IED ID | IndEnz0002006856 |
Enzyme Type ID | protease006856 |
Protein Name |
Metacaspase-1 EC 3.4.22.- Cleaved into: Large subunit p20; Small subunit p10 |
Gene Name | MCA1 YCA1 YOR197W |
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 | MYPGSGRYTYNNAGGNNGYQRPMAPPPNQQYGQQYGQQYEQQYGQQYGQQNDQQFSQQYAPPPGPPPMAYNRPVYPPPQFQQEQAKAQLSNGYNNPNVNASNMYGPPQNMSLPPPQTQTIQGTDQPYQYSQCTGRRKALIIGINYIGSKNQLRGCINDAHNIFNFLTNGYGYSSDDIVILTDDQNDLVRVPTRANMIRAMQWLVKDAQPNDSLFLHYSGHGGQTEDLDGDEEDGMDDVIYPVDFETQGPIIDDEMHDIMVKPLQQGVRLTALFDSCHSGTVLDLPYTYSTKGIIKEPNIWKDVGQDGLQAAISYATGNRAALIGSLGSIFKTVKGGMGNNVDRERVRQIKFSAADVVMLSGSKDNQTSADAVEDGQNTGAMSHAFIKVMTLQPQQSYLSLLQNMRKELAGKYSQKPQLSSSHPIDVNLQFIM |
Enzyme Length | 432 |
Uniprot Accession Number | Q08601 |
Absorption | |
Active Site | ACT_SITE 220; /evidence="ECO:0000305|PubMed:22761449"; ACT_SITE 276; /evidence="ECO:0000305|PubMed:11983181, ECO:0000305|PubMed:22761449" |
Activity Regulation | ACTIVITY REGULATION: Activated by Ca(2+) which induces self-processing and is required for the activity of the mature enzyme. {ECO:0000269|PubMed:22761449}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Cysteine protease that cleaves specifically after arginine or lysine residues (PubMed:22761449). Mediates cell death (apoptosis) triggered by oxygen stress, salt stress or chronological aging. Regulated cell death can prevent a release of toxic cellular components, thus avoiding necrotic collapse of the colony, and can also provide nutrients for healthy cells. Therefore, regulated cell death in yeast colonies can be as important for their development as are apoptosis and related processes that occur within metazoa. Promotes the removal of insoluble protein aggregates during normal growth. {ECO:0000269|PubMed:11983181, ECO:0000269|PubMed:14718573, ECO:0000269|PubMed:14970189, ECO:0000269|PubMed:15381687, ECO:0000269|PubMed:15489197, ECO:0000269|PubMed:15668299, ECO:0000269|PubMed:15939758, ECO:0000269|PubMed:16079294, ECO:0000269|PubMed:16170310, ECO:0000269|PubMed:16301538, ECO:0000269|PubMed:20624963, ECO:0000269|PubMed:22761449}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (12); Chain (3); Compositional bias (1); Erroneous initiation (2); Helix (8); Mutagenesis (6); Propeptide (1); Region (2); Site (4); Turn (4) |
Keywords | 3D-structure;Apoptosis;Cytoplasm;Direct protein sequencing;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. |
Modified Residue | |
Post Translational Modification | PTM: Proteolytic cleavage of the propeptide appears to occur after Arg-72 and/or Lys-86; it is not clear how the processing takes place (PubMed:11983181, PubMed:22761449). Proteolytic cleavage after Lys-331 generates a large (p20) and a small (p10) subunits (PubMed:22761449). The small subunit may be further cleaved to give rise to a shorter product starting at Gly-335 (PubMed:22761449). {ECO:0000269|PubMed:11983181, ECO:0000269|PubMed:22761449}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 4F6O; 4F6P; |
Mapped Pubmed ID | 10688190; 11283351; 11743162; 12062425; 12172961; 12297273; 14690591; 15489192; 15489193; 15525523; 15527405; 15556039; 15668005; 15670835; 15691845; 16387872; 16399892; 16420350; 16554755; 16738305; 16784770; 17087770; 17090424; 17107676; 17156009; 17156780; 17207637; 17244531; 17453165; 17507672; 17530929; 17615299; 17627776; 17881727; 17967946; 18162582; 18291112; 18319066; 18342634; 18355271; 18355456; 18358844; 18440231; 18445486; 18463984; 18474590; 18656474; 18698411; 18719252; 18782613; 18789900; 19066445; 19144191; 19160457; 19250922; 19416362; 19507234; 19536198; 19797862; 19841731; 19926288; 19941863; 20071174; 20075938; 20213854; 20222011; 20360952; 20370607; 20383156; 20460436; 20491936; 20721547; 20726897; 20726898; 20811357; 20931186; 20950655; 21317551; 21339834; 21397710; 21471218; 21717344; 21756235; 21772325; 21814286; 21836634; 21886177; 21912212; 21936842; 21936845; 22094424; 22094426; 22155640; 22188402; 22209905; 22337769; 22454613; 22586098; 22615903; 22737670; 22754872; 22783546; 22817540; 22876361; 22891165; 22993213; 23062268; 23072389; 23202731; 23282100; 23376483; 23430312; 23656787; 23672235; 23911092; 23943356; 24028627; 24305165; 24393541; 24437935; 24497836; 24731805; 24855027; 24948721; 25065265; 25159848; 25416836; 25483081; 25677381; 25697364; 26004510; 26032856; 26269384; 26272996; 26317359; 26636650; 26833421; 26904057; 26995056; 27048816; 27160815; 27450768; 27507670; 27540414; 27616453; 28012059; |
Motif | |
Gene Encoded By | |
Mass | 47,982 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |