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Barrierpepsin (EC 3.4.23.35) (BAR proteinase) (Extracellular 'barrier' protein)

 BAR1_YEAST              Reviewed;         587 AA.
P12630; D6VVR4;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
22-NOV-2017, entry version 158.
RecName: Full=Barrierpepsin;
EC=3.4.23.35;
AltName: Full=BAR proteinase;
AltName: Full=Extracellular 'barrier' protein;
Flags: Precursor;
Name=BAR1; Synonyms=SST1; OrderedLocusNames=YIL015W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3124102; DOI=10.1073/pnas.85.1.55;
Mackay V.L., Welch S.K., Insley M.Y., Manney T.R., Holly J.,
Saari G.C., Parker M.L.;
"The Saccharomyces cerevisiae BAR1 gene encodes an exported protein
with homology to pepsin.";
Proc. Natl. Acad. Sci. U.S.A. 85:55-59(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
-!- FUNCTION: This protein called "barrier activity" is excreted by
yeast cells mating type a. It is probably a protease that cleaves
alpha-factor and thus acts as an antagonist of this mating
pheromone and establishes optimal pheromone concentration for
conjugation.
-!- CATALYTIC ACTIVITY: Selective cleavage of 6-Leu-|-Lys-7 bond in
the pheromone alpha-mating factor.
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: By alpha factor.
-!- MISCELLANEOUS: It is found only in a mating type cells.
-!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z46881; CAA86977.1; -; Genomic_DNA.
EMBL; J03573; AAA34451.1; -; Genomic_DNA.
EMBL; BK006942; DAA08530.1; -; Genomic_DNA.
PIR; A34084; A34084.
RefSeq; NP_012249.1; NM_001179365.1.
ProteinModelPortal; P12630; -.
BioGrid; 34973; 87.
IntAct; P12630; 1.
MINT; MINT-2782575; -.
STRING; 4932.YIL015W; -.
MEROPS; A01.015; -.
MaxQB; P12630; -.
PRIDE; P12630; -.
EnsemblFungi; YIL015W; YIL015W; YIL015W.
GeneID; 854797; -.
KEGG; sce:YIL015W; -.
EuPathDB; FungiDB:YIL015W; -.
SGD; S000001277; BAR1.
GeneTree; ENSGT00550000075429; -.
HOGENOM; HOG000074716; -.
InParanoid; P12630; -.
KO; K01383; -.
OMA; ITETIDC; -.
OrthoDB; EOG092C3KPP; -.
BioCyc; YEAST:G3O-31291-MONOMER; -.
PRO; PR:P12630; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IDA:SGD.
GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:SGD.
GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IDA:SGD.
GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
GO; GO:0043171; P:peptide catabolic process; IDA:SGD.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
CDD; cd05474; SAP_like; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR033876; SAP-like.
PANTHER; PTHR13683; PTHR13683; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Aspartyl protease; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Pheromone response; Protease; Reference proteome; Secreted;
Signal.
SIGNAL 1 24
CHAIN 25 587 Barrierpepsin.
/FTId=PRO_0000025834.
DOMAIN 45 393 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 63 63 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 287 287 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 503 503 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 322 358 {ECO:0000250}.
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


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