MCA9_ARATH
ID MCA9_ARATH Reviewed; 325 AA.
AC Q9FYE1; Q8LCR8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Metacaspase-9;
DE Short=AtMC9;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Metacaspase-9 subunit p20;
DE Contains:
DE RecName: Full=Metacaspase-9 subunit p10;
DE AltName: Full=Metacaspase 2f;
DE Short=AtMCP2f;
GN Name=AMC9; Synonyms=MCP2F; OrderedLocusNames=At5g04200; ORFNames=F21E1.120;
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], PROTEIN SEQUENCE OF 184-190, AUTOCATALYTIC
RP CLEAVAGE, GENE FAMILY, NOMENCLATURE, AND MUTAGENESIS OF CYS-147.
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17028019; DOI=10.1016/j.jmb.2006.09.010;
RA Vercammen D., Belenghi B., van de Cotte B., Beunens T., Gavigan J.-A.,
RA De Rycke R., Brackenier A., Inze D., Harris J.L., van Breusegem F.;
RT "Serpin1 of Arabidopsis thaliana is a suicide inhibitor for metacaspase
RT 9.";
RL J. Mol. Biol. 364:625-636(2006).
RN [9]
RP ACTIVITY REGULATION, AND S-NITROSYLATION AT CYS-147.
RX PubMed=17110382; DOI=10.1074/jbc.m608931200;
RA Belenghi B., Romero-Puertas M.C., Vercammen D., Brackenier A., Inze D.,
RA Delledonne M., van Breusegem F.;
RT "Metacaspase activity of Arabidopsis thaliana is regulated by S-
RT nitrosylation of a critical cysteine residue.";
RL J. Biol. Chem. 282:1352-1358(2007).
RN [10]
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).
RN [11]
RP FUNCTION.
RX PubMed=25398910; DOI=10.15252/embj.201488582;
RA Wrzaczek M., Vainonen J.P., Stael S., Tsiatsiani L., Help-Rinta-Rahko H.,
RA Gauthier A., Kaufholdt D., Bollhoener B., Lamminmaeki A., Staes A.,
RA Gevaert K., Tuominen H., Van Breusegem F., Helariutta Y., Kangasjaervi J.;
RT "GRIM REAPER peptide binds to receptor kinase PRK5 to trigger cell death in
RT Arabidopsis.";
RL EMBO J. 34:55-66(2015).
CC -!- FUNCTION: Cysteine protease that cleaves specifically after arginine or
CC lysine residues. Does not cleave caspase-specific substrates. Required
CC for proteolytic processing of GRI (PubMed:25398910).
CC {ECO:0000269|PubMed:25398910}.
CC -!- ACTIVITY REGULATION: Inhibited by serpin ZX and nitric oxide through
CC cysteine nitrosylation. {ECO:0000269|PubMed:17028019,
CC ECO:0000269|PubMed:17110382}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:17028019}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, cauline leaves, flowers and
CC siliques. {ECO:0000269|PubMed:17028019, ECO:0000269|PubMed:21395887}.
CC -!- PTM: The two subunits are derived from the precursor sequence by an
CC autocatalytic mechanism.
CC -!- PTM: S-nitrosylation at Cys-147 suppresses both autoprocessing and
CC proteolytic activity of the full-length protein, but does not affect
CC the activity of the mature processed form.
CC {ECO:0000269|PubMed:17110382}.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY219834; AAP44522.1; -; mRNA.
DR EMBL; AY322531; AAP84712.1; -; mRNA.
DR EMBL; AL391716; CAC05502.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90710.1; -; Genomic_DNA.
DR EMBL; AY063830; AAL36186.1; -; mRNA.
DR EMBL; AY091308; AAM14247.1; -; mRNA.
DR EMBL; AY086438; AAM63441.1; ALT_INIT; mRNA.
DR RefSeq; NP_196040.1; NM_120502.3.
DR AlphaFoldDB; Q9FYE1; -.
DR SMR; Q9FYE1; -.
DR BioGRID; 15579; 74.
DR STRING; 3702.AT5G04200.1; -.
DR MEROPS; C14.034; -.
DR iPTMnet; Q9FYE1; -.
DR PaxDb; Q9FYE1; -.
DR PRIDE; Q9FYE1; -.
DR ProteomicsDB; 238317; -.
DR DNASU; 830299; -.
DR EnsemblPlants; AT5G04200.1; AT5G04200.1; AT5G04200.
DR GeneID; 830299; -.
DR Gramene; AT5G04200.1; AT5G04200.1; AT5G04200.
DR KEGG; ath:AT5G04200; -.
DR Araport; AT5G04200; -.
DR TAIR; locus:2146648; AT5G04200.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_4_1_1; -.
DR InParanoid; Q9FYE1; -.
DR OMA; FDSQHIE; -.
DR OrthoDB; 792090at2759; -.
DR PhylomeDB; Q9FYE1; -.
DR PRO; PR:Q9FYE1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FYE1; baseline and differential.
DR Genevisible; Q9FYE1; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:TAIR.
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 Apoplast; Autocatalytic cleavage; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; S-nitrosylation; Secreted;
KW Thiol protease.
FT CHAIN 1..325
FT /note="Metacaspase-9"
FT /id="PRO_0000334607"
FT CHAIN 1..183
FT /note="Metacaspase-9 subunit p20"
FT /id="PRO_0000334608"
FT CHAIN 184..325
FT /note="Metacaspase-9 subunit p10"
FT /id="PRO_0000334609"
FT ACT_SITE 95
FT /evidence="ECO:0000250"
FT ACT_SITE 147
FT SITE 29
FT /note="S-nitrosylation-insensitive cysteine; may replace
FT the S-nitrosylated cysteine residue within the catalytic
FT center (in mature processed form only)"
FT SITE 183..184
FT /note="Cleavage; by autolysis"
FT MOD_RES 147
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:17110382"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 29
FT /note="C->A: Reduced proteolytic activity."
FT MUTAGEN 147
FT /note="C->A: Loss of autoprocessing and protease activity."
FT /evidence="ECO:0000269|PubMed:15326173"
SQ SEQUENCE 325 AA; 35505 MW; AB574D648EDF3E0E CRC64;
MDQQGMVKKR LAVLVGCNYP NTRNELHGCI NDVLAMKETI LSRFGFKQDD IEVLTDEPES
KVKPTGANIK AALRRMVDKA QAGSGDILFF HYSGHGTRIP SVKSAHPFKQ DEAIVPCDFN
LITDVDFREL VNQLPKGTSF TMISDSCHSG GLIDKEKEQI GPSSVSSNIS PAIETTNKTI
TSRALPFKAV LDHLSSLTGI TTSDIGTHLL ELFGRDAGLK FRLPAMDLMD LLETMTAREK
HVDSGILMSG CQADETSADV GVGNGKAYGA FSNAIQRVLN ENEGAMKNKQ LVMMARDVLE
RLGFHQHPCL YCSDQNADAT FLSQP
