RD21A_ARATH
ID RD21A_ARATH Reviewed; 462 AA.
AC P43297;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cysteine proteinase RD21A {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Protein RESPONSIVE TO DEHYDRATION 21 {ECO:0000303|PubMed:8325504};
DE Short=RD21 {ECO:0000303|PubMed:8325504};
DE Flags: Precursor;
GN Name=RD21A {ECO:0000303|PubMed:8325504}; OrderedLocusNames=At1g47128;
GN ORFNames=F2G19.31;
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 [GENOMIC DNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8325504; DOI=10.1016/0378-1119(93)90266-6;
RA Koizumi M., Yamaguchi-Shinozaki K., Tsuji H., Shinozaki K.;
RT "Structure and expression of two genes that encode distinct drought-
RT inducible cysteine proteinases in Arabidopsis thaliana.";
RL Gene 129:175-182(1993).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11577182; DOI=10.1093/pcp/pce144;
RA Hayashi Y., Yamada K., Shimada T., Matsushima R., Nishizawa N.K.,
RA Nishimura M., Hara-Nishimura I.;
RT "A proteinase-storing body that prepares for cell death or stresses in the
RT epidermal cells of Arabidopsis.";
RL Plant Cell Physiol. 42:894-899(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11743107; DOI=10.1104/pp.010551;
RA Yamada K., Matsushima R., Nishimura M., Hara-Nishimura I.;
RT "A slow maturation of a cysteine protease with a granulin domain in the
RT vacuoles of senescing Arabidopsis leaves.";
RL Plant Physiol. 127:1626-1634(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=18660805; DOI=10.1038/nchembio.104;
RA Wang Z., Gu C., Colby T., Shindo T., Balamurugan R., Waldmann H.,
RA Kaiser M., van der Hoorn R.A.;
RT "Beta-lactone probes identify a papain-like peptide ligase in Arabidopsis
RT thaliana.";
RL Nat. Chem. Biol. 4:557-563(2008).
RN [8]
RP INTERACTION WITH SERPIN1.
RX PubMed=20181955; DOI=10.1074/jbc.m109.095075;
RA Lampl N., Budai-Hadrian O., Davydov O., Joss T.V., Harrop S.J., Curmi P.M.,
RA Roberts T.H., Fluhr R.;
RT "Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its
RT target protease RESPONSIVE TO DESICCATION-21 (RD21).";
RL J. Biol. Chem. 285:13550-13560(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22238602; DOI=10.1371/journal.pone.0029317;
RA Shindo T., Misas-Villamil J.C., Hoerger A.C., Song J., van der Hoorn R.A.;
RT "A role in immunity for Arabidopsis cysteine protease RD21, the ortholog of
RT the tomato immune protease C14.";
RL PLoS ONE 7:E29317-E29317(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, ACTIVE SITE, SUBCELLULAR
RP LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF CYS-161; HIS-297 AND
RP ASN-317, AND DISRUPTION PHENOTYPE.
RX PubMed=22396764; DOI=10.1371/journal.pone.0032422;
RA Gu C., Shabab M., Strasser R., Wolters P.J., Shindo T., Niemer M.,
RA Kaschani F., Mach L., van der Hoorn R.A.;
RT "Post-translational regulation and trafficking of the granulin-containing
RT protease RD21 of Arabidopsis thaliana.";
RL PLoS ONE 7:E32422-E32422(2012).
RN [11]
RP FUNCTION, INTERACTION WITH SERPIN1, AND SUBCELLULAR LOCATION.
RX PubMed=23398119; DOI=10.1111/tpj.12141;
RA Lampl N., Alkan N., Davydov O., Fluhr R.;
RT "Set-point control of RD21 protease activity by AtSerpin1 controls cell
RT death in Arabidopsis.";
RL Plant J. 74:498-510(2013).
RN [12]
RP INTERACTION WITH PRN2.
