ID   BAR1_YEAST              Reviewed;         587 AA.
AC   P12630; D6VVR4;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Barrierpepsin;
DE            EC=3.4.23.35;
DE   AltName: Full=BAR proteinase;
DE   AltName: Full=Extracellular 'barrier' protein;
DE   Flags: Precursor;
GN   Name=BAR1; Synonyms=SST1; OrderedLocusNames=YIL015W;
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 [GENOMIC DNA].
RX   PubMed=3124102; DOI=10.1073/pnas.85.1.55;
RA   Mackay V.L., Welch S.K., Insley M.Y., Manney T.R., Holly J., Saari G.C.,
RA   Parker M.L.;
RT   "The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with
RT   homology to pepsin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:55-59(1988).
RN   [2]
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   [3]
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   [4]
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).
CC   -!- FUNCTION: This protein called 'barrier activity' is excreted by yeast
CC       cells mating type a. It is probably a protease that cleaves alpha-
CC       factor and thus acts as an antagonist of this mating pheromone and
CC       establishes optimal pheromone concentration for conjugation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of 6-Leu-|-Lys-7 bond in the pheromone
CC         alpha-mating factor.; EC=3.4.23.35;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: By alpha factor.
CC   -!- MISCELLANEOUS: It is found only in a mating type cells.
CC   -!- MISCELLANEOUS: Present with 672 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; Z46881; CAA86977.1; -; Genomic_DNA.
DR   EMBL; J03573; AAA34451.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08530.1; -; Genomic_DNA.
DR   PIR; A34084; A34084.
DR   RefSeq; NP_012249.1; NM_001179365.1.
DR   AlphaFoldDB; P12630; -.
DR   SMR; P12630; -.
DR   BioGRID; 34973; 98.
DR   IntAct; P12630; 1.
DR   MINT; P12630; -.
DR   STRING; 4932.YIL015W; -.
DR   MEROPS; A01.015; -.
DR   GlyCosmos; P12630; 9 sites, No reported glycans.
DR   GlyGen; P12630; 9 sites.
DR   MaxQB; P12630; -.
DR   PaxDb; 4932-YIL015W; -.
DR   PeptideAtlas; P12630; -.
DR   EnsemblFungi; YIL015W_mRNA; YIL015W; YIL015W.
DR   GeneID; 854797; -.
DR   KEGG; sce:YIL015W; -.
DR   AGR; SGD:S000001277; -.
DR   SGD; S000001277; BAR1.
DR   VEuPathDB; FungiDB:YIL015W; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000166661; -.
DR   HOGENOM; CLU_013253_9_1_1; -.
DR   InParanoid; P12630; -.
DR   OMA; CMFGISP; -.
DR   OrthoDB; 615305at2759; -.
DR   BioCyc; YEAST:G3O-31291-MONOMER; -.
DR   BioGRID-ORCS; 854797; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P12630; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P12630; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IDA:SGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:SGD.
DR   GO; GO:0071444; P:cellular response to pheromone; IDA:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IDA: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:SF109; 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; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase;
KW   Pheromone response; Protease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT   CHAIN           25..587
FT                   /note="Barrierpepsin"
FT                   /id="PRO_0000025834"
FT   DOMAIN          45..393
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          466..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
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        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        468
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        322..358
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   587 AA;  63730 MW;  CC21DB7FDBC83984 CRC64;
     MSAINHLCLK LILASFAIIN TITALTNDGT GHLEFLLQHE EEMYYATTLD IGTPSQSLTV
     LFDTGSADFW VMDSSNPFCL PNSNTSSYSN ATYNGEEVKP SIDCRSMSTY NEHRSSTYQY
     LENGRFYITY ADGTFADGSW GTETVSINGI DIPNIQFGVA KYATTPVSGV LGIGFPRRES
     VKGYEGAPNE YYPNFPQILK SEKIIDVVAY SLFLNSPDSG TGSIVFGAID ESKFSGDLFT
     FPMVNEYPTI VDAPATLAMT IQGLGAQNKS SCEHETFTTT KYPVLLDSGT SLLNAPKVIA
     DKMASFVNAS YSEEEGIYIL DCPVSVGDVE YNFDFGDLQI SVPLSSLILS PETEGSYCGF
     AVQPTNDSMV LGDVFLSSAY VVFDLDNYKI SLAQANWNAS EVSKKLVNIQ TDGSISGAKI
     ATAEPWSTNE PFTVTSDIYS STGCKSRPFL QSSTASSLIA ETNVQSRNCS TKMPGTRSTT
     VLSKPTQNSA MHQSTGAVTQ TSNETKLELS STMANSGSVS LPTSNSIDKE FEHSKSQTTS
     DPSVAEHSTF NQTFVHETKY RPTHKTVITE TVTKYSTVLI NVCKPTY
//