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Q08602

- PGTA_RAT

UniProt

Q08602 - PGTA_RAT

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Protein

Geranylgeranyl transferase type-2 subunit alpha

Gene

Rabggta

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- 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

  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
Synonyms:Ggta
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 15

Organism-specific databases

RGDi621697. Rabggta.

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_0000119759Add
BLAST

Proteomic databases

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

GenevestigatoriQ08602.

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

Protein-protein interaction databases

DIPiDIP-6137N.
STRINGi10116.ENSRNOP00000049261.

Structurei

Secondary structure

1
567
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 4028
Helixi46 – 5611
Helixi63 – 7917
Helixi82 – 10221
Helixi107 – 11913
Beta strandi120 – 1223
Helixi125 – 13814
Helixi143 – 15513
Helixi160 – 17314
Helixi178 – 19114
Beta strandi197 – 1993
Helixi205 – 22117
Helixi226 – 23712
Beta strandi245 – 2517
Turni252 – 2554
Beta strandi256 – 26510
Beta strandi267 – 2693
Beta strandi274 – 28310
Beta strandi296 – 3038
Helixi306 – 3083
Beta strandi313 – 32210
Turni323 – 3264
Beta strandi327 – 3348
Beta strandi338 – 3436
Turni347 – 3504
Helixi353 – 3553
Helixi358 – 37720
Helixi382 – 39514
Turni397 – 4004
Helixi401 – 41414
Helixi416 – 4183
Helixi419 – 43820
Beta strandi444 – 4474
Helixi459 – 4624
Beta strandi467 – 4693
Helixi480 – 4845
Beta strandi490 – 4923
Helixi502 – 5043
Beta strandi512 – 5143
Beta strandi522 – 5243
Helixi527 – 5315
Beta strandi537 – 5393
Helixi544 – 5474
Beta strandi548 – 5503
Helixi554 – 5585
Beta strandi563 – 5664

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 2-567.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08602.

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

eggNOGiCOG5536.
GeneTreeiENSGT00550000075121.
HOGENOMiHOG000007845.
HOVERGENiHBG002171.
InParanoidiQ08602.
KOiK14050.
OMAiWNCRREV.
OrthoDBiEOG7PP56C.
PhylomeDBiQ08602.
TreeFamiTF315057.

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.
PROSITEiPS51147. PFTA. 6 hits.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691S → D AA sequence (PubMed:8505342)Curated
Sequence conflicti227 – 2271S → Q AA sequence (PubMed:8505342)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006252009.2.
XP_006252072.1. XM_006252010.2.
UniGeneiRn.29434.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L10415 mRNA. Translation: AAA41998.1 .
S62096 mRNA. Translation: AAB27018.1 .
BC086547 mRNA. Translation: AAH86547.1 .
PIRi A45977.
RefSeqi NP_113842.1. NM_031654.2.
XP_006252071.1. XM_006252009.2.
XP_006252072.1. XM_006252010.2.
UniGenei Rn.29434.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DCE X-ray 2.00 A/C 1-567 [» ]
1LTX X-ray 2.70 A 1-567 [» ]
3C72 X-ray 2.30 A 1-236 [» ]
A 353-441 [» ]
3DSS X-ray 1.80 A 1-237 [» ]
A 353-441 [» ]
3DST X-ray 1.90 A 1-237 [» ]
A 353-441 [» ]
3DSU X-ray 1.90 A 1-237 [» ]
A 353-441 [» ]
3DSV X-ray 2.10 A 1-237 [» ]
A 353-441 [» ]
3DSW X-ray 2.15 A 1-237 [» ]
A 353-441 [» ]
3DSX X-ray 2.10 A 1-237 [» ]
A 353-441 [» ]
3HXB X-ray 2.25 A 1-237 [» ]
A 353-441 [» ]
3HXC X-ray 1.95 A 1-237 [» ]
A 353-441 [» ]
3HXD X-ray 1.95 A 1-237 [» ]
A 353-441 [» ]
3HXE X-ray 1.95 A 1-237 [» ]
A 353-441 [» ]
3HXF X-ray 1.90 A 1-237 [» ]
A 353-441 [» ]
3PZ1 X-ray 1.95 A 1-237 [» ]
A 353-441 [» ]
3PZ2 X-ray 2.35 A 1-237 [» ]
A 353-441 [» ]
3PZ3 X-ray 2.00 A 1-237 [» ]
A 353-441 [» ]
4EHM X-ray 2.20 A 1-237 [» ]
A 353-441 [» ]
4GTS X-ray 2.45 A 1-237 [» ]
A 353-441 [» ]
4GTT X-ray 2.05 A 1-237 [» ]
A 353-441 [» ]
4GTV X-ray 1.95 A 1-237 [» ]
A 353-441 [» ]
ProteinModelPortali Q08602.
SMRi Q08602. Positions 2-567.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6137N.
STRINGi 10116.ENSRNOP00000049261.

