P25375 (PRTD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Saccharolysin
EC=3.4.24.37

Alternative name(s):
Oligopeptidase YSCD
Protease D
Proteinase yscD

Gene names

Name:	PRD1
Ordered Locus Names:	YCL057W
ORF Names:	YCL57W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	712 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Could be involved in late stage of protein degradation.
Catalytic activity	Cleavage of Pro-|-Phe and Ala-|-Ala bonds.
Cofactor	Binds 1 zinc ion By similarity.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 8910 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the peptidase M3 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	mitochondrial intermembrane space Inferred from direct assay Ref.1. Source: SGD
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from mutant phenotype Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 712	712	Saccharolysin		PRO_0000078156
Sites
	Active site	502	1	By similarity
	Metal binding	501	1	Zinc; catalytic By similarity
	Metal binding	505	1	Zinc; catalytic By similarity
	Metal binding	508	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	73	1	Phosphoserine Ref.6 Ref.7
	Modified residue	75	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	384	1	L → P in AAU09678. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P25375 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 340910B7FDAFBE37	FASTA	712	81,934
	10 20 30 40 50 60 MRLLLCKNWF ASPVISPLLY TRSLYSMANT TSFPIAPQAP PNWSFTPSDI SGKTNEIINN 70 80 90 100 110 120 SNNFYDSMSK VESPSVSNFV EPFMKFENEL GPIINQLTFL QHVSSDKEIR DASVNSSMKL 130 140 150 160 170 180 DELNIDLSLR HDIFLQFARV WQDVQSKADS VERETFKYVE KSYKDYIHSG LELDEGNRLK 190 200 210 220 230 240 IKEIKKKISV NSINFSKNLG EQKEYITFTK EQLEGVPDSI LTQFETIKSD KDSNETLYKV 250 260 270 280 290 300 TFKYPDIFPV MKLASSAQTR KQAFLADQNK VPENEAILLD TLKLRDELAS LLGYDTYANY 310 320 330 340 350 360 NLYDKMAEDS TTVMNFLNDL KDKLIPLGRK ELQVLQDMKA EDVKKLNQGA DPNYYIWDHR 370 380 390 400 410 420 YYDNKYLLEN FNVDLEKISE YFPLEATITG MLEIYETLFN LKFIETKDSQ NKSVWHDDVK 430 440 450 460 470 480 QIAVWNMDDP KSPNFVGWIY FDLHPRDGKY GHAANFGLSS SFMIDDTTRS YPVTALVCNF 490 500 510 520 530 540 SKSTKDKPSL LKHNEIVTFF HELGHGIHDL VGQNKESRFN GPGSVPWDFV EAPSQMLEFW 550 560 570 580 590 600 TWNKNELINL SSHYKTGEKI PESLINSLIK TKHVNGALFT LRQLHFGLFD MKVHTCKDLQ 610 620 630 640 650 660 NLSICDTWNQ LRQDISLISN GGTLSKGYDS FGHIMSDSYS AGYYGYLWAE VFATDMYHTK 670 680 690 700 710 FAKDPLNAKN GIQYRDIVLA RGGLYDINDN LKEFLGREPS KDAFLKELGL QN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15)." Buechler M., Tisljar U., Wolf D.H. Eur. J. Biochem. 219:627-639(1994) [PubMed: 8307027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, MASS SPECTROMETRY. Strain: ADR376.
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-75, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X76504 Genomic DNA. Translation: CAA54039.1. X59720 Genomic DNA. Translation: CAA42388.1. AY723761 Genomic DNA. Translation: AAU09678.1. BK006937 Genomic DNA. Translation: DAA07429.1.
PIR	S19387.
RefSeq	NP_009874.1. NM_001178701.1.
3D structure databases
ProteinModelPortal	P25375.
SMR	P25375. Positions 42-710.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4938N.
IntAct	P25375. 1 interaction.
MINT	MINT-542010.
STRING	P25375.
Protein family/group databases
MEROPS	M03.003.
Proteomic databases
PeptideAtlas	P25375.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCL057W; YCL057W; YCL057W.
GeneID	850301.
KEGG	sce:YCL057W.
NMPDR	fig|4932.3.peg.594.
Organism-specific databases
CYGD	YCL057w.
SGD	S000000562. PRD1.
Phylogenomic databases
eggNOG	fuNOG06686.
HOGENOM	HBG678447.
OMA	EQTKCVY.
OrthoDB	EOG4J6W01.
Gene expression databases
ArrayExpress	P25375.
Genevestigator	P25375.
GermOnline	YCL057W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR024079. MetalloPept_cat_dom. IPR024077. Neurolysin/TOP_dom2. IPR024080. Neurolysin/TOP_N. IPR001567. Pept_M3A_M3B. [Graphical view]
Gene3D	G3DSA:1.10.1370.10. G3DSA:1.10.1370.10. 2 hits. G3DSA:1.20.1050.40. G3DSA:1.20.1050.40. 1 hit. G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
KO	K01405.
Pfam	PF01432. Peptidase_M3. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	965679.

Entry information

Entry name

PRTD_YEAST

Accession

Primary (citable) accession number: P25375
Secondary accession number(s): D6VQW0, E9P942

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	December 14, 2011
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program