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Protein

Aspartic proteinase 3

Gene

YPS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves proteins C-terminally to mono- and paired-basic residues. Involved in the shedding of a subset of GPI-anchored plasma membrane proteins from the cell surface, including itself, GAS1 and MSB2. May also play a role in the maturation of GPI-mannoproteins associated with the cell wall. Can process the alpha-mating factor precursor. Required for cell wall integrity.4 Publications

Catalytic activityi

Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non-prime and prime positions.

pH dependencei

Optimum pH is 4.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei101 – 1011PROSITE-ProRule annotation
Active sitei371 – 3711PROSITE-ProRule annotation

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: SGD

GO - Biological processi

  • fungal-type cell wall organization Source: SGD
  • peptide mating pheromone maturation involved in conjugation with cellular fusion Source: SGD
  • protein processing Source: SGD
  • signal transduction involved in filamentous growth Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciYEAST:G3O-32265-MONOMER.
BRENDAi3.4.23.41. 984.
SABIO-RKP32329.

Protein family/group databases

MEROPSiA01.030.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartic proteinase 3 (EC:3.4.23.41)
Alternative name(s):
Proprotein convertase
Yapsin-1
Cleaved into the following 2 chains:
Gene namesi
Name:YPS1
Synonyms:YAP3
Ordered Locus Names:YLR120C
ORF Names:L2961, L9233.9
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR120C.
SGDiS000004110. YPS1.

Subcellular locationi

GO - Cellular componenti

  • anchored component of plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011D → A or E: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 67461 PublicationPRO_0000025838Add
BLAST
Chaini68 – 548481Aspartic proteinase 3PRO_0000025839Add
BLAST
Chaini68 – 12861Aspartic proteinase 3 subunit alphaPRO_0000372455Add
BLAST
Chaini145 – 548404Aspartic proteinase 3 subunit betaPRO_0000372456Add
BLAST
Propeptidei549 – 56921Removed in mature formSequence analysisPRO_0000025840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence analysis
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence analysis
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence analysis
Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence analysis
Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence analysis
Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence analysis
Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence analysis
Lipidationi548 – 5481GPI-anchor amidated asparagineSequence analysis

Post-translational modificationi

The zymogen is transported to the periplasm, where the propeptide is removed and the enzyme is further subjected to an internal, autocatalytic cleavage to generate an alpha/beta two-subunit endopeptidase. The proteolytic processing at the cell surface is regulated by the environmental pH.2 Publications
Extensively N-glycosylated.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei128 – 1292Cleavage; by autolysisCurated
Sitei144 – 1452Cleavage; by autolysis

Keywords - PTMi

Autocatalytic cleavage, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Zymogen

Proteomic databases

MaxQBiP32329.

Miscellaneous databases

PMAP-CutDBP32329.

Expressioni

Inductioni

Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation.1 Publication

Interactioni

Subunit structurei

Consists of an alpha and a beta subunit, which are maintained together by a disulfide bond.

Protein-protein interaction databases

BioGridi31392. 32 interactions.
DIPiDIP-2565N.
IntActiP32329. 1 interaction.
MINTiMINT-422799.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YPSmodel-A157-478[»]
ProteinModelPortaliP32329.
SMRiP32329. Positions 126-483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 475393Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00550000075429.
HOGENOMiHOG000248646.
InParanoidiP32329.
KOiK06009.
OMAiGFHINAP.
OrthoDBiEOG71P2M6.

Family and domain databases

Gene3Di2.40.70.10. 3 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 3 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 2 hits.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P32329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLKTVRSAV LSSLFASQVL GKIIPAANKR DDDSNSKFVK LPFHKLYGDS
60 70 80 90 100
LENVGSDKKP EVRLLKRADG YEEIIITNQQ SFYSVDLEVG TPPQNVTVLV
110 120 130 140 150
DTGSSDLWIM GSDNPYCSSN SMGSSRRRVI DKRDDSSSGG SLINDINPFG
160 170 180 190 200
WLTGTGSAIG PTATGLGGGS GTATQSVPAS EATMDCQQYG TFSTSGSSTF
210 220 230 240 250
RSNNTYFSIS YGDGTFASGT FGTDVLDLSD LNVTGLSFAV ANETNSTMGV
260 270 280 290 300
LGIGLPELEV TYSGSTASHS GKAYKYDNFP IVLKNSGAIK SNTYSLYLND
310 320 330 340 350
SDAMHGTILF GAVDHSKYTG TLYTIPIVNT LSASGFSSPI QFDVTINGIG
360 370 380 390 400
ISDSGSSNKT LTTTKIPALL DSGTTLTYLP QTVVSMIATE LGAQYSSRIG
410 420 430 440 450
YYVLDCPSDD SMEIVFDFGG FHINAPLSSF ILSTGTTCLL GIIPTSDDTG
460 470 480 490 500
TILGDSFLTN AYVVYDLENL EISMAQARYN TTSENIEIIT SSVPSAVKAP
510 520 530 540 550
GYTNTWSTSA SIVTGGNIFT VNSSQTASFS GNLTTSTASA TSTSSKRNVG
560
DHIVPSLPLT LISLLFAFI
Length:569
Mass (Da):60,010
Last modified:November 1, 1997 - v2
Checksum:i13FE892C9227EF8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti370 – 3701L → S in AAA19107 (PubMed:2183521).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31651 Unassigned DNA. Translation: AAA19107.1.
X89514 Genomic DNA. Translation: CAA61699.1.
Z73292 Genomic DNA. Translation: CAA97688.1.
U53877 Genomic DNA. Translation: AAB82367.1.
BK006945 Genomic DNA. Translation: DAA09434.1.
PIRiS64957.
RefSeqiNP_013221.1. NM_001182007.1.

