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P07267

- CARP_YEAST

UniProt

P07267 - CARP_YEAST

Protein

Saccharopepsin

Gene

PEP4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    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 – 1091PROSITE-ProRule annotation
    Active sitei294 – 2941PROSITE-ProRule annotation

    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

    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

    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 PublicationAdd
    BLAST
    Propeptidei23 – 7654Activation peptide1 PublicationPRO_0000025873Add
    BLAST
    Chaini77 – 405329SaccharopepsinPRO_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

    1
    405
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07267.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    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

    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: October 1, 2014
    This is version 159 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