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 22-FEB-2023, entry version 122. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q9FYE1; 1 site, No reported glycans. DR iPTMnet; Q9FYE1; -. DR PaxDb; 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; 531483at2759; -. 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:TAIR. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.12660; -; 2. DR InterPro; IPR029030; Caspase-like_dom_sf. DR InterPro; IPR011600; Pept_C14_caspase. DR PANTHER; PTHR48104; METACASPASE-4; 1. DR PANTHER; PTHR48104:SF7; METACASPASE-9; 1. DR Pfam; PF00656; Peptidase_C14; 1. DR SUPFAM; SSF52129; Caspase-like; 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 //