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Q08602

- PGTA_RAT

UniProt

Q08602 - PGTA_RAT

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
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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

    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

    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

    MHGRLKVKTS EEQAEAKRLE REQKLKLYQS ATQAVFQKRQ AGELDESVLE    50
    LTSQILGANP DFATLWNCRR EVLQHLETEK SPEESAALVK AELGFLESCL 100
    RVNPKSYGTW HHRCWLLSRL PEPNWARELE LCARFLEADE RNFHCWDYRR 150
    FVAAQAAVAP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ 200
    GRLPENVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAE PHDVLCCVHV 250
    SREEACLSVC FSRPLTVGSR MGTLLLMVDE APLSVEWRTP DGRNRPSHVW 300
    LCDLPAASLN DQLPQHTFRV IWTGSDSQKE CVLLKDRPEC WCRDSATDEQ 350
    LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY 400
    EKETLQYFST LKAVDPMRAA YLDDLRSKFL LENSVLKMEY ADVRVLHLAH 450
    KDLTVLCHLE QLLLVTHLDL SHNRLRALPP ALAALRCLEV LQASDNALEN 500
    VDGVANLPRL QELLLCNNRL QQSAAIQPLV SCPRLVLLNL QGNSLCQEEG 550
    IQERLAEMLP SVSSILT 567
    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_006252009.1.
    XP_006252072.1. XM_006252010.1.
    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_006252009.1.
    XP_006252072.1. XM_006252010.1.
    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

    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 1, 2014
    This is version 122 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