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Protein

Geranylgeranyl transferase type-2 subunit alpha

Gene

RABGGTA

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RABGGTA
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002297711 – 567Geranylgeranyl transferase type-2 subunit alphaAdd BLAST567

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei98PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000006478.

Structurei

3D structure databases

ProteinModelPortaliQ5NVK5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati44 – 78PFTA 1Add BLAST35
Repeati88 – 122PFTA 2Add BLAST35
Repeati124 – 158PFTA 3Add BLAST35
Repeati159 – 193PFTA 4Add BLAST35
Repeati207 – 241PFTA 5Add BLAST35
Repeati363 – 397PFTA 6Add BLAST35
Repeati442 – 463LRR 1Add BLAST22
Repeati464 – 486LRR 2Add BLAST23
Repeati487 – 508LRR 3Add BLAST22
Repeati509 – 530LRR 4Add BLAST22
Repeati534 – 555LRR 5Add BLAST22

Sequence similaritiesi

Contains 5 LRR (leucine-rich) repeats.Curated
Contains 6 PFTA repeats.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG0529. Eukaryota.
COG5536. LUCA.
HOVERGENiHBG002171.
InParanoidiQ5NVK5.
KOiK14050.

Family and domain databases

Gene3Di2.60.40.1130. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
IPR032955. RabGGTase_alpha.
[Graphical view]
PANTHERiPTHR11129:SF2. PTHR11129:SF2. 2 hits.
PfamiPF01239. PPTA. 4 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view]
ProDomiPD331837. RabGG_trans_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49594. SSF49594. 1 hit.
PROSITEiPS51450. LRR. 5 hits.
PS51147. PFTA. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5NVK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE
60 70 80 90 100
LTSQILGANP DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL
110 120 130 140 150
RVNPKSYGTW HHRCWLLGRL PEPNWTRELE LCARFLEVDE RNFHCWDYRR
160 170 180 190 200
FVATQAAVPP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ
210 220 230 240 250
GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD PQDALRCLHV
260 270 280 290 300
SREEACLTVS FSRPLLVGSR TEILLLMVDD SPLIVEWRTP DGRNRPSHVW
310 320 330 340 350
LCDLPAASLN DQLPQHTFRV IWTAGDVQKE CVLLKGRQEG WCRDSTTDEQ
360 370 380 390 400
LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY
410 420 430 440 450
EKETLRYFQT LKAVDPMRAA YLDDLRSKFL LENSVLKMEY AEVRVLHLAH
460 470 480 490 500
KDLTVLCHLE QLLLVTHLDL SHNRLRTLPP ALAALRCLEV LQASDNAIES
510 520 530 540 550
LDGVTNLPRL QELLLCNNRL QRPAVLQPLA SCPRLVLLNL QGNPLCQAVG
560
ILEQLAELPP SVNSILT
Length:567
Mass (Da):65,107
Last modified:January 4, 2005 - v1
Checksum:i6C511480882981F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR926021 mRNA. Translation: CAI29658.1.
RefSeqiNP_001127096.1. NM_001133624.1.
UniGeneiPab.536.

Genome annotation databases

GeneIDi100174130.
KEGGipon:100174130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR926021 mRNA. Translation: CAI29658.1.
RefSeqiNP_001127096.1. NM_001133624.1.
UniGeneiPab.536.

3D structure databases

ProteinModelPortaliQ5NVK5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000006478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174130.
KEGGipon:100174130.

Organism-specific databases

CTDi5875.

Phylogenomic databases

eggNOGiKOG0529. Eukaryota.
COG5536. LUCA.
HOVERGENiHBG002171.
InParanoidiQ5NVK5.
KOiK14050.

Family and domain databases

Gene3Di2.60.40.1130. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
IPR032955. RabGGTase_alpha.
[Graphical view]
PANTHERiPTHR11129:SF2. PTHR11129:SF2. 2 hits.
PfamiPF01239. PPTA. 4 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view]
ProDomiPD331837. RabGG_trans_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49594. SSF49594. 1 hit.
PROSITEiPS51450. LRR. 5 hits.
PS51147. PFTA. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGTA_PONAB
AccessioniPrimary (citable) accession number: Q5NVK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 4, 2005
Last modified: October 5, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.