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A6NGU5

- GGT3_HUMAN

UniProt

A6NGU5 - GGT3_HUMAN

Protein

Putative gamma-glutamyltranspeptidase 3

Gene

GGT3P

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Protein uncertaini
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Initiates extracellular glutathione (GSH) breakdown; catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei107 – 1071GlutamateBy similarity
    Active sitei381 – 3811NucleophileBy similarity
    Binding sitei399 – 3991GlutamateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glutathione biosynthetic process Source: UniProtKB-KW
    2. glutathione metabolic process Source: UniProtKB
    3. leukotriene biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Hydrolase, Protease, Transferase

    Keywords - Biological processi

    Glutathione biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00204.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative gamma-glutamyltranspeptidase 3 (EC:2.3.2.2)
    Short name:
    GGT 3
    Alternative name(s):
    Gamma-glutamyltransferase 3
    Glutathione hydrolase 3 (EC:3.4.19.13)
    Cleaved into the following 2 chains:
    Gene namesi
    Name:GGT3P
    Synonyms:GGT3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:4252. GGT3P.

    Subcellular locationi

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

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 380380Putative gamma-glutamyltranspeptidase 3 heavy chainBy similarityPRO_0000334690Add
    BLAST
    Chaini381 – 568188Putative gamma-glutamyltranspeptidase 3 light chainBy similarityPRO_0000334691Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi510 – 5101N-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

    PRIDEiA6NGU5.

    Expressioni

    Gene expression databases

    GenevestigatoriA6NGU5.

    Organism-specific databases

    HPAiHPA045635.

    Structurei

    3D structure databases

    ProteinModelPortaliA6NGU5.
    SMRiA6NGU5. Positions 33-375, 381-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini27 – 568542ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2622Helical; Signal-anchor for type II membrane proteinCuratedAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni450 – 4512Glutamate bindingBy similarity

    Sequence similaritiesi

    Belongs to the gamma-glutamyltransferase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG005835.
    InParanoidiA6NGU5.

    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.
    TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
    PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    A6NGU5-1 [UniParc]FASTAAdd to Basket

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    MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAVAADAKQC    50
    LEIGRDTLRD GGSAVDAAIA ALLCVGLMNA HSMGIGVGLF LTIYNSTTRK 100
    AEVINAREVA PRLAFASMFN SSEQSQKGGL SVAVPGEIRG YELAHQRHGR 150
    LPWARLFQPS IQLARQGFPV GKGLAAVLEN KRTVIEQQPV LCEVFCRDRK 200
    VLREGERLTL PRLADTYEML AIEGAQAFYN GSLMAQIVKD IQAAGGIVTA 250
    EDLNNYCAEL IEHPLNISLG DAVLYMPSAR LSGPVLALIL NILKGYNFSR 300
    ESVETPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF 350
    AAQLRSQISD HTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI 400
    NLYFGSKVCS PVSGILFNNM DDFSSPSITN EFGAPPSPAN FIQPGKQPLL 450
    SMCPTIMVGQ DGQVRMVVGA AGGTQITTDT ALAIIYNLWF GYDVKRAVEE 500
    PRLHNKLLPN VTTVERNIDQ AVTAALETRH HHTQIASTFI AVVQAIVRTA 550
    GGWAAASDSR KGGEPAGY 568
    Length:568
    Mass (Da):61,502
    Last modified:January 15, 2008 - v2
    Checksum:i48BF7C2A2DFEF165
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC008132 Genomic DNA. No translation available.
    UniGeneiHs.595809.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC008132 Genomic DNA. No translation available.
    UniGenei Hs.595809.

    3D structure databases

    ProteinModelPortali A6NGU5.
    SMRi A6NGU5. Positions 33-375, 381-568.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi A6NGU5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    GeneCardsi GC22M018765.
    HGNCi HGNC:4252. GGT3P.
    HPAi HPA045635.
    neXtProti NX_A6NGU5.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG005835.
    InParanoidi A6NGU5.

    Enzyme and pathway databases

    UniPathwayi UPA00204 .

    Gene expression databases

    Genevestigatori A6NGU5.

    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.
    TIGRFAMsi TIGR00066. g_glut_trans. 1 hit.
    PROSITEi PS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Assessment of copper status in epileptic patients treated with anticonvulsant drugs by measuring the specific oxidase activity of ceruloplasmin."
      Tutor-Crespo M.J., Hermida J., Tutor J.C.
      Epilepsy Res. 56:147-153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN EPILEPSY.
    3. Cited for: IDENTIFICATION, NOMENCLATURE.

    Entry informationi

    Entry nameiGGT3_HUMAN
    AccessioniPrimary (citable) accession number: A6NGU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 60 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    In some epileptic patients treated with phenytoin, phenobarbital and carbamazepin, GGT3 is found, as an additional form of GGT. This group of patients has levels of ceruloplasmin and oxidase activity that were significantly higher than in the group of patients without GGT3. However, levels of ceruloplasmin and oxidase activity are significantly higher in this group of patients without GGT3 than those of the control group.

    Caution

    Could be the product of a pseudogene. According to PubMed:18357469, it is not functional.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3