YPS1_YEAST
ID YPS1_YEAST Reviewed; 569 AA.
AC P32329; D6VYB8; Q12419;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Aspartic proteinase 3;
DE EC=3.4.23.41;
DE AltName: Full=Proprotein convertase;
DE AltName: Full=Yapsin-1;
DE Contains:
DE RecName: Full=Aspartic proteinase 3 subunit alpha;
DE Contains:
DE RecName: Full=Aspartic proteinase 3 subunit beta;
DE Flags: Precursor;
GN Name=YPS1; Synonyms=YAP3; OrderedLocusNames=YLR120C;
GN ORFNames=L2961, L9233.9;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ME768;
RX PubMed=2183521; DOI=10.1002/yea.320060206;
RA Egel-Mitani M., Flygenring H.P., Hansen M.T.;
RT "A novel aspartyl protease allowing KEX2-independent MF alpha propheromone
RT processing in yeast.";
RL Yeast 6:127-137(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8389368; DOI=10.1016/s0021-9258(19)50295-2;
RA Azaryan A.V., Wong M., Friedman T.C., Cawley N.X., Estivariz F.E.,
RA Chen H.C., Loh Y.P.;
RT "Purification and characterization of a paired basic residue-specific yeast
RT aspartic protease encoded by the YAP3 gene. Similarity to the mammalian
RT pro-opiomelanocortin-converting enzyme.";
RL J. Biol. Chem. 268:11968-11975(1993).
RN [6]
RP GPI-ANCHOR.
RX PubMed=7779785; DOI=10.1021/bi00022a016;
RA Cawley N.X., Wong M., Pu L.-P., Tam W., Loh Y.P.;
RT "Secretion of yeast aspartic protease 3 is regulated by its carboxy-
RT terminal tail: characterization of secreted YAP3p.";
RL Biochemistry 34:7430-7437(1995).
RN [7]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=7657670; DOI=10.1074/jbc.270.35.20847;
RA Ash J., Dominguez M., Bergeron J.J.M., Thomas D.Y., Bourbonnais Y.;
RT "The yeast proprotein convertase encoded by YAP3 is a
RT glycophosphatidylinositol-anchored protein that localizes to the plasma
RT membrane.";
RL J. Biol. Chem. 270:20847-20854(1995).
RN [8]
RP PROTEIN SEQUENCE OF 68-82 AND 145-159, FUNCTION, SUBCELLULAR LOCATION,
RP PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-101, GLYCOSYLATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE BOND.
RX PubMed=9417119; DOI=10.1074/jbc.273.1.584;
RA Cawley N.X., Olsen V., Zhang C.F., Chen H.C., Tan M., Loh Y.P.;
RT "Activation and processing of non-anchored yapsin 1 (Yap3p).";
RL J. Biol. Chem. 273:584-591(1998).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11737827; DOI=10.1034/j.1600-0854.2001.21205.x;
RA Sievi E., Suntio T., Makarow M.;
RT "Proteolytic function of GPI-anchored plasma membrane protease Yps1p in the
RT yeast vacuole and Golgi.";
RL Traffic 2:896-907(2001).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=14617149; DOI=10.1046/j.1365-2958.2003.03722.x;
RA Frieman M.B., Cormack B.P.;
RT "The omega-site sequence of glycosylphosphatidylinositol-anchored proteins
RT in Saccharomyces cerevisiae can determine distribution between the membrane
RT and the cell wall.";
RL Mol. Microbiol. 50:883-896(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=16087741; DOI=10.1128/ec.4.8.1364-1374.2005;
RA Krysan D.J., Ting E.L., Abeijon C., Kroos L., Fuller R.S.;
RT "Yapsins are a family of aspartyl proteases required for cell wall
RT integrity in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:1364-1374(2005).
RN [13]
RP FUNCTION.
RX PubMed=18591427; DOI=10.1083/jcb.200704079;
RA Vadaie N., Dionne H., Akajagbor D.S., Nickerson S.R., Krysan D.J.,
RA Cullen P.J.;
RT "Cleavage of the signaling mucin Msb2 by the aspartyl protease Yps1 is
RT required for MAPK activation in yeast.";
RL J. Cell Biol. 181:1073-1081(2008).
RN [14]
RP FUNCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=18573178; DOI=10.1111/j.1365-2958.2008.06339.x;
RA Gagnon-Arsenault I., Parise L., Tremblay J., Bourbonnais Y.;
RT "Activation mechanism, functional role and shedding of
RT glycosylphosphatidylinositol-anchored Yps1p at the Saccharomyces cerevisiae
RT cell surface.";
RL Mol. Microbiol. 69:982-993(2008).
RN [15]
RP 3D-STRUCTURE MODELING.
RX PubMed=9485427; DOI=10.1021/bi9724826;
RA Olsen V., Guruprasad K., Cawley N.X., Chen H.C., Blundell T.L., Loh Y.P.;
RT "Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p)
RT enhanced for substrates with arginine residues flanking the P1 site:
RT correlation with electronegative active-site pockets predicted by molecular
RT modeling.";
RL Biochemistry 37:2768-2777(1998).
CC -!- FUNCTION: Cleaves proteins C-terminally to mono- and paired-basic
CC residues. Involved in the shedding of a subset of GPI-anchored plasma
CC membrane proteins from the cell surface, including itself, GAS1 and
CC MSB2. May also play a role in the maturation of GPI-mannoproteins
CC associated with the cell wall. Can process the alpha-mating factor
CC precursor. Required for cell wall integrity.
