Gamma-glutamyltranspeptidase 1 precursor

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Q60928 (GGT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Gamma-glutamyltranspeptidase 1
Short name=GGT 1
EC=2.3.2.2

Alternative name(s):
Gamma-glutamyltransferase 1
CD_antigen=CD224

Cleaved into the following 2 chains:

Gamma-glutamyltranspeptidase 1 heavy chain
Gamma-glutamyltranspeptidase 1 light chain

Gene names

Name:	Ggt1
Synonyms:	Ggt, Ggtp

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. Indirectly regulates mutiple aspects of skeletal biology. Ref.5
Catalytic activity	(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid. Glutathione + H₂O = L-cysteinylglycine + L-glutamate.
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.
Involvement in disease	Note=Defects in Ggt1 are a cause of glutathionuria, severe growth failure, reduced life spans and infertility. Ggt1-deficient mice have multiple metabolic abnormalities and are dwarf. Some abnormalities can be ameliorated by N-acetylcysteine treatment. Ref.4 Ref.5
Sequence similarities	Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Cellular component	Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to mechanical stimulus Traceable author statement. Source: UniProtKB cysteine biosynthetic process Inferred from mutant phenotype. Source: UniProtKB glutathione biosynthetic process Inferred from mutant phenotype. Source: UniProtKB lung connective tissue development Traceable author statement. Source: UniProtKB regulation of immune system process Inferred from mutant phenotype. Source: UniProtKB regulation of inflammatory response Inferred from mutant phenotype. Source: UniProtKB spermatogenesis Inferred from mutant phenotype Ref.4. Source: MGI
Cellular component	integral to plasma membrane Traceable author statement Ref.1. Source: MGI
Molecular function	gamma-glutamyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 379

379

Gamma-glutamyltranspeptidase 1 heavy chain

PRO_0000011060

Chain

380 – 568

189

Gamma-glutamyltranspeptidase 1 light chain

PRO_0000011061

Regions

Topological domain

1 – 4

Cytoplasmic Potential

Transmembrane

5 – 26

Helical; Signal-anchor for type II membrane protein; Probable

Topological domain

27 – 568

542

Extracellular Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

114

N-linked (GlcNAc...) Ref.6

Glycosylation

119

N-linked (GlcNAc...) Potential

Glycosylation

120

N-linked (GlcNAc...) Ref.6

Glycosylation

229

N-linked (GlcNAc...) Ref.6

Glycosylation

343

N-linked (GlcNAc...) Potential

Glycosylation

510

N-linked (GlcNAc...) Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

Q60928 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 293C6E224FDC0766
Show »

FASTA

568

61,563

        10         20         30         40         50         60 
MKNRFLVLGL VAVVLVFVII GLCIWLPYTS GKPDHVYSRA AVATDAKRCS EIGRDILQEG 

        70         80         90        100        110        120 
GSVVDAAIAS LLCMGLMNAH SMGIGGGLFF TIYNSTTGKV EVINAREVAP RLANTTMFNN 

       130        140        150        160        170        180 
SKDSEEGGLS VAVPGEIRGY ELAHQRHGRL PWARLFQPSI QLARHGFPVG KGLAIALDKK 

       190        200        210        220        230        240 
RDVIEKTPAL CEVFCRQGKV LQEGETVTMP KLADTLQILA QEGAKAFYNG SLTAQIVKDI 

       250        260        270        280        290        300 
QEAGGIMTVE DLNNYRAELI EHPMSIGLGD ATLYVPSAPL SGPVLILILN ILKGYNFSPK 

       310        320        330        340        350        360 
SVATPEQKAL TYHRIVEAFR FAYAKRTMLG DPKFVDVSQV IRNMSSEFYA TQLRARITDE 

       370        380        390        400        410        420 
TTHPAAYYEP EFYLQDDGGT AHLSAVSEDG SAVAATSTIN LYFGSKVLSR VSGILFNDEM 

       430        440        450        460        470        480 
DDFSSPNFIN QFRVAPSPAN FIKPGKQPLS SMCPSIILDK DGQVRMVVGA SGGTQITTSV 

       490        500        510        520        530        540 
ALAIINSLWF GYDVKRAVEE PRLHNQLLPN TTTVEKDIDQ VVTAGLKIRH HHTEVTPTFI 

       550        560 
AVVQAVVRAS GGWAAASDSR KGGEPAGY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNA and genomic structure of the mouse gamma-glutamyl transpeptidase-encoding gene." Shi Z.Z., Habib G.M., Lebovitz R.M., Lieberman M.W. Gene 167:233-237(1995) [PubMed: 8566783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Kidney.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Mammary tumor.
[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.
[4]	"Mice with genetic gamma-glutamyl transpeptidase deficiency exhibit glutathionuria, severe growth failure, reduced life spans, and infertility." Harding C.O., Williams P., Wagner E., Chang D.S., Wild K., Colwell R.E., Wolff J.A. J. Biol. Chem. 272:12560-12567(1997) [PubMed: 9139708] [Abstract] Cited for: DISEASE.
[5]	"Reversible skeletal abnormalities in gamma-glutamyl transpeptidase-deficient mice." Levasseur R., Barrios R., Elefteriou F., Glass D.A. II, Lieberman M.W., Karsenty G. Endocrinology 144:2761-2764(2003) [PubMed: 12810527] [Abstract] Cited for: DISEASE, FUNCTION.
[6]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114; ASN-120; ASN-229 AND ASN-510, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U30509 mRNA. Translation: AAA97395.1. BC012969 mRNA. Translation: AAH12969.1.
IPI	IPI00122522.
PIR	JC4570.
RefSeq	NP_032142.1. NM_008116.2.
UniGene	Mm.4559.
3D structure databases
ProteinModelPortal	Q60928.
SMR	Q60928. Positions 34-568.
ModBase	Search...
Protein-protein interaction databases
STRING	Q60928.
Protein family/group databases
MEROPS	T03.006.
Proteomic databases
PRIDE	Q60928.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000006508; ENSMUSP00000006508; ENSMUSG00000006345. ENSMUST00000134503; ENSMUSP00000121312; ENSMUSG00000006345.
GeneID	14598.
KEGG	mmu:14598.
NMPDR	fig\|10090.3.peg.13864.
Organism-specific databases
CTD	2678.
MGI	MGI:95706. Ggt1.
Phylogenomic databases
GeneTree	ENSGT00550000074591.
HOGENOM	HBG738311.
HOVERGEN	HBG005835.
InParanoid	Q60928.
OMA	VRNMSSE.
PhylomeDB	Q60928.
Enzyme and pathway databases
BRENDA	2.3.2.2. 3474.
Gene expression databases
ArrayExpress	Q60928.
Bgee	Q60928.
CleanEx	MM_GGT1.
Genevestigator	Q60928.
GermOnline	ENSMUSG00000006345. Mus musculus.
Family and domain databases
InterPro	IPR000101. GGT_peptidase. [Graphical view]
KO	K00681.
PANTHER	PTHR11686. GGT_peptidase. 1 hit.
Pfam	PF01019. G_glu_transpept. 1 hit. [Graphical view]
PRINTS	PR01210. GGTRANSPTASE.
TIGRFAMs	TIGR00066. G_glut_trans. 1 hit.
PROSITE	PS00462. G_GLU_TRANSPEPTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	286360.
SOURCE	Search...

Entry information

Entry name

GGT1_MOUSE

Accession

Primary (citable) accession number: Q60928

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	November 16, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents