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P07267

- CARP_YEAST

UniProt

P07267 - CARP_YEAST

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Protein
Saccharopepsin
Gene
PEP4, PHO9, PRA1, YPL154C, P2585
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei109 – 1091 By similarity
Active sitei294 – 2941 By similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
  2. peptidase activity Source: SGD

GO - Biological processi

  1. autophagy Source: SGD
  2. cellular response to starvation Source: SGD
  3. microautophagy Source: SGD
  4. proteolysis involved in cellular protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciYEAST:YPL154C-MONOMER.

Protein family/group databases

MEROPSiA01.018.

Names & Taxonomyi

Protein namesi
Recommended name:
Saccharopepsin (EC:3.4.23.25)
Alternative name(s):
Aspartate protease
Short name:
PrA
Short name:
Proteinase A
Carboxypeptidase Y-deficient protein 4
Proteinase YSCA
Gene namesi
Name:PEP4
Synonyms:PHO9, PRA1
Ordered Locus Names:YPL154C
ORF Names:P2585
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL154c.
SGDiS000006075. PEP4.

Subcellular locationi

Vacuole
Note: Lysosome-like vacuoles.

GO - Cellular componenti

  1. fungal-type vacuole Source: SGD
  2. fungal-type vacuole lumen Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi294 – 2941D → A: Inactivation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 Publication
Add
BLAST
Propeptidei23 – 7654Activation peptide
PRO_0000025873Add
BLAST
Chaini77 – 405329Saccharopepsin
PRO_0000025874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi122 ↔ 127
Glycosylationi144 – 1441N-linked (GlcNAc...)
Disulfide bondi328 ↔ 361
Glycosylationi345 – 3451N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP07267.
PaxDbiP07267.
PeptideAtlasiP07267.

2D gel databases

UCD-2DPAGEP07267.

Miscellaneous databases

PMAP-CutDBP07267.

Expressioni

Gene expression databases

GenevestigatoriP07267.

Interactioni

Protein-protein interaction databases

BioGridi36029. 50 interactions.
DIPiDIP-4442N.
IntActiP07267. 8 interactions.
MINTiMINT-382859.
STRINGi4932.YPL154C.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi79 – 824
Beta strandi84 – 863
Turni87 – 893
Beta strandi90 – 978
Turni98 – 1014
Beta strandi102 – 1098
Beta strandi115 – 1195
Helixi125 – 1284
Helixi135 – 1373
Beta strandi142 – 15211
Beta strandi155 – 16814
Beta strandi171 – 18313
Helixi186 – 1894
Beta strandi195 – 1995
Helixi203 – 2053
Helixi207 – 2093
Helixi213 – 2197
Beta strandi224 – 2329
Helixi235 – 2373
Beta strandi240 – 24910
Helixi252 – 2543
Beta strandi255 – 2639
Turni267 – 2704
Beta strandi271 – 2799
Beta strandi282 – 2854
Beta strandi290 – 2934
Beta strandi300 – 3023
Helixi304 – 31411
Beta strandi317 – 3193
Beta strandi322 – 3265
Helixi328 – 3336
Beta strandi337 – 3415
Beta strandi344 – 3485
Turni350 – 3523
Beta strandi353 – 3575
Beta strandi360 – 3634
Beta strandi365 – 3673
Turni372 – 3743
Beta strandi376 – 3805
Helixi382 – 3854
Beta strandi388 – 3936
Turni394 – 3974
Beta strandi398 – 4047

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DP5X-ray2.20A77-405[»]
1DPJX-ray1.80A77-405[»]
1FMUX-ray2.70A77-405[»]
1FMXX-ray2.61A/B77-405[»]
1FQ4X-ray2.70A77-405[»]
1FQ5X-ray2.40A77-405[»]
1FQ6X-ray2.70A77-405[»]
1FQ7X-ray2.80A77-405[»]
1FQ8X-ray2.80A77-405[»]
1G0VX-ray2.00A77-405[»]
2JXRX-ray2.40A77-405[»]
ProteinModelPortaliP07267.
SMRiP07267. Positions 77-405.

