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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

  1. Rab geranylgeranyltransferase activity Source: UniProtKB
  2. Rab GTPase binding Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein geranylgeranylation Source: UniProtKB
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
ProteomesiUP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. Rab-protein geranylgeranyltransferase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567Geranylgeranyl transferase type-2 subunit alphaPRO_0000229771Add
BLAST

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

Structurei

3D structure databases

ProteinModelPortaliQ5NVK5.
SMRiQ5NVK5. Positions 2-567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 7835PFTA 1Add
BLAST
Repeati88 – 12235PFTA 2Add
BLAST
Repeati124 – 15835PFTA 3Add
BLAST
Repeati159 – 19335PFTA 4Add
BLAST
Repeati207 – 24135PFTA 5Add
BLAST
Repeati363 – 39735PFTA 6Add
BLAST
Repeati442 – 46322LRR 1Add
BLAST
Repeati464 – 48623LRR 2Add
BLAST
Repeati487 – 50822LRR 3Add
BLAST
Repeati509 – 53022LRR 4Add
BLAST
Repeati534 – 55522LRR 5Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

HOVERGENiHBG002171.
InParanoidiQ5NVK5.
KOiK14050.

Family and domain databases

Gene3Di2.60.40.1130. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF01239. PPTA. 5 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.
SMRiQ5NVK5. Positions 2-567.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174130.
KEGGipon:100174130.

Organism-specific databases

CTDi5875.

Phylogenomic databases

HOVERGENiHBG002171.
InParanoidiQ5NVK5.
KOiK14050.

Family and domain databases

Gene3Di2.60.40.1130. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF01239. PPTA. 5 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...

Publicationsi

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

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: January 7, 2015
This is version 63 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

External Data

Dasty 3

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 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.