Proteomic databases

PRIDEi Q08602.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000048455 ; ENSRNOP00000049261 ; ENSRNOG00000030483 .
GeneIDi 58983.
KEGGi rno:58983.
UCSCi RGD:621697. rat.

Organism-specific databases

CTDi 5875.
RGDi 621697. Rabggta.

Phylogenomic databases

eggNOGi COG5536.
GeneTreei ENSGT00550000075121.
HOGENOMi HOG000007845.
HOVERGENi HBG002171.
InParanoidi Q08602.
KOi K14050.
OMAi WNCRREV.
OrthoDBi EOG7PP56C.
PhylomeDBi Q08602.
TreeFami TF315057.

Miscellaneous databases

EvolutionaryTracei Q08602.
NextBioi 611680.
PROi Q08602.

Gene expression databases

Genevestigatori Q08602.

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 PS51147. PFTA. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of the alpha and beta subunits of rat Rab geranylgeranyl transferase."
    Armstrong S.A., Seabra M.C., Suedhof T.C., Goldstein J.L., Brown M.S.
    J. Biol. Chem. 268:12221-12229(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. "Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase with REP-1."
    Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K.
    J. Biol. Chem. 276:48637-48643(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  4. "Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution."
    Zhang H., Seabra M.C., Deisenhofer J.
    Structure 8:241-251(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RABGGTB, SUBUNIT.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH GERANYGERANYL PHOSHATE ANALOG; RABGGTB AND CHM/REP1, SUBUNIT.
  6. "Development of selective RabGGTase inhibitors and crystal structure of a RabGGTase-inhibitor complex."
    Guo Z., Wu Y.W., Tan K.T., Bon R.S., Guiu-Rozas E., Delon C., Nguyen T.U., Wetzel S., Arndt S., Goody R.S., Blankenfeldt W., Alexandrov K., Waldmann H.
    Angew. Chem. Int. Ed. Engl. 47:3747-3750(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-441 IN COMPLEX WITH INHIBITOR, FUNCTION, SUBUNIT.
  7. "Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation."
    Guo Z., Wu Y.W., Das D., Delon C., Cramer J., Yu S., Thuns S., Lupilova N., Waldmann H., Brunsveld L., Goody R.S., Alexandrov K., Blankenfeldt W.
    EMBO J. 27:2444-2456(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  8. "Design, synthesis, and characterization of peptide-based rab geranylgeranyl transferase inhibitors."
    Tan K.T., Guiu-Rozas E., Bon R.S., Guo Z., Delon C., Wetzel S., Arndt S., Alexandrov K., Waldmann H., Goody R.S., Wu Y.W., Blankenfeldt W.
    J. Med. Chem. 52:8025-8037(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-441, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.

Entry informationi

Entry nameiPGTA_RAT
AccessioniPrimary (citable) accession number: Q08602
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 123 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

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

External Data

Dasty 3