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Reviewed, UniProtKB/Swiss-Prot P20735 (GGT1_PIG)

Last modified October 13, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Gamma-glutamyltranspeptidase 1
    EC=2.3.2.2
Alternative name(s):
    Gamma-glutamyltransferase 1
      Short name=GGT 1
    CD_antigen=CD224
Cleaved into the following 2 chains:
    1- Recommended name:
            Gamma-glutamyltranspeptidase 1 heavy chain
    2- Recommended name:
            Gamma-glutamyltranspeptidase 1 light chain
Gene names
Name: GGT1
Synonyms: GGT
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate.

Catalytic activity

(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid.

Pathway

Sulfur metabolism; glutathione metabolism.

Subunit structure

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

Subcellular location

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

Tissue specificity

Highly expressed in kidney. Detected at lower levels in liver, lung, plexus choroideus and brain capillary endothelial cells.

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

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Ontologies

Keywords
   Biological processGlutathione biosynthesis
   Cellular componentMembrane
   DomainSignal-anchor
Transmembrane
   Molecular functionAcyltransferase
Transferase
   PTMGlycoprotein
Zymogen
Gene Ontology (GO)
   Biological processglutathione biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

gamma-glutamyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Gamma-glutamyltranspeptidase 1 heavy chain
PRO_0000011062
Chain380 – 568189Gamma-glutamyltranspeptidase 1 light chain
PRO_0000011063

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2622Signal-anchor for type II membrane protein Probable
Topological domain27 – 568542Extracellular Potential

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation2291N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential
Glycosylation5101N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
P20735-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: EB2D1896B1229487

FASTA56861,316
        10         20         30         40         50         60 
MKKRYLLLAL AAVALVLLIL GLCLWLPSNS KPHNHVYPRA AVAADALRCS EIGRDTLRDG 

        70         80         90        100        110        120 
GSAVDAAIAA LLCVGLMNAH SMGIGGGLFL TIYNSTTRKA EIINAREVAP RLASASMFNS 

       130        140        150        160        170        180 
SEQSEEGGLS VAVPGEIRGY ELAHQRHGRL PWARLFQPSI ELASQGFPVG KGLAAALERS 

       190        200        210        220        230        240 
QDAIKRHPAL CEVFCRNGNV LREGDLVTMP RLAKTYETLA VEGAQAFYNG SLTAQIVKDI 

       250        260        270        280        290        300 
QEAGGIVTAE DLNNYRAELI EQPLRISLGD AQLYAPNAPL SGPVLALILN ILKGYNFSRA 

       310        320        330        340        350        360 
SVETPEQKGL TYHRIVEAFR FAYAKRTLLG DPKFVNVTEV VRNMSSEFFA DQLRARISDT 

       370        380        390        400        410        420 
TTHPDSYYEP EFYTPDDAGT AHLSVVSDDG SAVSATSTIN LYFGSKVRSR ISGILFNDEM 

       430        440        450        460        470        480 
DDFSSPNITN QFGVRPSPAN FITPGKQPLS SMCPVIIVGE DGQVRMVVGA SGGTQITTST 

       490        500        510        520        530        540 
ALAIIHSLWF GYDVKRAVEE PRLHNQLLPN TTTLEKGIDQ AVAAALKTRH HYIQDASTFI 

       550        560 
GVVQAIVRTP SGWAAASDSR KGGEPAGY

« Hide

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References

[1]"Cloning and expression of gamma-glutamyl transpeptidase from isolated porcine brain capillaries."
Papandrikopoulou A., Frey A., Gassen H.G.
Eur. J. Biochem. 183:693-698(1989) [PubMed: 2476308] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
Tissue: Brain capillary.
[2]"Sequences and genetic variations of fourty-four porcine coat color related genes."
Okumura N., Matsumoto T., Hamasima N., Uenishi H., Ogawa T., Komatsuda A., Fukudome N., Ide H., Suzuki A., Kojima C., Awata T.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species."
Chikhi N., Holic N., Guellaen G., Laperche Y.
Comp. Biochem. Physiol. 122B:367-380(1999) [PubMed: 10392451] [Abstract]
Cited for: GENE ORGANIZATION, ALTERNATIVE PROMOTER USAGE.

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Cross-references

Sequence databases

Z46922 mRNA. Translation: CAA87031.1.
X16533 Genomic DNA. Translation: CAA34536.1.
AB271954 mRNA. Translation: BAF62329.1.
PIRS05532.
RefSeqNP_999195.1.
UniGeneSsc.116
Ssc.56552

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPST03.006.

Genome annotation databases

GeneID397095.
KEGGssc:397095.

Organism-specific databases

CTD397095.

Phylogenomic databases

HOVERGENP20735.

Enzyme and pathway databases

BRENDA2.3.2.2. 249.

Family and domain databases

InterProIPR000101. GGT_peptidase.
[Graphical view]
PANTHERPTHR11686. GGT_peptidase. 1 hit.
PfamPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
TIGRFAMsTIGR00066. g_glut_trans. 1 hit.
PROSITEPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGGT1_PIG
AccessionPrimary (citable) accession number: P20735
Secondary accession number(s): A5A784
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 13, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents