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YPS7_YEAST
ID   YPS7_YEAST              Reviewed;         596 AA.
AC   Q06325; D6VSX9; Q66RD4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Aspartic proteinase yapsin-7;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=YPS7; OrderedLocusNames=YDR349C;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
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   [6]
RP   IDENTIFICATION.
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).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 149 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; U28372; AAB64785.1; -; Genomic_DNA.
DR   EMBL; AY723792; AAU09709.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12189.1; -; Genomic_DNA.
DR   PIR; S61146; S61146.
DR   RefSeq; NP_010636.1; NM_001180657.1.
DR   AlphaFoldDB; Q06325; -.
DR   SMR; Q06325; -.
DR   BioGRID; 32405; 80.
DR   DIP; DIP-5244N; -.
DR   IntAct; Q06325; 2.
DR   STRING; 4932.YDR349C; -.
DR   MEROPS; A01.097; -.
DR   MaxQB; Q06325; -.
DR   PaxDb; Q06325; -.
DR   PRIDE; Q06325; -.
DR   EnsemblFungi; YDR349C_mRNA; YDR349C; YDR349C.
DR   GeneID; 851950; -.
DR   KEGG; sce:YDR349C; -.
DR   SGD; S000002757; YPS7.
DR   VEuPathDB; FungiDB:YDR349C; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000166661; -.
DR   HOGENOM; CLU_023427_0_0_1; -.
DR   InParanoid; Q06325; -.
DR   OMA; GYPIVPL; -.
DR   BioCyc; YEAST:G3O-29903-MON; -.
DR   PRO; PR:Q06325; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q06325; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component 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; IBA:GO_Central.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47965; PTHR47965; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW   Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..596
FT                   /note="Aspartic proteinase yapsin-7"
FT                   /id="PRO_0000270564"
FT   TOPO_DOM        26..575
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        576..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          56..440
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        321
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        549
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        552
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        299
FT                   /note="I -> V (in Ref. 3; AAU09709)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   596 AA;  64498 MW;  E7F4C5BB33FC28CA CRC64;
     MTCLILWYLW LISTFQLEFA TASTANTTTT AKSGTSSSTE EPFPVLAVGK DGRGNYYVNS
     TFGTPGQRQR LLVDIIQPYI NLVSGTSESH NEYSGVYHKH PSYLMNDSTS SVPVSPGQIY
     EISFIDGRAV NCTLVTDDMN FTNVSSENSS TALITDLMVT RDNVQFNSGS LSISNVSFFD
     IQSSNFKTSG LLGLSGKVTN PGNAIDSSQY TEQSYFLSLL KDADIIESSS YSLWLAGDTS
     TYKTYRDPIS NCGKLLLGGV DPSLFTGTLG KFDLIPYVDP VSNAVSVGYP IVPLGPIYIV
     SNSGQSLNMT SKDFLSPALL DSTSSVSYLP TSTIIQIAVQ IAATYVESLD RWLVQCSIAD
     MGVSLGFRLR ELTIEIPLRD LLSSTYDTST NSSMFFSSGQ EACFLTLYAN TNTGVNILGE
     AFIKNIYMAM DLEDNTIAIA QAKKVEDDAV TEETNETTAS TIIKKIKSGY IPYAKVMNSS
     NTRNLTLYPS YRSGYMFTVP GQLTAAYSNG VITGAGRSFY DTSRASTSAR PSSTQFDSFS
     VSASEEWSNS TNRTSSASGA GVRLSSPYTF NKDPAGHVTR IASLLLLSIF SILIVL
 
 
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