| IED ID | IndEnz0002014487 |
| Enzyme Type ID | protease014487 |
| Protein Name |
Barrierpepsin EC 3.4.23.35 BAR proteinase Extracellular 'barrier' protein |
| Gene Name | BAR1 SST1 YIL015W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSAINHLCLKLILASFAIINTITALTNDGTGHLEFLLQHEEEMYYATTLDIGTPSQSLTVLFDTGSADFWVMDSSNPFCLPNSNTSSYSNATYNGEEVKPSIDCRSMSTYNEHRSSTYQYLENGRFYITYADGTFADGSWGTETVSINGIDIPNIQFGVAKYATTPVSGVLGIGFPRRESVKGYEGAPNEYYPNFPQILKSEKIIDVVAYSLFLNSPDSGTGSIVFGAIDESKFSGDLFTFPMVNEYPTIVDAPATLAMTIQGLGAQNKSSCEHETFTTTKYPVLLDSGTSLLNAPKVIADKMASFVNASYSEEEGIYILDCPVSVGDVEYNFDFGDLQISVPLSSLILSPETEGSYCGFAVQPTNDSMVLGDVFLSSAYVVFDLDNYKISLAQANWNASEVSKKLVNIQTDGSISGAKIATAEPWSTNEPFTVTSDIYSSTGCKSRPFLQSSTASSLIAETNVQSRNCSTKMPGTRSTTVLSKPTQNSAMHQSTGAVTQTSNETKLELSSTMANSGSVSLPTSNSIDKEFEHSKSQTTSDPSVAEHSTFNQTFVHETKYRPTHKTVITETVTKYSTVLINVCKPTY |
| Enzyme Length | 587 |
| Uniprot Accession Number | P12630 |
| Absorption | |
| Active Site | ACT_SITE 63; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 287; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of 6-Leu-|-Lys-7 bond in the pheromone alpha-mating factor.; EC=3.4.23.35; |
| DNA Binding | |
| EC Number | 3.4.23.35 |
| Enzyme Function | 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (9); Region (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Pheromone response;Protease;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: By alpha factor. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10690410; 15077905; 16467474; 16554755; 16574642; 1667085; 16738305; 16980406; 17587671; 17975704; 18303948; 18559484; 1903837; 19052645; 1915278; 19536198; 20066086; 20300644; 21072241; 21179020; 21496492; 21868361; 22261724; 22485574; 22816435; 23071457; 23450187; 24173508; 24967739; 25329559; 25474997; 26726837; 26884462; 26907689; 27077831; 27404800; 27557894; 3079238; 3301002; 391400; 6345506; 6397123; 7040681; 7050665; 7050666; 8364097; 9249020; 9853747; |
| Motif | |
| Gene Encoded By | |
| Mass | 63,730 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |