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Q9Z2A9

- GGT5_MOUSE

UniProt

Q9Z2A9 - GGT5_MOUSE

Protein

Gamma-glutamyltransferase 5

Gene

Ggt5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (18 Sep 2013)
      Previous versions | rss
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    Functioni

    Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4).

    Catalytic activityi

    A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
    Glutathione + H2O = L-cysteinylglycine + L-glutamate.
    Leukotriene C4 + H2O = leukotriene D4 + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei110 – 1101GlutamateBy similarity
    Active sitei389 – 3891NucleophileBy similarity
    Binding sitei407 – 4071GlutamateBy similarity
    Binding sitei428 – 4281GlutamateBy similarity

    GO - Molecular functioni

    1. gamma-glutamyltransferase activity Source: MGI
    2. glutathione hydrolase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glutathione biosynthetic process Source: UniProtKB-KW
    2. inflammatory response Source: MGI
    3. leukotriene biosynthetic process Source: MGI

    Keywords - Molecular functioni

    Acyltransferase, Hydrolase, Protease, Transferase

    Keywords - Biological processi

    Glutathione biosynthesis, Leukotriene biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    SABIO-RKQ9Z2A9.
    UniPathwayiUPA00204.
    UPA00880.

    Protein family/group databases

    MEROPSiT03.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-glutamyltransferase 5 (EC:2.3.2.2)
    Short name:
    GGT 5
    Alternative name(s):
    Gamma-glutamyl leukotrienase
    Short name:
    GGL
    Gamma-glutamyltransferase-like activity 1
    Gamma-glutamyltranspeptidase 5
    Glutathione hydrolase 5 (EC:3.4.19.13)
    Leukotriene-C4 hydrolase (EC:3.4.19.14)
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Ggt5
    Synonyms:Ggtla1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1346063. Ggt5.

    Subcellular locationi

    Membrane By similarity; Single-pass type II membrane protein By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 388388Gamma-glutamyltransferase 5 heavy chainBy similarityPRO_0000011074Add
    BLAST
    Chaini389 – 573185Gamma-glutamyltransferase 5 light chainBy similarityPRO_0000011075Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Cleaved by autocatalysis into a large and a small subunit.By similarity

    Keywords - PTMi

    Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ9Z2A9.
    PaxDbiQ9Z2A9.
    PRIDEiQ9Z2A9.

    PTM databases

    PhosphoSiteiQ9Z2A9.

    Expressioni

    Tissue specificityi

    Very low level of expression. Detected in spleen lymphocytes, medullary and paracortical thymic lymphocytes, lung interstitial cells, bronchial epithelium, proximal tubules in kidney, crypt cells in small intestine, neurons in brain stem and cerebral cortex and in Purkinje cells.

    Gene expression databases

    CleanExiMM_GGT5.
    GenevestigatoriQ9Z2A9.

    Interactioni

    Subunit structurei

    Heterodimer composed of the light and heavy chains. The active site is located in the light chain By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000072074.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2A9.
    SMRiQ9Z2A9. Positions 35-573.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini30 – 573544ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni454 – 4552Glutamate bindingBy similarity

    Sequence similaritiesi

    Belongs to the gamma-glutamyltransferase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0405.
    GeneTreeiENSGT00550000074591.
    HOGENOMiHOG000175620.
    HOVERGENiHBG005835.
    InParanoidiQ9Z2A9.
    KOiK00681.
    OMAiCICAVSD.
    OrthoDBiEOG7V7665.
    TreeFamiTF313608.

    Family and domain databases

    InterProiIPR000101. GGT_peptidase.
    IPR029055. Ntn_hydrolases_N.
    [Graphical view]
    PANTHERiPTHR11686. PTHR11686. 1 hit.
    PfamiPF01019. G_glu_transpept. 1 hit.
    [Graphical view]
    PRINTSiPR01210. GGTRANSPTASE.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Z2A9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAWGHRATVC LVLLGVGLGL VIVVLAAVLS PRQASCGPGA FTRAAVAADS    50
    KICSDIGRAI LQQRGSPVDA AIAALVCTGV VNPQSMGLGG GVVFTIYNAS 100
    TGKVEIINAR ETVPASYDQG LLNQCKNVLP LGTGAQWIGV PGELRGYAEA 150
    HRRHGRLPWA QLFQPTIALL REGFRVPFIL SQFLNNSILR PHLSASTLRQ 200
    LFFNGTETLR SQDPFPWPAL ANTLETVAKE GAEVLYTGRL GRMLVEDIAK 250
    QGSLLTVQDL AAFQPEVVEP LEMPLGNYTL YSPPPPAGGA ILSFILNVLK 300
    GFNFSAETVA RPGGEVNMYH HLVETLKFAV GQRWRLWDPS SHPGIQNISR 350
    DLLREDLAQR IRQQIDGRGD HHQLSHYNLT GVRGNRMGTS HVSVLGEDGS 400
    AVAATSTINT PFGAMVYSPR TGILLNNELL DLCWRHMPTS PITPPPVPGE 450
    RPPSSMVPSI LVNKGQGSKL VIGGAGGELI ISAVAQTIMN KLWLGFDLTE 500
    AIASPILHVN SKGHVEYEPK FNQEVQKGLQ DRGQIQSQSQ RPVFLNAVQA 550
    VFQEGPCVYA ASDLRKAGKA SGY 573
    Length:573
    Mass (Da):61,674
    Last modified:September 18, 2013 - v2
    Checksum:iCB00F377DA1BE83E
    GO
    Isoform 2 (identifier: Q9Z2A9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         447-456: VPGERPPSSM → DYHEQAVAWL
         457-573: Missing.

