P07314 (GGT1_RAT) Reviewed, UniProtKB/Swiss-Prot

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:

1. Gamma-glutamyltranspeptidase 1 heavy chain
2. Gamma-glutamyltranspeptidase 1 light chain

Gene names

Name:	Ggt1
Synonyms:	Ggt

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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.
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.
Subcellular location	Membrane; Single-pass type II membrane protein.
Tissue specificity	Detected in adult kidney and mammary gland, and in fetal liver.
Post-translational modification	N-glycosylated on both chains; contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans. Ref.12 Ref.13 Ref.14 O-glycosylated; close to the membrane anchor on the heavy chain and on the light chain. The sugar moieties are localized to the stretch Thr-28 to Ser-30. Contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans. Ref.12 Ref.13 Ref.14
Sequence similarities	Belongs to the gamma-glutamyltransferase family.
Sequence caution	The sequence CAA27224.1 differs from that shown. Reason: Frameshift at positions 66 and 134.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Cellular component	Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Sialic acid
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	aging Inferred from expression pattern. Source: RGD cellular response to oxidative stress Inferred from expression pattern. Source: RGD glutathione biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW peptide modification Inferred from direct assay. Source: RGD response to estradiol stimulus Inferred from expression pattern. Source: RGD response to lipopolysaccharide Inferred from expression pattern. Source: RGD response to tumor necrosis factor Inferred from expression pattern. Source: RGD
Cellular component	extracellular space Inferred from direct assay. Source: RGD integral to plasma membrane Traceable author statement. Source: RGD
Molecular function	gamma-glutamyltransferase activity Inferred from direct assay. Source: RGD
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_0000011064
	Chain	380 – 568	189	Gamma-glutamyltranspeptidase 1 light chain		PRO_0000011065
Regions
	Topological domain	1 – 4	4	Cytoplasmic Potential
	Transmembrane	5 – 26	22	Helical; Signal-anchor for type II membrane protein; Probable
	Topological domain	27 – 568	542	Extracellular Potential
Amino acid modifications
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	114	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	229	1	N-linked (GlcNAc...) Potential
	Glycosylation	343	1	N-linked (GlcNAc...) Potential
	Glycosylation	427	1	N-linked (GlcNAc...) Potential
	Glycosylation	510	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	9	1	G → A in AAA41217. Ref.7
	Sequence conflict	39	1	R → K in AAA57295. Ref.2
	Sequence conflict	39	1	R → K in AAB59698. Ref.2
	Sequence conflict	111	1	R → K in AAB59698. Ref.2
	Sequence conflict	370	1	P → A in AAA57295. Ref.2
	Sequence conflict	370	1	P → A in AAB59698. Ref.2
	Sequence conflict	370	1	P → A in CAA27224. Ref.8
	Sequence conflict	397	1	S → M in CAA27224. Ref.8
	Sequence conflict	416	1	F → V in CAA27224. Ref.8
	Sequence conflict	444	1	P → L in AAA57295. Ref.2
	Sequence conflict	444	1	P → L in AAB59698. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P07314 [UniParc]. Last modified May 1, 2007. Version 4. Checksum: 24DC62A1DEEEA38C	FASTA	568	61,610
	10 20 30 40 50 60 MKNRFLVLGL VAVVLVFVII GLCIWLPTTS GKPDHVYSRA AVATDAKRCS EIGRDMLQEG 70 80 90 100 110 120 GSVVDAAIAS LLCMGLINAH SMGIGGGLFF TIYNSTTRKA EVINAREMAP RLANTSMFNN 130 140 150 160 170 180 SKDSEEGGLS VAVPGEIRGY ELAHQRHGRL PWARLFQPSI QLARHGFPVG KGLARALDKK 190 200 210 220 230 240 RDIIEKTPAL CEVFCRQGKV LQEGETVTMP KLADTLQILA QEGARAFYNG SLTAQIVKDI 250 260 270 280 290 300 QEAGGIMTVE DLNNYRAEVI EHPMSIGLGD STLYVPSAPL SGPVLILILN ILKGYNFSPK 310 320 330 340 350 360 SVATPEQKAL TYHRIVEAFR FAYAKRTMLG DPKFVDVSQV IRNMSSEFYA TQLRARITDE 370 380 390 400 410 420 TTHPTAYYEP EFYLPDDGGT AHLSVVSEDG SAVAATSTIN LYFGSKVLSR VSGILFNDEM 430 440 450 460 470 480 DDFSSPNFTN QFGVAPSPAN FIKPGKQPLS SMCPSIIVDK DGKVRMVVGA SGGTQITTSV 490 500 510 520 530 540 ALAIINSLWF GYDVKRAVEE PRLHNQLLPN TTTVEKNIDQ VVTAGLKTRH HHTEVTPDFI 550 560 AVVQAVVRTS GGWAAASDSR KGGEPAGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rat liver gamma glutamyl transpeptidase mRNA differs in the 5' untranslated sequence from the corresponding kidney mRNA." Griffiths S.A., Manson M.M. Cancer Lett. 46:69-74(1989) [PubMed: 2567622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Molecular cloning and nucleotide sequence of rat kidney gamma-glutamyl transpeptidase cDNA." Laperche Y., Bulle F., Aissani T., Chobert M.-N., Aggerbeck M., Hanoune J., Guellaen G. Proc. Natl. Acad. Sci. U.S.A. 83:937-941(1986) [PubMed: 2869484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-43 AND 380-388. Tissue: Kidney.
