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Database: UniProt
Entry: YPS6_YEAST
LinkDB: YPS6_YEAST
Original site: YPS6_YEAST 
ID   YPS6_YEAST              Reviewed;         537 AA.
AC   P40583; D6VVX0; E9PAD7;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Aspartic proteinase yapsin-6;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=YPS6; OrderedLocusNames=YIR039C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [2]
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   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10383953; DOI=10.1128/jb.181.13.3886-3889.1999;
RA   Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
RT   "Amino acid residues in the omega-minus region participate in cellular
RT   localization of yeast glycosylphosphatidylinositol-attached proteins.";
RL   J. Bacteriol. 181:3886-3889(1999).
RN   [4]
RP   FUNCTION.
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   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX   PubMed=19756047; DOI=10.1038/msb.2009.64;
RA   Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT   "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT   new roles for protein glycosylation in eukaryotes.";
RL   Mol. Syst. Biol. 5:308-308(2009).
CC   -!- FUNCTION: Cleaves proteins C-terminally to mono- and paired-basic
CC       residues (By similarity). Required for cell wall integrity.
CC       {ECO:0000250, ECO:0000269|PubMed:16087741}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10383953};
CC       Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:10383953}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; Z38061; CAA86199.1; -; Genomic_DNA.
DR   EMBL; Z46902; CAA86998.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08586.1; -; Genomic_DNA.
DR   PIR; S50344; S50344.
DR   RefSeq; NP_012305.3; NM_001179561.3.
DR   AlphaFoldDB; P40583; -.
DR   SMR; P40583; -.
DR   BioGRID; 35030; 68.
DR   DIP; DIP-2688N; -.
DR   IntAct; P40583; 3.
DR   MINT; P40583; -.
DR   STRING; 4932.YIR039C; -.
DR   MEROPS; A01.030; -.
DR   MEROPS; A01.A62; -.
DR   GlyCosmos; P40583; 11 sites, No reported glycans.
DR   MaxQB; P40583; -.
DR   PaxDb; 4932-YIR039C; -.
DR   PeptideAtlas; P40583; -.
DR   EnsemblFungi; YIR039C_mRNA; YIR039C; YIR039C.
DR   GeneID; 854857; -.
DR   KEGG; sce:YIR039C; -.
DR   AGR; SGD:S000001478; -.
DR   SGD; S000001478; YPS6.
DR   VEuPathDB; FungiDB:YIR039C; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000166661; -.
DR   HOGENOM; CLU_013253_9_1_1; -.
DR   InParanoid; P40583; -.
DR   OMA; LDGHYYH; -.
DR   OrthoDB; 615305at2759; -.
DR   BioCyc; YEAST:G3O-31451-MONOMER; -.
DR   BioGRID-ORCS; 854857; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40583; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40583; Protein.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 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:SF12; ASPARTIC PROTEINASE 3-RELATED; 1.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Cell membrane; Cleavage on pair of basic residues;
KW   Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease;
KW   Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..52
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025844"
FT   CHAIN           53..515
FT                   /note="Aspartic proteinase yapsin-6"
FT                   /id="PRO_0000025845"
FT   PROPEP          516..537
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025846"
FT   DOMAIN          67..426
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   LIPID           515
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   537 AA;  58214 MW;  80C14D25D49D32CE CRC64;
     MQLISILSLL SSLMCSLTVL GSSASSYVKF PVQKLADIIN ICTQDVSTVF KRNEVLNTTV
     INGIGVYVVK MEIGTPPQTL YLQLDTGSSD MIVNNADIAY CKSMSDGSDY ASTDNYELTA
     TFNGLPSTTI SSEAYNTLCS YWGTFDASNS STFENNATFF NNTYGDGTYY AGTYGTDVVS
     FENITLNDFT FGVSNDTIGN PSGILGISLP IAEFTDGIEY ALALNRTPFI YDNFPMELKN
     QGKINKIAYS LFLNGPDAHF GSILFGAVDK SKYTGQLYTL PMLQAFNTLG SNPGMIITAQ
     SVAILDSESG NKTVSDIQFP VMLDSGTTFS YLPTEIAEAI GKSFDGEYSS DDQGYIFDCS
     KVNDTLLSVD FGGFNISANI SNFVTSAKDR CVLNVKQSES TYMLGDAFLV DAYVVYDLEN
     YEISIAQASF NNQEEDIEVI SDTVPGATPA PGYFSTWVYK PGSPIGTGDF INVSWTSYSE
     FSQYKSLLAT AAQSDDASSF SSSGGSSEST TKKQNAGYKY RSSFSFSLLS FISYFLL
//
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