Genome annotation databases

EnsemblFungiiYLR120C; YLR120C; YLR120C.
GeneIDi850811.
KEGGisce:YLR120C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31651 Unassigned DNA. Translation: AAA19107.1.
X89514 Genomic DNA. Translation: CAA61699.1.
Z73292 Genomic DNA. Translation: CAA97688.1.
U53877 Genomic DNA. Translation: AAB82367.1.
BK006945 Genomic DNA. Translation: DAA09434.1.
PIRiS64957.
RefSeqiNP_013221.1. NM_001182007.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YPSmodel-A157-478[»]
ProteinModelPortaliP32329.
SMRiP32329. Positions 126-483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31392. 32 interactions.
DIPiDIP-2565N.
IntActiP32329. 1 interaction.
MINTiMINT-422799.

Protein family/group databases

MEROPSiA01.030.

Proteomic databases

MaxQBiP32329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR120C; YLR120C; YLR120C.
GeneIDi850811.
KEGGisce:YLR120C.

Organism-specific databases

EuPathDBiFungiDB:YLR120C.
SGDiS000004110. YPS1.

Phylogenomic databases

GeneTreeiENSGT00550000075429.
HOGENOMiHOG000248646.
InParanoidiP32329.
KOiK06009.
OMAiGFHINAP.
OrthoDBiEOG71P2M6.

Enzyme and pathway databases

BioCyciYEAST:G3O-32265-MONOMER.
BRENDAi3.4.23.41. 984.
SABIO-RKP32329.

Miscellaneous databases

PMAP-CutDBP32329.
PROiP32329.

Family and domain databases

Gene3Di2.40.70.10. 3 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 3 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 2 hits.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel aspartyl protease allowing KEX2-independent MF alpha propheromone processing in yeast."
    Egel-Mitani M., Flygenring H.P., Hansen M.T.
    Yeast 6:127-137(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ME768.
  2. "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found."
    Verhasselt P., Volckaert G.
    Yeast 13:241-250(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90840 / EAY235 / FY23.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme."
    Azaryan A.V., Wong M., Friedman T.C., Cawley N.X., Estivariz F.E., Chen H.C., Loh Y.P.
    J. Biol. Chem. 268:11968-11975(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Secretion of yeast aspartic protease 3 is regulated by its carboxy-terminal tail: characterization of secreted YAP3p."
    Cawley N.X., Wong M., Pu L.-P., Tam W., Loh Y.P.
    Biochemistry 34:7430-7437(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR.
  7. "The yeast proprotein convertase encoded by YAP3 is a glycophosphatidylinositol-anchored protein that localizes to the plasma membrane."
    Ash J., Dominguez M., Bergeron J.J.M., Thomas D.Y., Bourbonnais Y.
    J. Biol. Chem. 270:20847-20854(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
  8. "Activation and processing of non-anchored yapsin 1 (Yap3p)."
    Cawley N.X., Olsen V., Zhang C.F., Chen H.C., Tan M., Loh Y.P.
    J. Biol. Chem. 273:584-591(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 68-82 AND 145-159, FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-101, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BOND.
  9. "Proteolytic function of GPI-anchored plasma membrane protease Yps1p in the yeast vacuole and Golgi."
    Sievi E., Suntio T., Makarow M.
    Traffic 2:896-907(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "The omega-site sequence of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae can determine distribution between the membrane and the cell wall."
    Frieman M.B., Cormack B.P.
    Mol. Microbiol. 50:883-896(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae."
    Krysan D.J., Ting E.L., Abeijon C., Kroos L., Fuller R.S.
    Eukaryot. Cell 4:1364-1374(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  13. "Cleavage of the signaling mucin Msb2 by the aspartyl protease Yps1 is required for MAPK activation in yeast."
    Vadaie N., Dionne H., Akajagbor D.S., Nickerson S.R., Krysan D.J., Cullen P.J.
    J. Cell Biol. 181:1073-1081(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Activation mechanism, functional role and shedding of glycosylphosphatidylinositol-anchored Yps1p at the Saccharomyces cerevisiae cell surface."
    Gagnon-Arsenault I., Parise L., Tremblay J., Bourbonnais Y.
    Mol. Microbiol. 69:982-993(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC PROCESSING.
  15. "Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p) enhanced for substrates with arginine residues flanking the P1 site: correlation with electronegative active-site pockets predicted by molecular modeling."
    Olsen V., Guruprasad K., Cawley N.X., Chen H.C., Blundell T.L., Loh Y.P.
    Biochemistry 37:2768-2777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiYPS1_YEAST
AccessioniPrimary (citable) accession number: P32329
Secondary accession number(s): D6VYB8, Q12419
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5000 molecules/cell in log phase SD medium.1 Publication

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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.