Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Gamma-glutamyltranspeptidase 1

Gene

GGT1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism.By similarity

Catalytic activityi

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

Enzyme regulationi

Activated by autocatalytic cleavage.By similarity

Pathwayi: glutathione metabolism

This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061GlutamateBy similarity
Active sitei380 – 3801NucleophileBy similarity
Binding sitei398 – 3981GlutamateBy similarity
Binding sitei419 – 4191GlutamateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Protease, Transferase

Keywords - Biological processi

Glutathione biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00204.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyltranspeptidase 1 (EC:2.3.2.2By similarity)
Short name:
GGT 1
Alternative name(s):
Gamma-glutamyltransferase 1
Glutathione hydrolase 1 (EC:3.4.19.13By similarity)
Leukotriene-C4 hydrolase (EC:3.4.19.14By similarity)
CD_antigen: CD224
Cleaved into the following 2 chains:
Gene namesi
Name:GGT1
Synonyms:GGT
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Cell membrane By similarity; Single-pass type II membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2622Helical; Signal-anchor for type II membrane proteinCuratedAdd
BLAST
Topological domaini27 – 568542ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Gamma-glutamyltranspeptidase 1 heavy chainPRO_0000011062Add
BLAST
Chaini380 – 568189Gamma-glutamyltranspeptidase 1 light chainPRO_0000011063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 73By similarity
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi191 ↔ 195By similarity
Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence analysis
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence analysis
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence analysis
Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence analysis
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated on both chains.By similarity
Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP20735.
PeptideAtlasiP20735.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028318.

Structurei

3D structure databases

ProteinModelPortaliP20735.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG2410. Eukaryota.
COG0405. LUCA.
HOGENOMiHOG000175620.
HOVERGENiHBG005835.
InParanoidiP20735.
KOiK18592.

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.

P20735-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRYLLLAL AAVALVLLIL GLCLWLPSNS KPHNHVYPRA AVAADALRCS
60 70 80 90 100
EIGRDTLRDG GSAVDAAIAA LLCVGLMNAH SMGIGGGLFL TIYNSTTRKA
110 120 130 140 150
EIINAREVAP RLASASMFNS SEQSEEGGLS VAVPGEIRGY ELAHQRHGRL
160 170 180 190 200
PWARLFQPSI ELASQGFPVG KGLAAALERS QDAIKRHPAL CEVFCRNGNV
210 220 230 240 250
LREGDLVTMP RLAKTYETLA VEGAQAFYNG SLTAQIVKDI QEAGGIVTAE
260 270 280 290 300
DLNNYRAELI EQPLRISLGD AQLYAPNAPL SGPVLALILN ILKGYNFSRA
310 320 330 340 350
SVETPEQKGL TYHRIVEAFR FAYAKRTLLG DPKFVNVTEV VRNMSSEFFA
360 370 380 390 400
DQLRARISDT TTHPDSYYEP EFYTPDDAGT AHLSVVSDDG SAVSATSTIN
410 420 430 440 450
LYFGSKVRSR ISGILFNDEM DDFSSPNITN QFGVRPSPAN FITPGKQPLS
460 470 480 490 500
SMCPVIIVGE DGQVRMVVGA SGGTQITTST ALAIIHSLWF GYDVKRAVEE
510 520 530 540 550
PRLHNQLLPN TTTLEKGIDQ AVAAALKTRH HYIQDASTFI GVVQAIVRTP
560
SGWAAASDSR KGGEPAGY
Length:568
Mass (Da):61,316
Last modified:February 1, 1991 - v1
Checksum:iEB2D1896B1229487
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46922 mRNA. Translation: CAA87031.1.
X16533 Genomic DNA. Translation: CAA34536.1.
AB271954 mRNA. Translation: BAF62329.1.
PIRiS05532.
RefSeqiNP_999195.1. NM_214030.1.
UniGeneiSsc.116.

Genome annotation databases

GeneIDi397095.
KEGGissc:397095.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46922 mRNA. Translation: CAA87031.1.
X16533 Genomic DNA. Translation: CAA34536.1.
AB271954 mRNA. Translation: BAF62329.1.
PIRiS05532.
RefSeqiNP_999195.1. NM_214030.1.
UniGeneiSsc.116.

3D structure databases

ProteinModelPortaliP20735.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028318.

Proteomic databases

PaxDbiP20735.
PeptideAtlasiP20735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397095.
KEGGissc:397095.

Organism-specific databases

CTDi2678.

Phylogenomic databases

eggNOGiKOG2410. Eukaryota.
COG0405. LUCA.
HOGENOMiHOG000175620.
HOVERGENiHBG005835.
InParanoidiP20735.
KOiK18592.

Enzyme and pathway databases

UniPathwayiUPA00204.

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]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: GENE ORGANIZATION, ALTERNATIVE PROMOTER USAGE.

Entry informationi

Entry nameiGGT1_PIG
AccessioniPrimary (citable) accession number: P20735
Secondary accession number(s): A5A784
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 110 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.