Reviewed, UniProtKB/Swiss-Prot P07267 (CARP_YEAST)

Names and origin

Protein names

Recommended name:
    Saccharopepsin
    EC=3.4.23.25
Alternative name(s):
    Aspartate protease
      Short name(s)=Proteinase A
    Proteinase YSCA
    Carboxypeptidase Y-deficient protein 4

Gene names

Name:	PEP4
Synonyms:	PHO9, PRA1
Ordered Locus Names:	YPL154C
ORF Names:	P2585

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	405 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.
Catalytic activity	Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
Subcellular location	Vacuole. Note= Lysosome-like vacuoles.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Vacuole
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular response to starvation Inferred from mutant phenotype. Source: SGD microautophagy Inferred from mutant phenotype. Source: SGD sporulation Inferred from mutant phenotype. Source: SGD vacuolar protein catabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	fungal-type vacuole lumen Traceable author statement. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	saccharopepsin activity Traceable author statement. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 22

22

Propeptide

23 – 76

54

Activation peptide

Chain

77 – 405

329

Saccharopepsin

Sites

Active site

109

1

By similarity

Active site

294

1

By similarity

Amino acid modifications

Glycosylation

144

1

N-linked (GlcNAc...)

Glycosylation

345

1

N-linked (GlcNAc...)

Disulfide bond

122 ↔ 127

Disulfide bond

328 ↔ 361

Experimental info

Mutagenesis

294

1

D → A: Inactivation

Secondary structure

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405

Helix Strand Turn

Details...

