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 10-MAY-2017, entry version 98. 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; GN ORFNames=F21E1.120; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA 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., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA 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., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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 RT inhibitor-1 in plants: their possible roles as regulator of programmed RT cell death."; RL Mol. Plant Pathol. 5:65-70(2004). RN [8] RP ENZYME 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 RT metacaspase 9."; RL J. Mol. Biol. 364:625-636(2006). RN [9] RP ENZYME 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., RA Inze D., 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 RT induced 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., RA Help-Rinta-Rahko H., Gauthier A., Kaufholdt D., Bollhoener B., RA Lamminmaeki A., Staes A., Gevaert K., Tuominen H., Van Breusegem F., RA Helariutta Y., Kangasjaervi J.; RT "GRIM REAPER peptide binds to receptor kinase PRK5 to trigger cell RT death in Arabidopsis."; RL EMBO J. 34:55-66(2015). CC -!- FUNCTION: Cysteine protease that cleaves specifically after CC arginine or lysine residues. Does not cleave caspase-specific CC substrates. Required for proteolytic processing of GRI CC (PubMed:25398910). {ECO:0000269|PubMed:25398910}. CC -!- ENZYME 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, CC flowers and siliques. {ECO:0000269|PubMed:17028019, CC ECO:0000269|PubMed:21395887}. CC -!- PTM: The two subunits are derived from the precursor sequence by CC an autocatalytic mechanism. CC -!- PTM: S-nitrosylation at Cys-147 suppresses both autoprocessing and CC proteolytic activity of the full length protein, but does not CC affect 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=Translation N-terminally extended.; 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 UniGene; At.27184; -. DR ProteinModelPortal; Q9FYE1; -. DR BioGrid; 15579; 74. DR STRING; 3702.AT5G04200.1; -. DR MEROPS; C14.034; -. DR iPTMnet; Q9FYE1; -. DR PaxDb; Q9FYE1; -. 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 eggNOG; ENOG410Y41C; LUCA. DR HOGENOM; HOG000238362; -. DR InParanoid; Q9FYE1; -. DR OMA; MERGQKK; -. DR OrthoDB; EOG09360BVN; -. 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 InterPro; IPR029030; Caspase-like_dom. DR SUPFAM; SSF52129; SSF52129; 1. PE 1: Evidence at protein level; KW Apoplast; Autocatalytic cleavage; Complete proteome; KW Direct protein sequencing; Glycoprotein; Hydrolase; Protease; KW Reference proteome; S-nitrosylation; Secreted; Thiol protease. FT CHAIN 1 325 Metacaspase-9. FT /FTId=PRO_0000334607. FT CHAIN 1 183 Metacaspase-9 subunit p20. FT /FTId=PRO_0000334608. FT CHAIN 184 325 Metacaspase-9 subunit p10. FT /FTId=PRO_0000334609. FT ACT_SITE 95 95 {ECO:0000250}. FT ACT_SITE 147 147 FT SITE 29 29 S-nitrosylation-insensitive cysteine; may FT replace the S-nitrosylated cysteine FT residue within the catalytic center (in FT mature processed form only). FT SITE 183 184 Cleavage; by autolysis. FT MOD_RES 147 147 S-nitrosocysteine. FT {ECO:0000269|PubMed:17110382}. FT CARBOHYD 177 177 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT MUTAGEN 29 29 C->A: Reduced proteolytic activity. FT MUTAGEN 147 147 C->A: Loss of autoprocessing and protease FT activity. {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 //