BAR1_YEAST
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 03-AUG-2022, entry version 185.
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; 89.
DR IntAct; P12630; 1.
DR MINT; P12630; -.
DR STRING; 4932.YIL015W; -.
DR MEROPS; A01.015; -.
DR MaxQB; P12630; -.
DR PaxDb; P12630; -.
DR PRIDE; P12630; -.
DR EnsemblFungi; YIL015W_mRNA; YIL015W; YIL015W.
DR GeneID; 854797; -.
DR KEGG; sce:YIL015W; -.
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 BioCyc; YEAST:G3O-31291-MON; -.
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:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; 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; 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; 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