Beta strand

79 – 82

4

Beta strand

84 – 86

3

Turn

87 – 89

3

Beta strand

90 – 97

8

Turn

98 – 101

4

Beta strand

102 – 109

8

Beta strand

115 – 119

5

Helix

125 – 128

4

Helix

135 – 137

3

Beta strand

142 – 152

11

Beta strand

155 – 168

14

Beta strand

171 – 183

13

Helix

186 – 189

4

Beta strand

195 – 199

5

Helix

203 – 205

3

Helix

207 – 209

3

Helix

213 – 219

7

Beta strand

224 – 232

9

Helix

235 – 237

3

Beta strand

240 – 249

10

Helix

252 – 254

3

Beta strand

255 – 263

9

Turn

267 – 270

4

Beta strand

271 – 279

9

Beta strand

282 – 285

4

Beta strand

290 – 293

4

Beta strand

300 – 302

3

Helix

304 – 313

10

Beta strand

322 – 326

5

Helix

328 – 333

6

Beta strand

337 – 341

5

Beta strand

344 – 348

5

Turn

350 – 352

3

Beta strand

353 – 357

5

Beta strand

360 – 363

4

Beta strand

365 – 367

3

Turn

372 – 374

3

Beta strand

376 – 380

5

Helix

382 – 385

4

Beta strand

388 – 393

6

Turn

394 – 397

4

Beta strand

398 – 404

7

Sequences

	Sequence		Length	Mass (Da)
	P07267-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: B0AA36BA098D2BF7	FASTA	405	44,499
	10 20 30 40 50 60 MFSLKALLPL ALLLVSANQV AAKVHKAKIY KHELSDEMKE VTFEQHLAHL GQKYLTQFEK 70 80 90 100 110 120 ANPEVVFSRE HPFFTEGGHD VPLTNYLNAQ YYTDITLGTP PQNFKVILDT GSSNLWVPSN 130 140 150 160 170 180 ECGSLACFLH SKYDHEASSS YKANGTEFAI QYGTGSLEGY ISQDTLSIGD LTIPKQDFAE 190 200 210 220 230 240 ATSEPGLTFA FGKFDGILGL GYDTISVDKV VPPFYNAIQQ DLLDEKRFAF YLGDTSKDTE 250 260 270 280 290 300 NGGEATFGGI DESKFKGDIT WLPVRRKAYW EVKFEGIGLG DEYAELESHG AAIDTGTSLI 310 320 330 340 350 360 TLPSGLAEMI NAEIGAKKGW TGQYTLDCNT RDNLPDLIFN FNGYNFTIGP YDYTLEVSGS 370 380 390 400 CISAITPMDF PEPVGPLAIV GDAFLRKYYS IYDLGNNAVG LAKAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases." Woolford C.A., Daniels L.B., Park F.J., Jones E.W., van Arsdell J.N., Innis M.A. Mol. Cell. Biol. 6:2500-2510(1986) [PubMed: 3537721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors." Ammerer G., Hunter C.P., Rothman J.H., Saari G.C., Valls L.A., Stevens T.H. Mol. Cell. Biol. 6:2490-2499(1986) [PubMed: 3023936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a small nuclear RNA, a new putative protein kinase and two new putative regulators." Purnelle B., Coster F., Goffeau A. Yeast 12:1483-1492(1996) [PubMed: 8948103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	"Primary structure of the aspartic proteinase A from Saccharomyces cerevisiae." Dreyer T., Halkier B., Svendsen I., Ottesen M. Carlsberg Res. Commun. 51:27-41(1986) Cited for: PROTEIN SEQUENCE OF 77-405.
[6]	"Kinesin-related proteins required for assembly of the mitotic spindle." Roof D.M., Meluh P.B., Rose M.D. J. Cell Biol. 118:95-108(1992) [PubMed: 1618910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 373-405. Strain: ATCC 204508 / S288c.
[7]	"Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A." Wolff A.M., Dimn N., Petersen J.G.L. Yeast 12:823-832(1996) [PubMed: 8840499] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-31 AND 68-86.
[8]	"Biogenesis of the yeast vacuole (lysosome). Active site mutation in the vacuolar aspartate proteinase yscA blocks maturation of vacuolar proteinases." Rupp S., Hirsch H.H., Wolf D.H. FEBS Lett. 293:62-66(1991) [PubMed: 1959673] [Abstract] Cited for: MUTAGENESIS OF ASP-294.
[9]	"The three-dimensional structure at 2.4-A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae." Aguilar C.F., Cronin N.B., Badasso M., Dreyer T., Newman M.P., Cooper J.B., Hoover D.J., Wood S.P., Johnson M.S., Blundell T.L. J. Mol. Biol. 267:899-915(1997) [PubMed: 9135120] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M13358 Genomic DNA. Translation: AAB63975.1.
X96770 Genomic DNA. Translation: CAA65567.1.
Z73510 Genomic DNA. Translation: CAA97859.1.
Z11963 Genomic DNA. Translation: CAA78020.1.

PIR

A25379.

RefSeq

NP_015171.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DP5	X-ray	2.20	A	77-405	[»]
1DPJ	X-ray	1.80	A	77-405	[»]
1FMU	X-ray	2.70	A	77-405	[»]
1FMX	X-ray	2.61	A/B	77-405	[»]
1FQ4	X-ray	2.70	A	77-405	[»]
1FQ5	X-ray	2.40	A	77-405	[»]
1FQ6	X-ray	2.70	A	77-405	[»]
1FQ7	X-ray	2.80	A	77-405	[»]
1FQ8	X-ray	2.80	A	77-405	[»]
1G0V	X-ray	2.00	A	77-405	[»]
2JXR	X-ray	2.40	A	77-405	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4442N.

IntAct

P07267.

Protein family/group databases

MEROPS

A01.018.

Proteomic databases

PeptideAtlas

P07267.

Genome annotation databases

Ensembl

YPL154C. Saccharomyces cerevisiae. [Contig view]

GeneID

855949.

GenomeReviews

Gene locus YPL154C in contig U00094_GR.

KEGG

sce:YPL154C.

NMPDR

fig|4932.3.peg.6300.

Organism-specific databases

CYGD

YPL154c.

SGD

S000006075. PEP4.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P07267.

Gene expression databases

GermOnline

YPL154C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001969. Pept_Asp_AS.
IPR009007. Pept_Aspartc_cat.
IPR001461