Q9US04 (GGT1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-glutamyltranspeptidase 1
EC=2.3.2.2

Alternative name(s):
Gamma-glutamyltransferase 1

Cleaved into the following 2 chains:

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

Gene names

Name:	ggt1
ORF Names:	SPAC664.09

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	630 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. 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	Endoplasmic reticulum membrane; Single-pass type II membrane protein Potential Ref.4.
Induction	Induced upon nitrogen starvation. Also induced by non-fermentable carbon sources such as glycerol, acetate and ethanol in a pap1-independent manner. Ref.3
Sequence similarities	Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Traceable author statement. Source: GeneDB_Spombe cellular response to nitrogen starvation Inferred from direct assay. Source: GeneDB_Spombe glutathione catabolic process Inferred by curator. Source: GeneDB_Spombe
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	gamma-glutamyltransferase activity Inferred from direct assay. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 440	440	Gamma-glutamyltranspeptidase 1 heavy chain By similarity		PRO_0000247898
	Chain	441 – 630	190	Gamma-glutamyltranspeptidase 1 light chain By similarity		PRO_0000247899
Regions
	Topological domain	1 – 49	49	Cytoplasmic Potential
	Transmembrane	50 – 70	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	71 – 630	560	Lumenal Potential
Amino acid modifications
	Glycosylation	156	1	N-linked (GlcNAc...) Potential
	Glycosylation	180	1	N-linked (GlcNAc...) Potential
	Glycosylation	315	1	N-linked (GlcNAc...) Potential
	Glycosylation	397	1	N-linked (GlcNAc...) Potential
	Glycosylation	417	1	N-linked (GlcNAc...) Potential
	Glycosylation	612	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9US04 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E85E83D21AC24B20	FASTA	630	68,722
	10 20 30 40 50 60 MGINTSSAQS SGAASIARSS VNVKSGNRHL SSNKKSATSA LEERASRPSI LVTFLVLAGT 70 80 90 100 110 120 ILSLYIWPIL SPDLFFANQR CSFKYKNKGS QRVVVEGKNG VVATEEETCS QIGVGILKAG 130 140 150 160 170 180 GNAVDAAIAS GICIGAVNSF SSGIGGGGFM LIRHPNGTAH SLNFRETAPA GASKNMFHGN 190 200 210 220 230 240 STLSQVGGLS VAVPGEIAGY ERAWKMYGSL PWHKLFEPTI RLMRDGMPMP KELASRIRRP 250 260 270 280 290 300 EFSYFKTHPD WSKIFAPEGV FLHVGEKFYR PALASTLEEI AKFGPEVFYT GKIAERLVKF 310 320 330 340 350 360 VQQQGGILTM EDMANFSVVV EEPIYGNFYD REVITCGSPC SGEALILGLN VLSKVDLSEG 370 380 390 400 410 420 TSILGCEMTD IGVHHLIETM KWMSAGRTVL ADPTFYNNTD HVEQLLSLEY ADEIRNNISN 430 440 450 460 470 480 ERTFDFTHYK AEYDFPNDHG TTHLSVIDKD NMAVGLTASI NLMFGSQLLE PETGIILNDH 490 500 510 520 530 540 MDDFASPGIV NAFGLSPSPY NFIAPGKRPQ SSAVPTILVY NGEVEMVLGG SGGSRIVTAV 550 560 570 580 590 600 LDTIIKKYKW GKSLLESVES PRFHHQLMPN IVYIDETVEI EVLRALEKFG HIVDLIPVQY 610 620 630 PFSEIQAVFR TNGTLYGLSD SRKQAVAAAY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and regulation of the gamma-glutamyl transpeptidase gene from the fission yeast Schizosaccharomyces pombe." Park H.-J., Lim H.-W., Kim K., Kim I.-H., Park E.-H., Lim C.-J. Can. J. Microbiol. 50:61-66(2004) [PubMed: 15052323] [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 Schizosaccharomyces pombe gene encoding gamma-glutamyl transpeptidase I is regulated by non-fermentable carbon sources and nitrogen starvation." Kim H.-G., Park H.-J., Kang H.-J., Lim H.-W., Kim K., Park E.-H., Ahn K., Lim C.-J. J. Microbiol. 43:44-48(2005) [PubMed: 15765057] [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	AF535133 Genomic DNA. Translation: AAN01227.1. CU329670 Genomic DNA. Translation: CAB65810.1.
PIR	T50239.
RefSeq	NP_593457.1. NM_001018890.1.
3D structure databases
ProteinModelPortal	Q9US04.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9US04.
Protein family/group databases
MEROPS	T03.011.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC664.09.1; SPAC664.09.1:pep; SPAC664.09.
GeneID	2543536.
GenomeReviews	Gene locus ggt1 in contig CU329670_GR.
KEGG	spo:SPAC664.09.
NMPDR	fig|4896.1.peg.3427.
Organism-specific databases
GeneDB_Spombe	SPAC664.09.
Phylogenomic databases
eggNOG	fuNOG04439.
GeneTree	EFGT00050000000262.
HOGENOM	HBG738311.
OMA	HAYGQRT.
OrthoDB	EOG4GTPN8.
Gene expression databases
ArrayExpress	Q9US04.
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

GGT1_SCHPO

Accession

Primary (citable) accession number: Q9US04

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program