MCA6_ARATH
ID MCA6_ARATH Reviewed; 368 AA.
AC O64519;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Metacaspase-6;
DE Short=AtMC6;
DE EC=3.4.22.-;
DE AltName: Full=Metacaspase 2c;
DE Short=AtMCP2c;
DE AltName: Full=Metacaspase-5;
GN Name=AMC6; Synonyms=AMC5, MCP2C; OrderedLocusNames=At1g79320;
GN ORFNames=YUP8H12R.6;
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], AUTOCATALYTIC CLEAVAGE, GENE FAMILY, AND
RP 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 TISSUE SPECIFICITY.
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 -!- TISSUE SPECIFICITY: Expressed in roots and flower buds.
CC {ECO:0000269|PubMed:21395887}.
CC -!- PTM: Proteolytically processed; by an autocatalytic mechanism.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
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DR EMBL; AY219831; AAP44519.1; -; mRNA.
DR EMBL; AY322532; AAP84713.1; -; mRNA.
DR EMBL; AC002986; AAC17078.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36230.1; -; Genomic_DNA.
DR EMBL; BT029232; ABJ98564.1; -; mRNA.
DR PIR; T01023; T01023.
DR RefSeq; NP_178050.1; NM_106580.2.
DR AlphaFoldDB; O64519; -.
DR SMR; O64519; -.
DR STRING; 3702.AT1G79320.1; -.
DR MEROPS; C14.A01; -.
DR PaxDb; O64519; -.
DR PRIDE; O64519; -.
DR ProteomicsDB; 238285; -.
DR EnsemblPlants; AT1G79320.1; AT1G79320.1; AT1G79320.
DR GeneID; 844270; -.
DR Gramene; AT1G79320.1; AT1G79320.1; AT1G79320.
DR KEGG; ath:AT1G79320; -.
DR Araport; AT1G79320; -.
DR TAIR; locus:2207440; AT1G79320.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_4_1_1; -.
DR InParanoid; O64519; -.
DR OMA; DAHVKNR; -.
DR OrthoDB; 792090at2759; -.
DR PhylomeDB; O64519; -.
DR PRO; PR:O64519; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64519; baseline and differential.
DR Genevisible; O64519; AT.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Hydrolase; Protease; Reference proteome;
KW S-nitrosylation; Thiol protease.
FT CHAIN 1..368
FT /note="Metacaspase-6"
FT /id="PRO_0000334604"
FT REGION 153..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /evidence="ECO:0000250"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT MOD_RES 139
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYE1"
SQ SEQUENCE 368 AA; 40242 MW; 0805E526F9420D33 CRC64;
MAKKALLIGI NYVGTKAELR GCVNDVRRMR ISLVERYGFS EENIKMLIDT DSSSIKPTGK
NIRQALLDLV EPAKSGDVLF VHYSGHGTRL PAETGEDDDT GYDECIVPSD MNLITDDDFR
DLVDMVPKDC PITIISDSCH SGGLIDEAKE QIGESTKKKK DSGDSSTINK ETEAEIIEVG
NRSLPLETLI DMLKQETGND DIEVGKIRTT LFDMFGDDSS PKVKKFMNVI LSNLQETTTT
IQTVSDEVLG SVENLAQEFL EQKLSDDVKP AIQDVYAGAI NGALPDNGIL ISGCQTDQTS
SDASPPGHPE LAYGALTNAI QIIIGETKGK ISNKDLVLKA RKLLRKQGFD QRPGLYCNDA
YVNARFIC