[3]	Erratum Laperche Y., Bulle F., Aissani T., Chobert M.-N., Aggerbeck M., Hanoune J., Guellaen G. Proc. Natl. Acad. Sci. U.S.A. 86:3159-3159(1989) Cited for: SEQUENCE REVISION TO 66-135.
[4]	"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]. Tissue: Testis.
[5]	"Studies on the structure of gamma-glutamyltranspeptidase. III. Evidence that the amino terminus of the heavy subunit is the membrane binding segment." Matsuda Y., Tsuji A., Katunuma N. J. Biochem. 93:1427-1433(1983) [PubMed: 6136502] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21.
[6]	"Functional characterization of the rat gamma-glutamyl transpeptidase promoter that is expressed and regulated in the liver and hepatoma cells." Brouillet A., Darbouy M., Okamoto T., Chobert M.-N., Lahuna O., Garlatti M., Goodspeed D.C., Laperche Y. J. Biol. Chem. 269:14878-14884(1994) [PubMed: 7910821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-18. Strain: Wistar. Tissue: Liver.
[7]	"Organization of the 5' end of the rat gamma-glutamyl transpeptidase gene: structure of a promoter active in the kidney." Kurauchi O., Lahuna O., Darbouy M., Aggerbeck M., Chobert M.-N., Laperche Y. Biochemistry 30:1618-1623(1991) [PubMed: 1671556] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. Tissue: Kidney.
[8]	"Characterization and sequence of a cDNA clone of gamma-glutamyltranspeptidase." Coloma J., Pitot H.C. Nucleic Acids Res. 14:1393-1403(1986) [PubMed: 2869471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-568. Tissue: Kidney.
[9]	"The primary structure of human gamma-glutamyl transpeptidase." Sakamuro D., Yamazoe M., Matsuda Y., Kangawa K., Taniguchi N., Matsuo H., Yoshikawa H., Ogasawara N. Gene 73:1-9(1988) [PubMed: 2907498] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-136.
[10]	"Renal gamma-glutamyl transpeptidases: structural and immunological studies." Tate S.S., Khadse V., Wellner D. Arch. Biochem. Biophys. 262:397-408(1988) [PubMed: 2896486] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-47 AND 380-402. Tissue: Kidney.
[11]	"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.
[12]	"Subunit structure and isozymic forms of gamma-glutamyl transpeptidase." Tate S.S., Meister A. Proc. Natl. Acad. Sci. U.S.A. 73:2599-2603(1976) [PubMed: 8776] [Abstract] Cited for: GLYCOSYLATION, SIALIC ACID CONTENT.
[13]	"In vitro translation and processing of rat kidney gamma-glutamyl transpeptidase." Nash B., Tate S.S. J. Biol. Chem. 259:678-685(1984) [PubMed: 6142889] [Abstract] Cited for: GLYCOSYLATION.
[14]	"O-linked glycosylation of rat renal gamma-glutamyltranspeptidase adjacent to its membrane anchor domain." Blochberger T.C., Sabatine J.M., Lee Y.C., Hughey R.P. J. Biol. Chem. 264:20718-20722(1989) [PubMed: 2573604] [Abstract] Cited for: GLYCOSYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15443 mRNA. Translation: CAA33483.1. M33821 mRNA. Translation: AAA57295.1. Sequence problems. M33822 mRNA. Translation: AAB59698.1. BC078768 mRNA. Translation: AAH78768.1. L29167 mRNA. Translation: AAA41218.1. M57672 Genomic DNA. Translation: AAA41217.1. X03518 mRNA. Translation: CAA27224.1. Frameshift.
IPI	IPI00206254.
PIR	A05225.
RefSeq	NP_446292.2. NM_053840.2.
UniGene	Rn.10010.
3D structure databases
ProteinModelPortal	P07314.
ModBase	Search...
Protein family/group databases
MEROPS	T03.006.
PTM databases
GlycoSuiteDB	P07314.
Proteomic databases
PRIDE	P07314.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	116568.
KEGG	rno:116568.
Organism-specific databases
CTD	2678.
RGD	2683. Ggt1.
Phylogenomic databases
eggNOG	roNOG06339.
HOVERGEN	HBG005835.
PhylomeDB	P07314.
Gene expression databases
Genevestigator	P07314.
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	619251.

Entry information

Entry name

GGT1_RAT

Accession

Primary (citable) accession number: P07314
Secondary accession number(s): Q63217, Q63218, Q6AZ32

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	May 1, 2007
Last modified:	November 16, 2011
This is version 111 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program