MCA4_ARATH
ID MCA4_ARATH Reviewed; 418 AA.
AC O64517; Q7XBI1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Metacaspase-4;
DE Short=AtMC4;
DE EC=3.4.22.-;
DE AltName: Full=Metacaspase 2d;
DE Short=AtMCP2d;
DE AltName: Full=Metacaspase-7;
DE Contains:
DE RecName: Full=Metacaspase-4 subunit p20;
DE Contains:
DE RecName: Full=Metacaspase-4 subunit p10;
GN Name=AMC4; Synonyms=AMC7, MCP2D; OrderedLocusNames=At1g79340;
GN ORFNames=YUP8H12R.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOCATALYTIC CLEAVAGE, GENE FAMILY,
RP NOMENCLATURE, AND MUTAGENESIS OF CYS-139.
RX PubMed=15326173; DOI=10.1074/jbc.m406329200;
RA Vercammen D., van de Cotte B., De Jaeger G., Eeckhout D., Casteels P.,
RA Vandepoele K., Vandenberghe I., van Beeumen J., Inze D., van Breusegem F.;
RT "Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave
RT substrates after arginine and lysine.";
RL J. Biol. Chem. 279:45329-45336(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ikeda Y., Krishnamurthy N., Chua N.-H.;
RT "Characterization of metacaspases.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP GENE FAMILY.
RX PubMed=20565583; DOI=10.1111/j.1364-3703.2004.00206.x;
RA Watanabe N., Lam E.;
RT "Recent advance in the study of caspase-like proteases and Bax inhibitor-1
RT in plants: their possible roles as regulator of programmed cell death.";
RL Mol. Plant Pathol. 5:65-70(2004).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AUTOCATALYTIC
RP CLEAVAGE, AND MUTAGENESIS OF CYS-139; ARG-190; LYS-225 AND LYS-271.
RX PubMed=21209078; DOI=10.1074/jbc.m110.194340;
RA Watanabe N., Lam E.;
RT "Calcium-dependent activation and autolysis of Arabidopsis metacaspase
RT 2d.";
RL J. Biol. Chem. 286:10027-10040(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21395887; DOI=10.1111/j.1365-313x.2011.04554.x;
RA Watanabe N., Lam E.;
RT "Arabidopsis metacaspase 2d is a positive mediator of cell death induced
RT during biotic and abiotic stresses.";
RL Plant J. 66:969-982(2011).
CC -!- FUNCTION: Cysteine protease that cleaves specifically after arginine or
CC lysine residues. Does not cleave caspase-specific substrates. Plays a
CC positive regulatory role in biotic and abiotic stress-induced
CC programmed cell death. {ECO:0000269|PubMed:15326173,
CC ECO:0000269|PubMed:21209078, ECO:0000269|PubMed:21395887}.
CC -!- ACTIVITY REGULATION: Activated by Ca(2+) which induces self-processing
CC and accelerates the rate of the enzyme activity, but has no effect on
CC Km. {ECO:0000269|PubMed:21209078}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=312 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the
CC presence of 2 mM Ca(2+)) {ECO:0000269|PubMed:21209078};
CC KM=292 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the
CC presence of 10 mM Ca(2+)) {ECO:0000269|PubMed:21209078};
CC KM=283 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the
CC presence of 50 mM Ca(2+)) {ECO:0000269|PubMed:21209078};
CC Vmax=0.53 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-
CC aminomethylcoumarin (in the presence of 2 mM Ca(2+))
CC {ECO:0000269|PubMed:21209078};
CC Vmax=2.28 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-
CC aminomethylcoumarin (in the presence of 10 mM Ca(2+))
CC {ECO:0000269|PubMed:21209078};
CC Vmax=4.37 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-
CC aminomethylcoumarin (in the presence of 50 mM Ca(2+))
CC {ECO:0000269|PubMed:21209078};
CC -!- INTERACTION:
CC O64517; O64517: AMC4; NbExp=4; IntAct=EBI-5889420, EBI-5889420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21395887}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, cauline
CC leaves, pollen and embryos. {ECO:0000269|PubMed:21395887}.
CC -!- PTM: The two subunits are derived from the precursor sequence by an
CC autocatalytic mechanism.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions, but reduced sensitivity to cell death induced by the
CC mycotoxin fumonisin B1, methyl viologen (oxidative stress) and
CC infection with an avirulent strain of P.syringae DC3000.
CC {ECO:0000269|PubMed:21395887}.
CC -!- MISCELLANEOUS: Plants overexpressing MCA4 are more sensitive to the
CC mycotoxin fumonisin B1 and methyl viologen (oxidative stress) and
CC exhibited accelerated cell-death progression.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
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DR EMBL; AY219829; AAP44517.1; -; mRNA.
