MCA3C_PHATC
ID MCA3C_PHATC Reviewed; 337 AA.
AC B7G6D3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Metacaspase III c {ECO:0000303|PubMed:34566902};
DE Short=PtMCA-IIIc {ECO:0000303|PubMed:34566902};
DE EC=3.4.22.- {ECO:0000269|PubMed:34566902};
DE Contains:
DE RecName: Full=Small subunit p10 {ECO:0000305|PubMed:34566902};
DE Contains:
DE RecName: Full=Large subunit p20 {ECO:0000305|PubMed:34566902};
GN Name=MCA-IIIc {ECO:0000303|PubMed:34566902};
GN ORFNames=PHATRDRAFT_54873 {ECO:0000312|EMBL:EEC45993.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484 {ECO:0000312|Proteomes:UP000000759};
RN [1] {ECO:0000312|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000312|Proteomes:UP000000759};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2] {ECO:0000312|Proteomes:UP000000759}
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1 {ECO:0000312|Proteomes:UP000000759};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PROTEOLYTIC CLEAVAGE,
RP DISULFIDE BOND, OXIDATION AT CYS-202, MUTAGENESIS OF CYS-202; CYS-259 AND
RP CYS-264, AND CORRECTION OF N-TERMINUS.
RX PubMed=34566902; DOI=10.3389/fmicb.2021.688199;
RA Graff van Creveld S., Ben-Dor S., Mizrachi A., Alcolombri U., Hopes A.,
RA Mock T., Rosenwasser S., Vardi A.;
RT "Biochemical Characterization of a Novel Redox-Regulated Metacaspase in a
RT Marine Diatom.";
RL Front. Microbiol. 12:688199-688199(2021).
CC -!- FUNCTION: Cysteine protease that cleaves specifically after arginine
CC residues. {ECO:0000269|PubMed:34566902}.
CC -!- ACTIVITY REGULATION: Activated by Ca(2+).
CC {ECO:0000269|PubMed:34566902}.
CC -!- PTM: Auto-proteolytic cleavage into a large and a small subunit which
CC probably remain associated by non-covalent bonds.
CC {ECO:0000269|PubMed:34566902}.
CC -!- PTM: Following oxidative stress, the oxidation of Cys-202 leads to the
CC formation of a disulfide bond between Cys-202 and Cys-259 which
CC enhances catalytic activity. {ECO:0000269|PubMed:34566902}.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
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DR EMBL; CM000618; EEC45993.1; -; Genomic_DNA.
DR RefSeq; XP_002182706.1; XM_002182670.1.
DR STRING; 2850.Phatr54873; -.
DR PRIDE; B7G6D3; -.
DR GeneID; 7203528; -.
DR KEGG; pti:PHATRDRAFT_54873; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_058143_0_0_1; -.
DR InParanoid; B7G6D3; -.
DR OrthoDB; 821819at2759; -.
DR Proteomes; UP000000759; Chromosome 16.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR SUPFAM; SSF52129; SSF52129; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Disulfide bond; Hydrolase; Metal-binding;
KW Oxidation; Protease; Reference proteome; Thiol protease; Zymogen.
FT CHAIN 1..337
FT /note="Metacaspase III c"
FT /id="PRO_0000454698"
FT PROPEP 1..6
FT /evidence="ECO:0000305"
FT /id="PRO_0000454699"
FT CHAIN 7..115
FT /note="Small subunit p10"
FT /evidence="ECO:0000305|PubMed:34566902"
FT /id="PRO_0000454700"
FT PROPEP 116..125
FT /evidence="ECO:0000305"
FT /id="PRO_0000454701"
FT CHAIN 126..289
FT /note="Large subunit p20"
FT /evidence="ECO:0000305|PubMed:34566902"
FT /id="PRO_0000454702"
FT PROPEP 290..337
FT /evidence="ECO:0000305"
FT /id="PRO_0000454703"
FT ACT_SITE 207
FT /evidence="ECO:0000250|UniProtKB:Q08601"
FT ACT_SITE 264
FT /evidence="ECO:0000250|UniProtKB:Q585F3"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q585F3"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q585F3"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q585F3"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q585F3"
FT MOD_RES 202
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:34566902"
FT DISULFID 202..259
FT /evidence="ECO:0000305|PubMed:34566902"
FT MUTAGEN 202
FT /note="C->S: Severe reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:34566902"
FT MUTAGEN 259
FT /note="C->S: Severe reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:34566902"
FT MUTAGEN 264
FT /note="C->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:34566902"
SQ SEQUENCE 337 AA; 37250 MW; 009DFB8C9211AF52 CRC64;
MGFLRRQLRE QFEKKKPEAL QADIRMISGC QDVQTSADVS NVSSFQLPDP AGNAGGACTS
TLLNVLYKDH QTPEDTMSFV ELLNKMRENL EAKGFSQVPQ LTASHPIDVN DDFDLVPPAA
TGTRRALLIG INYVGHEQGV LRGCHNDVKN MVEYIKAVHG FEDENITILM DDGEHTAPTH
ANMIAAYKKI VALSKADDAL FCHFSGHGAK IRDDDRGEED DGYDETLVPI DYHENGMIRD
DDLYDILIKP LVQGVHLVCL MDCCHSGTVL DLPYVYKADG NFTEMEIDEN FDFKKLLGKF
GIDDFDKFGG EALGKINGDA LGKVGKDALG KLNKFFG
