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Protein

Geranylgeranyl transferase type-2 subunit alpha

Gene

Rabggta

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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.6 Publications

Catalytic activityi

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.4 Publications

Enzyme regulationi

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

GO - Molecular functioni

  • protein heterodimerization activity Source: CAFA
  • Rab geranylgeranyltransferase activity Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • protein-containing complex assembly Source: CAFA
  • protein geranylgeranylation Source: UniProtKB

Keywordsi

Molecular functionPrenyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-RNO-6803205 TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain
R-RNO-8873719 RAB geranylgeranylation

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
Synonyms:Ggta
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi621697 Rabggta

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197591 – 567Geranylgeranyl transferase type-2 subunit alphaAdd BLAST567

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei98PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ08602
PRIDEiQ08602

Expressioni

Tissue specificityi

Most abundant in the heart, brain, spleen and liver. Less in the lung, muscle, kidney and testis; in these tissues less abundant than the beta subunit.

Gene expression databases

BgeeiENSRNOG00000030483
GenevisibleiQ08602 RN

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.9 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: CAFA
  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-6137N
IntActiQ08602, 1 interactor
STRINGi10116.ENSRNOP00000049261

Structurei

Secondary structure

1567
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 40Combined sources28
Helixi46 – 56Combined sources11
Helixi63 – 79Combined sources17
Helixi82 – 102Combined sources21
Helixi107 – 119Combined sources13
Beta strandi120 – 122Combined sources3
Helixi125 – 138Combined sources14
Helixi143 – 155Combined sources13
Helixi160 – 173Combined sources14
Helixi178 – 191Combined sources14
Beta strandi197 – 199Combined sources3
Helixi205 – 221Combined sources17
Helixi226 – 237Combined sources12
Beta strandi245 – 251Combined sources7
Turni252 – 255Combined sources4
Beta strandi256 – 265Combined sources10
Beta strandi267 – 269Combined sources3
Beta strandi274 – 283Combined sources10
Beta strandi296 – 303Combined sources8
Helixi306 – 308Combined sources3
Beta strandi313 – 322Combined sources10
Turni323 – 326Combined sources4
Beta strandi327 – 334Combined sources8
Beta strandi338 – 343Combined sources6
Turni347 – 350Combined sources4
Helixi353 – 355Combined sources3
Helixi358 – 377Combined sources20
Helixi382 – 395Combined sources14
Turni397 – 400Combined sources4
Helixi401 – 414Combined sources14
Helixi416 – 418Combined sources3
Helixi419 – 438Combined sources20
Beta strandi444 – 447Combined sources4
Helixi459 – 462Combined sources4
Beta strandi467 – 469Combined sources3
Helixi480 – 484Combined sources5
Beta strandi490 – 492Combined sources3
Helixi502 – 504Combined sources3
Beta strandi512 – 514Combined sources3
Beta strandi522 – 524Combined sources3
Helixi527 – 531Combined sources5
Beta strandi537 – 539Combined sources3
Helixi544 – 547Combined sources4
Beta strandi548 – 550Combined sources3
Helixi554 – 558Combined sources5
Beta strandi563 – 566Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DCEX-ray2.00A/C1-567[»]
1LTXX-ray2.70A1-567[»]
3C72X-ray2.30A1-236[»]
A353-441[»]
3DSSX-ray1.80A1-237[»]
A353-441[»]
3DSTX-ray1.90A1-237[»]
A353-441[»]
3DSUX-ray1.90A1-237[»]
A353-441[»]
3DSVX-ray2.10A1-237[»]
A353-441[»]
3DSWX-ray2.15A1-237[»]
A353-441[»]
3DSXX-ray2.10A1-237[»]
A353-441[»]
3HXBX-ray2.25A1-237[»]
A353-441[»]
3HXCX-ray1.95A1-237[»]
A353-441[»]
3HXDX-ray1.95A1-237[»]
A353-441[»]
3HXEX-ray1.95A1-237[»]
A353-441[»]
3HXFX-ray1.90A1-237[»]
A353-441[»]
3PZ1X-ray1.95A1-237[»]
A353-441[»]
3PZ2X-ray2.35A1-237[»]
A353-441[»]
3PZ3X-ray2.00A1-237[»]
A353-441[»]
4EHMX-ray2.20A1-237[»]
A353-441[»]
4GTSX-ray2.45A1-237[»]
A353-441[»]
4GTTX-ray2.05A1-237[»]
A353-441[»]
4GTVX-ray1.95A1-237[»]
A353-441[»]
ProteinModelPortaliQ08602
SMRiQ08602
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08602

