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

Glutathione hydrolase 1 proenzyme

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)DescriptionActionsGraphical viewLength
Binding sitei106GlutamateBy similarity1
Active sitei380NucleophileBy similarity1
Binding sitei398GlutamateBy similarity1
Binding sitei419GlutamateBy similarity1

GO - Molecular functioni

  • glutathione hydrolase activity Source: UniProtKB
  • hypoglycin A gamma-glutamyl transpeptidase activity Source: UniProtKB-EC

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Hydrolase, Protease, Transferase
Biological processGlutathione biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00204.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione hydrolase 1 proenzyme (EC:3.4.19.13By similarity)
Alternative name(s):
Gamma-glutamyltransferase 1
Gamma-glutamyltranspeptidase 1 (EC:2.3.2.2By similarity)
Short name:
GGT 1
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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4CytoplasmicSequence analysis4
Transmembranei5 – 26Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST22
Topological domaini27 – 568ExtracellularSequence analysisAdd BLAST542

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000110621 – 379Glutathione hydrolase 1 heavy chainAdd BLAST379
ChainiPRO_0000011063380 – 568Glutathione hydrolase 1 light chainAdd BLAST189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 73By similarity
Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi191 ↔ 195By similarity
Glycosylationi229N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi296N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi336N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi343N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi427N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi510N-linked (GlcNAc...) asparagineSequence analysis1

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.
PRIDEiP20735.

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.
SMRiP20735.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni450 – 451Glutamate bindingBy similarity2

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

InterProiView protein in InterPro
IPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiView protein in Pfam
PF01019. G_glu_transpept. 1 hit.
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiView protein in PROSITE
PS00462. G_GLU_TRANSPEPTIDASE. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiGGT1_PIG
AccessioniPrimary (citable) accession number: P20735
Secondary accession number(s): A5A784
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: September 27, 2017
This is version 114 of the entry and version 1 of the sequence. See 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