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Q5NVK5

- PGTA_PONAB

UniProt

Q5NVK5 - PGTA_PONAB

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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: 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 GTPase binding Source: UniProtKB
  2. Rab geranylgeranyltransferase activity Source: UniProtKB
  3. zinc ion binding Source: InterPro
Complete GO annotation...

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: 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 alpha
PRO_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.

Structurei

3D structure databases

ProteinModelPortaliQ5NVK5.
SMRiQ5NVK5. Positions 2-567.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 6 PFTA repeats.

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

MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE    50
LTSQILGANP DFATLWNCRR EVLQQLETQK SPEELAALVK AELGFLESCL 100
RVNPKSYGTW HHRCWLLGRL PEPNWTRELE LCARFLEVDE RNFHCWDYRR 150
FVATQAAVPP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ 200
GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD PQDALRCLHV 250
SREEACLTVS FSRPLLVGSR TEILLLMVDD SPLIVEWRTP DGRNRPSHVW 300
LCDLPAASLN DQLPQHTFRV IWTAGDVQKE CVLLKGRQEG WCRDSTTDEQ 350
LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY 400
EKETLRYFQT LKAVDPMRAA YLDDLRSKFL LENSVLKMEY AEVRVLHLAH 450
KDLTVLCHLE QLLLVTHLDL SHNRLRTLPP ALAALRCLEV LQASDNAIES 500
LDGVTNLPRL QELLLCNNRL QRPAVLQPLA SCPRLVLLNL QGNPLCQAVG 550
ILEQLAELPP SVNSILT 567
Length:567
Mass (Da):65,107
Last modified:January 4, 2005 - v1
Checksum:i6C511480882981F2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CR926021 mRNA. Translation: CAI29658.1 .
RefSeqi NP_001127096.1. NM_001133624.1.
UniGenei Pab.536.

3D structure databases

ProteinModelPortali Q5NVK5.
SMRi Q5NVK5. Positions 2-567.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100174130.
KEGGi pon:100174130.

Organism-specific databases

CTDi 5875.

Phylogenomic databases

HOVERGENi HBG002171.
InParanoidi Q5NVK5.
KOi K14050.

Family and domain databases

Gene3Di 2.60.40.1130. 1 hit.
InterProi IPR001611. Leu-rich_rpt.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view ]
Pfami PF00560. LRR_1. 1 hit.
PF01239. PPTA. 5 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view ]
ProDomi PD331837. RabGG_trans_A. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF49594. SSF49594. 1 hit.
PROSITEi PS51450. LRR. 5 hits.
PS51147. PFTA. 6 hits.
[Graphical view ]
ProtoNeti Search...

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: February 19, 2014
This is version 61 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

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