Reviewed, UniProtKB/Swiss-Prot O14194 (GGT2_SCHPO)

Names and origin

Protein names

Recommended name:
    Gamma-glutamyltranspeptidase 2
    EC=2.3.2.2
Alternative name(s):
    Gamma-glutamyltransferase 2
Cleaved into the following 2 chains:
    1- Recommended name:
            Gamma-glutamyltranspeptidase 2 heavy chain
    2- Recommended name:
            Gamma-glutamyltranspeptidase 2 light chain

Gene names

Name:	ggt2
ORF Names:	SPAC56E4.06c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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. Ref.1
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 Potential.
Induction	Induced upon nitrogen starvation and oxidative stress. Ref.3
Sequence similarities	Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Cellular component	Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to oxidative stress Ref.1 Ref.3 Traceable author statement. Source: GeneDB_SPombe glutathione biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	fungal-type vacuole Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW gamma-glutamyltransferase activity Inferred from electronic annotation. Source: EC protein-glutamine gamma-glutamyltransferase activity Ref.1 Traceable author statement. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	Gamma-glutamyltranspeptidase 2 heavy chain By similarity		PRO_0000247900
	Chain	420 – 611	192	Gamma-glutamyltranspeptidase 2 light chain By similarity		PRO_0000247901
Regions
	Topological domain	1 – 42	42	Cytoplasmic Potential
	Transmembrane	43 – 63	21	Signal-anchor for type II membrane protein Potential
	Topological domain	64 – 611	548	Extracellular Potential
Amino acid modifications
	Glycosylation	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	153	1	N-linked (GlcNAc...) Potential
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	396	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O14194-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 5A74721D93CC8C26	FASTA	611	67,825
	10 20 30 40 50 60 MSPTDTTPLL YSWDDQSRHQ DPDWHKLRNY HGAWYRRISR RRFSQFIFAF GLMTLFVLVY 70 80 90 100 110 120 SISSNLHTPT QFTGHKVRGR RGAVASEVPV CSDIGVSMLA DGGNAVDAAI ASTFCIGVVN 130 140 150 160 170 180 FFSSGIGGGG FMLIKHPNET AQSLTFREIA PGNVSKHMFD KNPMLAQVGP LSIAIPGELA 190 200 210 220 230 240 GLYEAWKSHG LLDWSKLLEP NVKLAREGFP VTRAMERVLK LPEMAHLLKD PIWQPILMPN 250 260 270 280 290 300 GKVLRAGDKM FRPAYAKTLE IIANKGIEPF YRGELTNSMV KFIQDNGGIV TVEDFGNYST 310 320 330 340 350 360 VFADALHTSY RGHDVYTCTL PTSGPALIEG LNILDGYPLN TPSLAFPKRL HLEVEAMKWL 370 380 390 400 410 420 SAGRTQFGDP DFLPLDHLDV VSKLLSKEFA SQIRNNISLS KTYPWEHYNP SYDLPISHGT 430 440 450 460 470 480 THVSTVDSNN LAVSITSTVN LLFGSQLMDP VTGVVFNDQM DDFSIPGASN AFNLSPSPWN 490 500 510 520 530 540 FIEPFKRPQS SSAPTILTDI NGDFEMALGA SGGSRIVTAV LDSIIKRIDM DYDIESMVAS 550 560 570 580 590 600 ARPHHQLLPD ILILESGFSK SVATRMKKYG HKVWRLKQHD TPLSQIQAVT RHHSEYYGMS 610 DPRKYGQAAA Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a second gene encoding gamma-glutamyl transpeptidase from Schizosaccharomyces pombe." Park H.-J., Moon J.-S., Kim H.-G., Kim I.-H., Kim K., Park E.-H., Lim C.-J. Can. J. Microbiol. 51:269-275(2005) [PubMed: 15920625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"The gene encoding gamma-glutamyl transpeptidase II in the fission yeast is regulated by oxidative and metabolic stress." Kang H.-J., Kim B.-C., Park E.-H., Ahn K., Lim C.-J. J. Biochem. Mol. Biol. 38:609-618(2005) [PubMed: 16202243] [Abstract] Cited for: INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY359853 Genomic DNA. Translation: AAQ57121.1. CU329670 Genomic DNA. Translation: CAB16397.1.
PIR	T38908.
RefSeq	NP_593273.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O14194.
Protein family/group databases
MEROPS	T03.011.
Genome annotation databases
GeneID	2543110.
GenomeReviews	Gene locus ggt2 in contig CU329670_GR.
KEGG	spo:SPAC56E4.06c.
NMPDR	fig|4896.1.peg.3243.
Organism-specific databases
GeneDB_Spombe	SPAC56E4.06c.
Phylogenomic databases
OMA	LELIANN.
Enzyme and pathway databases
BRENDA	2.3.2.2. 653.
Gene expression databases
ArrayExpress	O14194.
Family and domain databases
InterPro	IPR000101. GGT_peptidase. [Graphical view]
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GGT2_SCHPO

Accession

Primary (citable) accession number: O14194

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)