CC {ECO:0000269|PubMed:16087741, ECO:0000269|PubMed:18573178,
CC ECO:0000269|PubMed:18591427, ECO:0000269|PubMed:9417119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes various precursor proteins with Arg or Lys in P1,
CC and commonly Arg or Lys also in P2. The P3 amino acid is usually non-
CC polar, but otherwise additional basic amino acids are favorable in
CC both non-prime and prime positions.; EC=3.4.23.41;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:9417119};
CC -!- SUBUNIT: Consists of an alpha and a beta subunit, which are maintained
CC together by a disulfide bond.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11737827,
CC ECO:0000269|PubMed:14617149, ECO:0000269|PubMed:7657670,
CC ECO:0000269|PubMed:9417119}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:11737827, ECO:0000269|PubMed:14617149,
CC ECO:0000269|PubMed:7657670, ECO:0000269|PubMed:9417119}. Note=GPI-
CC anchored plasma membrane protein (GPI-PMP), peripherally distributed
CC over the entire cell surface.
CC -!- INDUCTION: Positively regulated by cell integrity signaling through
CC MPK1 in response to cell wall perturbation.
CC {ECO:0000269|PubMed:16087741}.
CC -!- PTM: The zymogen is transported to the periplasm, where the propeptide
CC is removed and the enzyme is further subjected to an internal,
CC autocatalytic cleavage to generate an alpha/beta two-subunit
CC endopeptidase. The proteolytic processing at the cell surface is
CC regulated by the environmental pH. {ECO:0000269|PubMed:18573178,
CC ECO:0000269|PubMed:9417119}.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000269|PubMed:7657670,
CC ECO:0000269|PubMed:9417119}.
CC -!- MISCELLANEOUS: Present with 5000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; L31651; AAA19107.1; -; Unassigned_DNA.
DR EMBL; X89514; CAA61699.1; -; Genomic_DNA.
DR EMBL; Z73292; CAA97688.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82367.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09434.1; -; Genomic_DNA.
DR PIR; S64957; S64957.
DR RefSeq; NP_013221.1; NM_001182007.1.
DR AlphaFoldDB; P32329; -.
DR SMR; P32329; -.
DR BioGRID; 31392; 119.
DR DIP; DIP-2565N; -.
DR IntAct; P32329; 1.
DR MINT; P32329; -.
DR STRING; 4932.YLR120C; -.
DR MEROPS; A01.030; -.
DR MaxQB; P32329; -.
DR PaxDb; P32329; -.
DR PRIDE; P32329; -.
DR EnsemblFungi; YLR120C_mRNA; YLR120C; YLR120C.
DR GeneID; 850811; -.
DR KEGG; sce:YLR120C; -.
DR SGD; S000004110; YPS1.
DR VEuPathDB; FungiDB:YLR120C; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000166661; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; P32329; -.
DR OMA; LYFMGGV; -.
DR BioCyc; YEAST:G3O-32265-MON; -.
DR BRENDA; 3.4.23.41; 984.
DR SABIO-RK; P32329; -.
DR PRO; PR:P32329; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32329; protein.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:SGD.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR GO; GO:0071432; P:peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion; IGI:SGD.
DR GO; GO:0016485; P:protein processing; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47965; PTHR47965; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Autocatalytic cleavage; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..67
FT /evidence="ECO:0000269|PubMed:9417119"
FT /id="PRO_0000025838"
FT CHAIN 68..548
FT /note="Aspartic proteinase 3"
FT /id="PRO_0000025839"
FT CHAIN 68..128
FT /note="Aspartic proteinase 3 subunit alpha"
FT /id="PRO_0000372455"
FT CHAIN 145..548
FT /note="Aspartic proteinase 3 subunit beta"
FT /id="PRO_0000372456"
FT PROPEP 549..569
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025840"
FT DOMAIN 83..475
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT SITE 128..129
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305"
FT SITE 144..145
FT /note="Cleavage; by autolysis"
FT LIPID 548
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 101
FT /note="D->A,E: Loss of function."
FT /evidence="ECO:0000269|PubMed:9417119"
FT CONFLICT 370
FT /note="L -> S (in Ref. 1; AAA19107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 60010 MW; 13FE892C9227EF8B CRC64;
MKLKTVRSAV LSSLFASQVL GKIIPAANKR DDDSNSKFVK LPFHKLYGDS LENVGSDKKP
EVRLLKRADG YEEIIITNQQ SFYSVDLEVG TPPQNVTVLV DTGSSDLWIM GSDNPYCSSN
SMGSSRRRVI DKRDDSSSGG SLINDINPFG WLTGTGSAIG PTATGLGGGS GTATQSVPAS
EATMDCQQYG TFSTSGSSTF RSNNTYFSIS YGDGTFASGT FGTDVLDLSD LNVTGLSFAV
ANETNSTMGV LGIGLPELEV TYSGSTASHS GKAYKYDNFP IVLKNSGAIK SNTYSLYLND
SDAMHGTILF GAVDHSKYTG TLYTIPIVNT LSASGFSSPI QFDVTINGIG ISDSGSSNKT
LTTTKIPALL DSGTTLTYLP QTVVSMIATE LGAQYSSRIG YYVLDCPSDD SMEIVFDFGG
FHINAPLSSF ILSTGTTCLL GIIPTSDDTG TILGDSFLTN AYVVYDLENL EISMAQARYN
TTSENIEIIT SSVPSAVKAP GYTNTWSTSA SIVTGGNIFT VNSSQTASFS GNLTTSTASA
TSTSSKRNVG DHIVPSLPLT LISLLFAFI
