P43616 (DUG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cys-Gly metallodipeptidase DUG1
EC=3.4.13.-

Alternative name(s):
Deficient in utilization of glutathione protein 1
GSH degradosomal complex subunit DUG1

Gene names

Name:	DUG1
Ordered Locus Names:	YFR044C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2-DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides. Ref.8 Ref.10
Cofactor	Zinc or manganese. Ref.10
Subunit structure	Homodimer. Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3. Ref.8 Ref.10
Subcellular location	Cytoplasm Ref.6 Ref.8.
Disruption phenotype	Accumulation of Cys-Gly dipeptide and enhanced GSH toxicity. Ref.10
Miscellaneous	Present with 22300 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the peptidase M20A family.
Biophysicochemical properties	Kinetic parameters: KM=0.4 mM for Cys-Gly (at pH 8.0 and in the presence of 20 µM manganese ions) KM=0.8 mM for Cys-Gly (at pH 8.0 and in the presence of 200 µM zinc ions)

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione catabolic process Inferred from mutant phenotype Ref.8. Source: SGD proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from direct assay Ref.6PubMed 16823961. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallodipeptidase activity Inferred from direct assay Ref.10. Source: SGD omega peptidase activity Inferred from genetic interaction Ref.8. Source: SGD tripeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-5137,EBI-5137

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	Cys-Gly metallodipeptidase DUG1		PRO_0000185275
Sites
	Active site	104	1	By similarity
	Active site	171	1	Proton acceptor By similarity
	Metal binding	102	1	Zinc 2 By similarity
	Metal binding	137	1	Zinc 1 By similarity
	Metal binding	137	1	Zinc 2 By similarity
	Metal binding	172	1	Zinc 1 By similarity
	Metal binding	200	1	Zinc 2 By similarity
	Metal binding	450	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	451	1	Phosphoserine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P43616 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 3E53773A945F5EBC	FASTA	481	52,871
	10 20 30 40 50 60 MSHSLTSVFQ KIDSLKPQFF SRLTKAIQIP AVSSDESLRS KVFDKAKFIS EQLSQSGFHD 70 80 90 100 110 120 IKMVDLGIQP PPISTPNLSL PPVILSRFGS DPSKKTVLVY GHYDVQPAQL EDGWDTEPFK 130 140 150 160 170 180 LVIDEAKGIM KGRGVTDDTG PLLSWINVVD AFKASGQEFP VNLVTCFEGM EESGSLKLDE 190 200 210 220 230 240 LIKKEANGYF KGVDAVCISD NYWLGTKKPV LTYGLRGCNY YQTIIEGPSA DLHSGIFGGV 250 260 270 280 290 300 VAEPMIDLMQ VLGSLVDSKG KILIDGIDEM VAPLTEKEKA LYKDIEFSVE ELNAATGSKT 310 320 330 340 350 360 SLYDKKEDIL MHRWRYPSLS IHGVEGAFSA QGAKTVIPAK VFGKFSIRTV PDMDSEKLTS 370 380 390 400 410 420 LVQKHCDAKF KSLNSPNKCR TELIHDGAYW VSDPFNAQFT AAKKATKLVY GVDPDFTREG 430 440 450 460 470 480 GSIPITLTFQ DALNTSVLLL PMGRGDDGAH SINEKLDISN FVGGMKTMAA YLQYYSESPE N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae." Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y. Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels." Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M. Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae." Ganguli D., Kumar C., Bachhawat A.K. Genetics 175:1137-1151(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE GSH DEGRADOSOMAL COMPLEX, SUBCELLULAR LOCATION.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, MASS SPECTROMETRY.
[10]	"Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases." Kaur H., Kumar C., Junot C., Toledano M.B., Bachhawat A.K. J. Biol. Chem. 284:14493-14502(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, FUNCTION, COFACTOR, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50617 Genomic DNA. Translation: BAA09283.1. AY692702 Genomic DNA. Translation: AAT92721.1. BK006940 Genomic DNA. Translation: DAA12487.1.
PIR	S56299.
RefSeq	NP_116702.1. NM_001180009.1.
3D structure databases
ProteinModelPortal	P43616.
SMR	P43616. Positions 4-477.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6492N.
IntAct	P43616. 3 interactions.
MINT	MINT-640305.
STRING	4932.YFR044C.
Protein family/group databases
MEROPS	M20.017.
Proteomic databases
PaxDb	P43616.
PeptideAtlas	P43616.
PRIDE	P43616.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YFR044C; YFR044C; YFR044C.
GeneID	850605.
KEGG	sce:YFR044C.
Organism-specific databases
CYGD	YFR044c.
SGD	S000001940. DUG1.
Phylogenomic databases
eggNOG	COG0624.
GeneTree	ENSGT00390000009682.
HOGENOM	HOG000216709.
KO	K15428.
OMA	DYALVCD.
OrthoDB	EOG40ZV66.
Enzyme and pathway databases
BioCyc	YEAST:G3O-30491-MONOMER. YEAST:MONOMER3O-4.
SABIO-RK	P43616.
Gene expression databases
Genevestigator	P43616.
GermOnline	YFR044C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.70.360. 1 hit.
InterPro	IPR017153. GSH_degradosome_DUG1. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. False negative. PS00759. ARGE_DAPE_CPG2_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	966481.

Entry information

Entry name

DUG1_YEAST

Accession

Primary (citable) accession number: P43616
Secondary accession number(s): D6VTS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program