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P32329 (YPS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartic proteinase 3
EC=3.4.23.41
Alternative name(s):
Proprotein convertase
Yapsin-1

Cleaved into the following 2 chains:

  1. Aspartic proteinase 3 subunit alpha
  2. Aspartic proteinase 3 subunit beta
Gene names
Name:YPS1
Synonyms:YAP3
Ordered Locus Names:YLR120C
ORF Names:L2961, L9233.9
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.12 Ref.13 Ref.14

Catalytic activity

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.

Subunit structure

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

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor. Note: GPI-anchored plasma membrane protein (GPI-PMP), peripherally distributed over the entire cell surface. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Induction

Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation. Ref.12

Post-translational modification

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.

Extensively N-glycosylated. Ref.7 Ref.8

Miscellaneous

Present with 5000 molecules/cell in log phase SD medium. Ref.11

Sequence similarities

Belongs to the peptidase A1 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.0. Ref.8

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 6746
PRO_0000025838
Chain68 – 548481Aspartic proteinase 3
PRO_0000025839
Chain68 – 12861Aspartic proteinase 3 subunit alpha
PRO_0000372455
Chain145 – 548404Aspartic proteinase 3 subunit beta
PRO_0000372456
Propeptide549 – 56921Removed in mature form Potential
PRO_0000025840

Sites

Active site1011 By similarity
Active site3711 By similarity
Site128 – 1292Cleavage; by autolysis Probable
Site144 – 1452Cleavage; by autolysis

Amino acid modifications

Lipidation5481GPI-anchor amidated asparagine Potential
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation5321N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis1011D → A or E: Loss of function. Ref.8
Sequence conflict3701L → S in AAA19107. Ref.1

Secondary structure

1 .............................................................. 569
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32329 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 13FE892C9227EF8B

FASTA56960,010
        10         20         30         40         50         60 
MKLKTVRSAV LSSLFASQVL GKIIPAANKR DDDSNSKFVK LPFHKLYGDS LENVGSDKKP 

        70         80         90        100        110        120 
EVRLLKRADG YEEIIITNQQ SFYSVDLEVG TPPQNVTVLV DTGSSDLWIM GSDNPYCSSN 

       130        140        150        160        170        180 
SMGSSRRRVI DKRDDSSSGG SLINDINPFG WLTGTGSAIG PTATGLGGGS GTATQSVPAS 

       190        200        210        220        230        240 
EATMDCQQYG TFSTSGSSTF RSNNTYFSIS YGDGTFASGT FGTDVLDLSD LNVTGLSFAV 

       250        260        270        280        290        300 
ANETNSTMGV LGIGLPELEV TYSGSTASHS GKAYKYDNFP IVLKNSGAIK SNTYSLYLND 

       310        320        330        340        350        360 
SDAMHGTILF GAVDHSKYTG TLYTIPIVNT LSASGFSSPI QFDVTINGIG ISDSGSSNKT 

       370        380        390        400        410        420 
LTTTKIPALL DSGTTLTYLP QTVVSMIATE LGAQYSSRIG YYVLDCPSDD SMEIVFDFGG 

       430        440        450        460        470        480 
FHINAPLSSF ILSTGTTCLL GIIPTSDDTG TILGDSFLTN AYVVYDLENL EISMAQARYN 

       490        500        510        520        530        540 
TTSENIEIIT SSVPSAVKAP GYTNTWSTSA SIVTGGNIFT VNSSQTASFS GNLTTSTASA 

       550        560 
TSTSSKRNVG DHIVPSLPLT LISLLFAFI

« Hide

References

« Hide 'large scale' references
[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: 2183521] [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: 9090053] [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. expand/collapse author list , 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: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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: 8389368] [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: 7779785] [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: 7657670] [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: 9417119] [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: 11737827] [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: 14617149] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
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: 16087741] [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: 18591427] [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: 18573178] [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: 9485427] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRS64957.
RefSeqNP_013221.1. NM_001182007.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YPSmodel-A157-478[»]
ProteinModelPortalP32329.
SMRP32329. Positions 71-489.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2565N.
MINTMINT-422799.
STRINGP32329.

Protein family/group databases

MEROPSA01.030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR120C; YLR120C; YLR120C.
GeneID850811.
KEGGsce:YLR120C.
NMPDRfig|4932.3.peg.4213.

Organism-specific databases

CYGDYLR120c.
SGDS000004110. YPS1.

Phylogenomic databases

eggNOGfuNOG05617.
GeneTreeEFGT00050000001345.
HOGENOMHBG398805.
OMAGSFNTEN.
OrthoDBEOG4PVS79.

Gene expression databases

ArrayExpressP32329.
GenevestigatorP32329.
GermOnlineYLR120C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 3 hits.
KOK06009.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio967049.
PMAP-CutDBP32329.

Entry information

Entry nameYPS1_YEAST
AccessionPrimary (citable) accession number: P32329
Secondary accession number(s): D6VYB8, Q12419
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents