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Q5NVK5 (PGTA_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

Enzyme regulation

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

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 By similarity.

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_0000229771

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

Sequences

Sequence LengthMass (Da)Tools
Q5NVK5 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 6C511480882981F2

FASTA56765,107
        10         20         30         40         50         60 
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE LTSQILGANP 

        70         80         90        100        110        120 
DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL RVNPKSYGTW HHRCWLLGRL 

       130        140        150        160        170        180 
PEPNWTRELE LCARFLEVDE RNFHCWDYRR FVATQAAVPP AEELAFTDSL ITRNFSNYSS 

       190        200        210        220        230        240 
WHYRSCLLPQ LHPQPDSGPQ GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD 

       250        260        270        280        290        300 
PQDALRCLHV SREEACLTVS FSRPLLVGSR TEILLLMVDD SPLIVEWRTP DGRNRPSHVW 

       310        320        330        340        350        360 
LCDLPAASLN DQLPQHTFRV IWTAGDVQKE CVLLKGRQEG WCRDSTTDEQ LFRCELSVEK 

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

       430        440        450        460        470        480 
YLDDLRSKFL LENSVLKMEY AEVRVLHLAH KDLTVLCHLE QLLLVTHLDL SHNRLRTLPP 

       490        500        510        520        530        540 
ALAALRCLEV LQASDNAIES LDGVTNLPRL QELLLCNNRL QRPAVLQPLA SCPRLVLLNL 

       550        560 
QGNPLCQAVG ILEQLAELPP SVNSILT 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR926021 mRNA. Translation: CAI29658.1.
RefSeqNP_001127096.1. NM_001133624.1.
UniGenePab.536.

3D structure databases

ProteinModelPortalQ5NVK5.
SMRQ5NVK5. Positions 2-567.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174130.
KEGGpon:100174130.

Organism-specific databases

CTD5875.

Phylogenomic databases

HOVERGENHBG002171.
InParanoidQ5NVK5.
KOK14050.

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.
PROSITEPS51450. LRR. 5 hits.
PS51147. PFTA. 6 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGTA_PONAB
AccessionPrimary (citable) accession number: Q5NVK5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 61 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