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

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG0529 Eukaryota
COG5536 LUCA
GeneTreeiENSGT00550000075121
HOGENOMiHOG000007845
HOVERGENiHBG002171
InParanoidiQ08602
KOiK14050
OMAiMRAAYLD
OrthoDBiEOG091G0L9H
PhylomeDBiQ08602
TreeFamiTF315057

Family and domain databases

Gene3Di3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR032675 LRR_dom_sf
IPR002088 Prenyl_trans_a
IPR036254 RabGGT_asu_insert-dom_sf
IPR009087 RabGGT_asu_insert-domain
IPR032955 RabGGTase_alpha
PANTHERiPTHR11129:SF2 PTHR11129:SF2, 1 hit
PfamiView protein in Pfam
PF01239 PPTA, 4 hits
PF07711 RabGGT_insert, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD331837 RabGG_trans_A, 1 hit
SUPFAMiSSF49594 SSF49594, 1 hit
PROSITEiView protein in PROSITE
PS51147 PFTA, 6 hits

Sequencei

Sequence statusi: Complete.

Q08602-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE
60 70 80 90 100
LTSQILGANP DFATLWNCRR EVLQHLETEK SPEESAALVK AELGFLESCL
110 120 130 140 150
RVNPKSYGTW HHRCWLLSRL PEPNWARELE LCARFLEADE RNFHCWDYRR
160 170 180 190 200
FVAAQAAVAP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ
210 220 230 240 250
GRLPENVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAE PHDVLCCVHV
260 270 280 290 300
SREEACLSVC FSRPLTVGSR MGTLLLMVDE APLSVEWRTP DGRNRPSHVW
310 320 330 340 350
LCDLPAASLN DQLPQHTFRV IWTGSDSQKE CVLLKDRPEC WCRDSATDEQ
360 370 380 390 400
LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY
410 420 430 440 450
EKETLQYFST LKAVDPMRAA YLDDLRSKFL LENSVLKMEY ADVRVLHLAH
460 470 480 490 500
KDLTVLCHLE QLLLVTHLDL SHNRLRALPP ALAALRCLEV LQASDNALEN
510 520 530 540 550
VDGVANLPRL QELLLCNNRL QQSAAIQPLV SCPRLVLLNL QGNSLCQEEG
560
IQERLAEMLP SVSSILT
Length:567
Mass (Da):64,904
Last modified:February 1, 1995 - v1
Checksum:i1F9D235F973EABD5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti169S → D AA sequence (PubMed:8505342).Curated1
Sequence conflicti227S → Q AA sequence (PubMed:8505342).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10415 mRNA Translation: AAA41998.1
S62096 mRNA Translation: AAB27018.1
BC086547 mRNA Translation: AAH86547.1
PIRiA45977
RefSeqiNP_113842.1, NM_031654.2
XP_006252071.1, XM_006252009.3
XP_006252072.1, XM_006252010.3
UniGeneiRn.29434

Genome annotation databases

EnsembliENSRNOT00000048455; ENSRNOP00000049261; ENSRNOG00000030483
GeneIDi58983
KEGGirno:58983
UCSCiRGD:621697 rat

Similar proteinsi

Entry informationi

Entry nameiPGTA_RAT
AccessioniPrimary (citable) accession number: Q08602
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 25, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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