O14194 (GGT2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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

Gene names

Name:	ggt2
ORF Names:	SPAC56E4.06c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [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	Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation By similarity. Ref.1
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	Vacuole membrane; Single-pass type II membrane protein Potential Ref.4.
Induction	Induced upon nitrogen starvation and oxidative stress. Ref.3
Sequence similarities	Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
Cellular component	Membrane Vacuole
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to oxidative stress Traceable author statement. Source: GeneDB_Spombe
Cellular component	fungal-type vacuole Inferred from direct assay. Source: GeneDB_Spombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW vacuolar membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	gamma-glutamyltransferase activity 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	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	64 – 611	548	Lumenal 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 [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: 972 / ATCC 24843.
[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.
[4]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY359853 Genomic DNA. Translation: AAQ57121.1. CU329670 Genomic DNA. Translation: CAB16397.1.
PIR	T38908.
RefSeq	NP_593273.1. NM_001018670.1.
3D structure databases
ProteinModelPortal	O14194.
ModBase	Search...
Protein-protein interaction databases
STRING	O14194.
Protein family/group databases
MEROPS	T03.011.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC56E4.06c.1; SPAC56E4.06c.1:pep; SPAC56E4.06c.
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
eggNOG	fuNOG04439.
GeneTree	EFGT00050000000262.
HOGENOM	HBG738311.
OMA	VRNMSSE.
OrthoDB	EOG4GTPN8.
Enzyme and pathway databases
BRENDA	2.3.2.2. 5615.
Gene expression databases
ArrayExpress	O14194.
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. 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:	December 14, 2011
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program