MCA1_ARATH
ID MCA1_ARATH Reviewed; 367 AA.
AC Q7XJE6; O81911;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Metacaspase-1;
DE Short=AtMC1;
DE EC=3.4.22.-;
DE AltName: Full=Metacaspase 1b;
DE Short=AtMCP1b;
DE AltName: Full=Protein LSD ONE LIKE 3;
GN Name=AMC1; Synonyms=LOL3, MCP1B; OrderedLocusNames=At1g02170;
GN ORFNames=T7I23.17;
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], GENE FAMILY, AND NOMENCLATURE.
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 (JUN-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 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 [6]
RP FUNCTION, AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF CYS-220.
RX PubMed=15691845; DOI=10.1074/jbc.m413527200;
RA Watanabe N., Lam E.;
RT "Two Arabidopsis metacaspases AtMCP1b and AtMCP2b are arginine/lysine-
RT specific cysteine proteases and activate apoptosis-like cell death in
RT yeast.";
RL J. Biol. Chem. 280:14691-14699(2005).
RN [7]
RP FUNCTION, INTERACTION WITH LSD1, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-220.
RX PubMed=21097903; DOI=10.1126/science.1194980;
RA Coll N.S., Vercammen D., Smidler A., Clover C., Van Breusegem F.,
RA Dangl J.L., Epple P.;
RT "Arabidopsis type I metacaspases control cell death.";
RL Science 330:1393-1397(2010).
CC -!- FUNCTION: Cysteine protease that cleaves specifically after arginine or
CC lysine residues. Does not cleave caspase-specific substrates. Acts as a
CC positive regulator of cell death. Required for both oxidative stress
CC cell death response and hypersensitive cell death response mediated by
CC immune response. {ECO:0000269|PubMed:15691845,
CC ECO:0000269|PubMed:21097903}.
CC -!- SUBUNIT: Interacts (via N-terminus) with LSD1.
CC {ECO:0000269|PubMed:21097903}.
CC -!- INTERACTION:
CC Q7XJE6; P94077: LSD1; NbExp=3; IntAct=EBI-5849501, EBI-5849461;
CC -!- PTM: Proteolytically processed; by an autocatalytic mechanism.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but suppression of hypersensitive cell death response upon
CC infection with avirulent pathogen. {ECO:0000269|PubMed:21097903}.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24380.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY219826; AAP44514.1; -; mRNA.
DR EMBL; AY322525; AAP84706.1; -; mRNA.
DR EMBL; U89959; AAC24380.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27396.1; -; Genomic_DNA.
DR RefSeq; NP_171719.2; NM_100097.5.
DR AlphaFoldDB; Q7XJE6; -.
DR SMR; Q7XJE6; -.
DR BioGRID; 24796; 12.
DR IntAct; Q7XJE6; 13.
DR STRING; 3702.AT1G02170.1; -.
DR MEROPS; C14.047; -.
DR MetOSite; Q7XJE6; -.
DR PaxDb; Q7XJE6; -.
DR PRIDE; Q7XJE6; -.
DR ProteomicsDB; 238821; -.
DR EnsemblPlants; AT1G02170.1; AT1G02170.1; AT1G02170.
DR GeneID; 839561; -.
DR Gramene; AT1G02170.1; AT1G02170.1; AT1G02170.
DR KEGG; ath:AT1G02170; -.
DR Araport; AT1G02170; -.
DR TAIR; locus:2204798; AT1G02170.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_2_4_1; -.
DR InParanoid; Q7XJE6; -.
DR OMA; DFRTAGH; -.
DR OrthoDB; 821819at2759; -.
DR PhylomeDB; Q7XJE6; -.
DR PRO; PR:Q7XJE6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7XJE6; baseline and differential.
DR Genevisible; Q7XJE6; AT.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IDA:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033180; Metacaspase_type_1_plant.
DR InterPro; IPR005735; Znf_LSD1.
DR PANTHER; PTHR48104:SF32; PTHR48104:SF32; 1.
DR Pfam; PF06943; zf-LSD1; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR TIGRFAMs; TIGR01053; LSD1; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Hydrolase; Plant defense; Protease;
KW Reference proteome; Thiol protease.
FT CHAIN 1..367
FT /note="Metacaspase-1"
FT /id="PRO_0000334599"
FT REGION 47..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..71
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT MUTAGEN 220
FT /note="C->A: Loss of autoprocessing and cell death
FT regulatory function."
FT /evidence="ECO:0000269|PubMed:15691845,
FT ECO:0000269|PubMed:21097903"
SQ SEQUENCE 367 AA; 39792 MW; 98DCC44A986E0C5A CRC64;
MYPPPPSSIY APPMLVNCSG CRTPLQLPSG ARSIRCALCQ AVTHIADPRT APPPQPSSAP
SPPPQIHAPP GQLPHPHGRK RAVICGISYR FSRHELKGCI NDAKCMRHLL INKFKFSPDS
ILMLTEEETD PYRIPTKQNM RMALYWLVQG CTAGDSLVFH YSGHGSRQRN YNGDEVDGYD
ETLCPLDFET QGMIVDDEIN ATIVRPLPHG VKLHSIIDAC HSGTVLDLPF LCRMNRAGQY
VWEDHRPRSG LWKGTAGGEA ISISGCDDDQ TSADTSALSK ITSTGAMTFC FIQAIERSAQ
GTTYGSLLNS MRTTIRNTGN DGGGSGGVVT TVLSMLLTGG SAIGGLRQEP QLTACQTFDV
YAKPFTL
