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 03-AUG-2022, entry version 169.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 MaxQB; P40583; -.
DR PaxDb; P40583; -.
DR EnsemblFungi; YIR039C_mRNA; YIR039C; YIR039C.
DR GeneID; 854857; -.
DR KEGG; sce:YIR039C; -.
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; SEGTFCF; -.
DR BioCyc; YEAST:G3O-31451-MON; -.
DR PRO; PR:P40583; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40583; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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; IBA:GO_Central.
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; 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