Miscellaneous databases

EvolutionaryTraceiP07267.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG248684.
GeneTreeiENSGT00710000106265.
HOGENOMiHOG000197681.
KOiK01381.
OMAiCRSANIG.
OrthoDBiEOG7MKWGD.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 2 hits.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07267-1 [UniParc]FASTAAdd to Basket

« Hide

MFSLKALLPL ALLLVSANQV AAKVHKAKIY KHELSDEMKE VTFEQHLAHL    50
GQKYLTQFEK ANPEVVFSRE HPFFTEGGHD VPLTNYLNAQ YYTDITLGTP 100
PQNFKVILDT GSSNLWVPSN ECGSLACFLH SKYDHEASSS YKANGTEFAI 150
QYGTGSLEGY ISQDTLSIGD LTIPKQDFAE ATSEPGLTFA FGKFDGILGL 200
GYDTISVDKV VPPFYNAIQQ DLLDEKRFAF YLGDTSKDTE NGGEATFGGI 250
DESKFKGDIT WLPVRRKAYW EVKFEGIGLG DEYAELESHG AAIDTGTSLI 300
TLPSGLAEMI NAEIGAKKGW TGQYTLDCNT RDNLPDLIFN FNGYNFTIGP 350
YDYTLEVSGS CISAITPMDF PEPVGPLAIV GDAFLRKYYS IYDLGNNAVG 400
LAKAI 405
Length:405
Mass (Da):44,499
Last modified:April 1, 1988 - v1
Checksum:iB0AA36BA098D2BF7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13358 Genomic DNA. Translation: AAB63975.1.
X96770 Genomic DNA. Translation: CAA65567.1.
Z73510 Genomic DNA. Translation: CAA97859.1.
Z11963 Genomic DNA. Translation: CAA78020.1.
BK006949 Genomic DNA. Translation: DAA11280.1.
PIRiA25379.
RefSeqiNP_015171.1. NM_001183968.1.

Genome annotation databases

EnsemblFungiiYPL154C; YPL154C; YPL154C.
GeneIDi855949.
KEGGisce:YPL154C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13358 Genomic DNA. Translation: AAB63975.1 .
X96770 Genomic DNA. Translation: CAA65567.1 .
Z73510 Genomic DNA. Translation: CAA97859.1 .
Z11963 Genomic DNA. Translation: CAA78020.1 .
BK006949 Genomic DNA. Translation: DAA11280.1 .
PIRi A25379.
RefSeqi NP_015171.1. NM_001183968.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P07267.
SMRi P07267. Positions 77-405.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36029. 50 interactions.
DIPi DIP-4442N.
IntActi P07267. 8 interactions.
MINTi MINT-382859.
STRINGi 4932.YPL154C.

Chemistry

BindingDBi P07267.
ChEMBLi CHEMBL4451.

Protein family/group databases

MEROPSi A01.018.

2D gel databases

UCD-2DPAGE P07267.

Proteomic databases

MaxQBi P07267.
PaxDbi P07267.
PeptideAtlasi P07267.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL154C ; YPL154C ; YPL154C .
GeneIDi 855949.
KEGGi sce:YPL154C.

Organism-specific databases

CYGDi YPL154c.
SGDi S000006075. PEP4.

Phylogenomic databases

eggNOGi NOG248684.
GeneTreei ENSGT00710000106265.
HOGENOMi HOG000197681.
KOi K01381.
OMAi CRSANIG.
OrthoDBi EOG7MKWGD.

Enzyme and pathway databases

BioCyci YEAST:YPL154C-MONOMER.

Miscellaneous databases

EvolutionaryTracei P07267.
NextBioi 980726.
PMAP-CutDB P07267.

Gene expression databases

Genevestigatori P07267.

Family and domain databases

Gene3Di 2.40.70.10. 2 hits.
InterProi IPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view ]
PANTHERi PTHR13683. PTHR13683. 1 hit.
Pfami PF00026. Asp. 1 hit.
[Graphical view ]
PRINTSi PR00792. PEPSIN.
SUPFAMi SSF50630. SSF50630. 2 hits.
PROSITEi PS00141. ASP_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "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.
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 373-405.
    Strain: ATCC 204508 / S288c.
  8. "Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A."
    Wolff A.M., Dimn N., Petersen J.G.L.
    Yeast 12:823-832(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-31 AND 68-86.
  9. "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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-294.
  10. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiCARP_YEAST
AccessioniPrimary (citable) accession number: P07267
Secondary accession number(s): D6W3L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

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