic databases

eggNOGCOG5029.
HOVERGENHBG008182.
InParanoidQ08603.
KOK05956.
PhylomeDBQ08603.

Gene expression databases

GenevestigatorQ08603.

Family and domain databases

Gene3D1.50.10.20. 1 hit.
InterProIPR001330. Prenyltrans.
IPR026873. Ptb1.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERPTHR11774:SF9. PTHR11774:SF9. 1 hit.
PfamPF00432. Prenyltrans. 2 hits.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ08603.
NextBio607037.
PROQ08603.

Entry information

Entry namePGTB2_RAT
AccessionPrimary (citable) accession number: Q08603
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 108 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