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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)DescriptionActionsGraphical viewLength
Active sitei101PROSITE-ProRule annotation1
Active sitei371PROSITE-ProRule annotation1

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 catabolic process Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi101D → A or E: Loss of function. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000002583822 – 671 PublicationAdd BLAST46
ChainiPRO_000002583968 – 548Aspartic proteinase 3Add BLAST481
ChainiPRO_000037245568 – 128Aspartic proteinase 3 subunit alphaAdd BLAST61
ChainiPRO_0000372456145 – 548Aspartic proteinase 3 subunit betaAdd BLAST404
PropeptideiPRO_0000025840549 – 569Removed in mature formSequence analysisAdd BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi95N-linked (GlcNAc...)Sequence analysis1
Glycosylationi203N-linked (GlcNAc...)Sequence analysis1
Glycosylationi232N-linked (GlcNAc...)Sequence analysis1
Glycosylationi242N-linked (GlcNAc...)Sequence analysis1
Glycosylationi245N-linked (GlcNAc...)Sequence analysis1
Glycosylationi299N-linked (GlcNAc...)Sequence analysis1
Glycosylationi358N-linked (GlcNAc...)Sequence analysis1
Glycosylationi480N-linked (GlcNAc...)Sequence analysis1
Glycosylationi522N-linked (GlcNAc...)Sequence analysis1
Glycosylationi532N-linked (GlcNAc...)Sequence analysis1
Lipidationi548GPI-anchor amidated asparagineSequence analysis1

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)DescriptionActionsGraphical viewLength
Sitei128 – 129Cleavage; by autolysisCurated2
Sitei144 – 145Cleavage; by autolysis2

Keywords - PTMi

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

Proteomic databases

MaxQBiP32329.
PRIDEiP32329.

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 interactors.
DIPiDIP-2565N.
IntActiP32329. 1 interactor.
MINTiMINT-422799.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YPSmodel-A157-478[»]
ProteinModelPortaliP32329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini83 – 475Peptidase A1PROSITE-ProRule annotationAdd BLAST393

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.
OrthoDBiEOG092C3KPP.

Family and domain databases

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 3 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti370L → S in AAA19107 (PubMed:2183521).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YPSmodel-A157-478[»]
ProteinModelPortaliP32329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31392. 32 interactors.
DIPiDIP-2565N.
IntActiP32329. 1 interactor.
MINTiMINT-422799.

Protein family/group databases

MEROPSiA01.030.

Proteomic databases

MaxQBiP32329.
PRIDEiP32329.

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.
OrthoDBiEOG092C3KPP.

Enzyme and pathway databases

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

Miscellaneous databases

PMAP-CutDBP32329.
PROiP32329.

Family and domain databases

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 3 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
[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...

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: November 30, 2016
This is version 163 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.