    Note: Very low expression.

    Show »
    Length:456
    Mass (Da):49,360
    Checksum:iBEEEBF6F12478985
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti479 – 4791L → P in AAC71001. (PubMed:9774450)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei447 – 45610VPGERPPSSM → DYHEQAVAWL in isoform 2. 1 PublicationVSP_008147
    Alternative sequencei457 – 573117Missing in isoform 2. 1 PublicationVSP_008148Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077765 mRNA. Translation: AAC71001.1.
    AK052183 mRNA. Translation: BAC34873.1.
    AK170326 mRNA. Translation: BAE41720.1.
    AC087540 Genomic DNA. No translation available.
    CH466553 Genomic DNA. Translation: EDL31901.1.
    BC113775 mRNA. Translation: AAI13776.1.
    CCDSiCCDS23928.1. [Q9Z2A9-1]
    RefSeqiNP_035950.2. NM_011820.4. [Q9Z2A9-1]
    UniGeneiMm.257927.

    Genome annotation databases

    EnsembliENSMUST00000072217; ENSMUSP00000072074; ENSMUSG00000006344. [Q9Z2A9-1]
    GeneIDi23887.
    KEGGimmu:23887.
    UCSCiuc007fqq.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077765 mRNA. Translation: AAC71001.1 .
    AK052183 mRNA. Translation: BAC34873.1 .
    AK170326 mRNA. Translation: BAE41720.1 .
    AC087540 Genomic DNA. No translation available.
    CH466553 Genomic DNA. Translation: EDL31901.1 .
    BC113775 mRNA. Translation: AAI13776.1 .
    CCDSi CCDS23928.1. [Q9Z2A9-1 ]
    RefSeqi NP_035950.2. NM_011820.4. [Q9Z2A9-1 ]
    UniGenei Mm.257927.

    3D structure databases

    ProteinModelPortali Q9Z2A9.
    SMRi Q9Z2A9. Positions 35-573.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000072074.

    Protein family/group databases

    MEROPSi T03.002.

    PTM databases

    PhosphoSitei Q9Z2A9.

    Proteomic databases

    MaxQBi Q9Z2A9.
    PaxDbi Q9Z2A9.
    PRIDEi Q9Z2A9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000072217 ; ENSMUSP00000072074 ; ENSMUSG00000006344 . [Q9Z2A9-1 ]
    GeneIDi 23887.
    KEGGi mmu:23887.
    UCSCi uc007fqq.1. mouse.

    Organism-specific databases

    CTDi 2687.
    MGIi MGI:1346063. Ggt5.

    Phylogenomic databases

    eggNOGi COG0405.
    GeneTreei ENSGT00550000074591.
    HOGENOMi HOG000175620.
    HOVERGENi HBG005835.
    InParanoidi Q9Z2A9.
    KOi K00681.
    OMAi CICAVSD.
    OrthoDBi EOG7V7665.
    TreeFami TF313608.

    Enzyme and pathway databases

    UniPathwayi UPA00204 .
    UPA00880 .
    Reactomei REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    SABIO-RK Q9Z2A9.

    Miscellaneous databases

    NextBioi 303635.
    PROi Q9Z2A9.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_GGT5.
    Genevestigatori Q9Z2A9.

    Family and domain databases

    InterProi IPR000101. GGT_peptidase.
    IPR029055. Ntn_hydrolases_N.
    [Graphical view ]
    PANTHERi PTHR11686. PTHR11686. 1 hit.
    Pfami PF01019. G_glu_transpept. 1 hit.
    [Graphical view ]
    PRINTSi PR01210. GGTRANSPTASE.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gamma-glutamyl leukotrienase, a gamma-glutamyl transpeptidase gene family member, is expressed primarily in spleen."
      Carter B.Z., Shi Z.-Z., Barrios R., Lieberman M.W.
      J. Biol. Chem. 273:28277-28285(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6 X 129.
      Tissue: Spleen.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Heart.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].

    Entry informationi

    Entry nameiGGT5_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2A9
    Secondary accession number(s): Q8C7B4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2003
    Last sequence update: September 18, 2013
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3