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A5A779 (PGTA_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

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_0000331286

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
A5A779 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 79BFCA2DD50C4F97

FASTA56764,901
        10         20         30         40         50         60 
MHGRLKVKTS EEQAEAKRLE REQKLKLYQT ATQTVFQKRQ AGELDESVLE LTSQILGANP 

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

       130        140        150        160        170        180 
PEPNWARELE LCARFLEVDE RNFHCWDYRR FVASQAAVPP AEELAFTDSL ITRNFSNYSS 

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

       250        260        270        280        290        300 
PQDALRCLHV SRDEACLTVS FSRPLLVGPS TETLLLMVNE SPLSVEWRTP DGRNRPSHVW 

       310        320        330        340        350        360 
LCDLPAASLN DHLPQHTFRV IWTAGNAQKE CVLLKGRQEG WCRDSATDEQ LFRCELSVEK 

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

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

       490        500        510        520        530        540 
ALAALRCLEV LQANDNAIES LDGVTNLPRL QELSLCNNRL QQPAVLQPLA SCPRLVLLNL 

       550        560 
QDNPLCQAVG ISEHLAELLP SVSSILT 

« Hide

References

[1]"Sequences and genetic variations of fourty-four porcine coat color related genes."
Okumura N., Matsumoto T., Hamasima N., Uenishi H., Ogawa T., Komatsuda A., Fukudome N., Ide H., Suzuki A., Kojima C., Awata T.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB271949 mRNA. Translation: BAF62324.1.
RefSeqNP_001092063.1. NM_001098593.1.
XP_005666280.1. XM_005666223.1.
UniGeneSsc.45681.

3D structure databases

ProteinModelPortalA5A779.
SMRA5A779. Positions 2-567.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000002178.

Proteomic databases

PaxDbA5A779.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000002230; ENSSSCP00000002178; ENSSSCG00000001992.
GeneID100049679.
KEGGssc:100049679.

Organism-specific databases

CTD5875.

Phylogenomic databases

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

Family and domain databases

Gene3D2.60.40.1130. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF12799. LRR_4. 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...

Entry information

Entry namePGTA_PIG
AccessionPrimary (citable) accession number: A5A779
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 51 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