DR EMBL; AY322529; AAP84710.2; -; mRNA.
DR EMBL; AC002986; AAC17081.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36232.1; -; Genomic_DNA.
DR EMBL; AY080746; AAL85992.1; -; mRNA.
DR EMBL; AY133847; AAM91781.1; -; mRNA.
DR PIR; T01021; T01021.
DR RefSeq; NP_178052.1; NM_106582.4.
DR PDB; 6W8R; X-ray; 2.80 A; A/B=1-418.
DR PDB; 6W8S; X-ray; 3.48 A; A/B/C/D=1-418.
DR PDB; 6W8T; X-ray; 3.20 A; A/B=1-418.
DR PDBsum; 6W8R; -.
DR PDBsum; 6W8S; -.
DR PDBsum; 6W8T; -.
DR AlphaFoldDB; O64517; -.
DR SMR; O64517; -.
DR STRING; 3702.AT1G79340.1; -.
DR MEROPS; C14.033; -.
DR iPTMnet; O64517; -.
DR PaxDb; O64517; -.
DR PRIDE; O64517; -.
DR ProteomicsDB; 238817; -.
DR EnsemblPlants; AT1G79340.1; AT1G79340.1; AT1G79340.
DR GeneID; 844272; -.
DR Gramene; AT1G79340.1; AT1G79340.1; AT1G79340.
DR KEGG; ath:AT1G79340; -.
DR Araport; AT1G79340; -.
DR TAIR; locus:2207350; AT1G79340.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_4_1_1; -.
DR InParanoid; O64517; -.
DR OMA; IGCNYQG; -.
DR OrthoDB; 792090at2759; -.
DR PhylomeDB; O64517; -.
DR PRO; PR:O64517; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64517; baseline and differential.
DR Genevisible; O64517; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IDA:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR SUPFAM; SSF52129; SSF52129; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cytoplasm; Hydrolase; Plant defense;
KW Protease; Reference proteome; S-nitrosylation; Thiol protease.
FT CHAIN 1..418
FT /note="Metacaspase-4"
FT /id="PRO_0000334602"
FT CHAIN 1..225
FT /note="Metacaspase-4 subunit p20"
FT /id="PRO_0000411017"
FT CHAIN 226..418
FT /note="Metacaspase-4 subunit p10"
FT /id="PRO_0000411018"
FT REGION 153..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /evidence="ECO:0000250"
FT ACT_SITE 139
FT SITE 225..226
FT /note="Cleavage; by autolysis"
FT MOD_RES 139
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYE1"
FT MUTAGEN 139
FT /note="C->A: Loss of autoprocessing and protease activity."
FT /evidence="ECO:0000269|PubMed:15326173,
FT ECO:0000269|PubMed:21209078"
FT MUTAGEN 190
FT /note="R->G: No effect on protease activity."
FT /evidence="ECO:0000269|PubMed:21209078"
FT MUTAGEN 225
FT /note="K->G: Loss of autoprocessing."
FT /evidence="ECO:0000269|PubMed:21209078"
FT MUTAGEN 271
FT /note="K->G: No effect on protease activity."
FT /evidence="ECO:0000269|PubMed:21209078"
FT CONFLICT 203
FT /note="E -> V (in Ref. 1; AAP84710 and 2; AAP44517)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 78..91
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6W8T"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:6W8R"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:6W8S"
FT HELIX 284..302
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:6W8R"
FT HELIX 383..396
FT /evidence="ECO:0007829|PDB:6W8R"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:6W8R"
FT TURN 409..413
FT /evidence="ECO:0007829|PDB:6W8T"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:6W8R"
SQ SEQUENCE 418 AA; 45484 MW; F1E844F476FB51C4 CRC64;
MTKKAVLIGI NYPGTKAELR GCVNDVRRMY KCLVERYGFS EENITVLIDT DESSTQPTGK
NIRRALADLV ESADSGDVLV VHYSGHGTRL PAETGEDDDT GFDECIVPCD MNLITDDDFR
DLVDKVPPGC RMTIISDSCH SGGLIDEAKE QIGESTKKEA EDEDESEESS SRFGFRKFLR
SKVEGAIESR GFHIGGNKKD EDEAEEIETK EIELEDGETI HAKDKSLPLQ TLIDILKQQT
GNDNIEVGKI RPSLFDAFGD DSSPKVKKFM KVILGKLQAG NGEEGGLMGM LGKLASGFLE
GKLNDEDYVK PAMQTHVGSK EEVYAGGSRG SVPLPDSGIL ISGCQTDQTS ADATPAGKPT
EAYGAMSNSI QTILEETDGE ISNREMVTRA RKALKKQGFT QQPGLYCHDG YANAPFIC