RX PubMed=24947605; DOI=10.1111/tpj.12602;
RA Zhang B., Tremousaygue D., Denance N., van Esse H.P., Hoerger A.C.,
RA Dabos P., Goffner D., Thomma B.P., van der Hoorn R.A., Tuominen H.;
RT "PIRIN2 stabilizes cysteine protease XCP2 and increases susceptibility to
RT the vascular pathogen Ralstonia solanacearum in Arabidopsis.";
RL Plant J. 79:1009-1019(2014).
RN [13]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH WSCP.
RX PubMed=26160583; DOI=10.1093/jxb/erv327;
RA Boex-Fontvieille E., Rustgi S., Reinbothe S., Reinbothe C.;
RT "A Kunitz-type protease inhibitor regulates programmed cell death during
RT flower development in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:6119-6135(2015).
RN [14]
RP INTERACTION WITH WSCP.
RX PubMed=26016527; DOI=10.1073/pnas.1507714112;
RA Boex-Fontvieille E., Rustgi S., von Wettstein D., Reinbothe S.,
RA Reinbothe C.;
RT "Water-soluble chlorophyll protein is involved in herbivore resistance
RT activation during greening of Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7303-7308(2015).
RN [15]
RP FUNCTION.
RX PubMed=26884487; DOI=10.1104/pp.15.02026;
RA Koh E., Carmieli R., Mor A., Fluhr R.;
RT "Singlet oxygen induced membrane disruption and serpin-protease balance in
RT vacuolar driven cell death in Arabidopsis thaliana.";
RL Plant Physiol. 171:1616-1625(2016).
RN [16]
RP INTERACTION WITH TZF4; TZF5 AND TZF6, AND SUBCELLULAR LOCATION.
RX PubMed=26978070; DOI=10.1371/journal.pone.0151574;
RA Bogamuwa S., Jang J.C.;
RT "Plant tandem CCCH zinc finger proteins interact with ABA, drought, and
RT stress response regulators in processing-bodies and stress granules.";
RL PLoS ONE 11:E0151574-E0151574(2016).
CC -!- FUNCTION: Cysteine protease that plays a role in immunity, senescence,
CC and biotic and abiotic stresses (Probable). Involved in immunity
CC against the necrotrophic fungal pathogen Botrytis cinerea
CC (PubMed:22238602). Involved in elicitor-stimulated programmed cell
CC death (PCD). During infection by the necrotrophic fungal pathogen
CC Botrytis cinerea, functions as PCD-promoting protease that is released
CC from the ER body or vacuole to the cytoplasm (PubMed:23398119).
CC Accumulates in endoplasmic reticulum-derived bodies in epidermal cells
CC and may participate in cell death in stressed or injured cells
CC (PubMed:11577182). Involved in water stress-induced cell death through
CC its protease activity that is released to the cytoplasm after vacuolar
CC collapse (PubMed:26884487). Possesses protease activity in vitro and is
CC involved in cell death in the transmitting tract and septum epidermis
CC during flower development (PubMed:26160583). Possesses peptide ligase
CC activity. Can ligate peptides to unmodified N-termini of acceptor
CC proteins. Probably ligates through a thioester intermediate
CC (PubMed:18660805). {ECO:0000269|PubMed:11577182,
CC ECO:0000269|PubMed:18660805, ECO:0000269|PubMed:22238602,
CC ECO:0000269|PubMed:23398119, ECO:0000269|PubMed:26160583,
CC ECO:0000269|PubMed:26884487, ECO:0000305|PubMed:22396764}.
CC -!- ACTIVITY REGULATION: Inhibited by the cysteine protease inhibitor E-64.
CC {ECO:0000269|PubMed:26160583}.
CC -!- SUBUNIT: Interacts with SERPIN1 (PubMed:23398119, PubMed:20181955).
CC Interacts with PRN2 (PubMed:24947605). Interacts with WSCP
CC (PubMed:26160583, PubMed:26016527). Interacts with TZF4, TZF5 and TZF6
CC (PubMed:26978070). {ECO:0000269|PubMed:20181955,
CC ECO:0000269|PubMed:23398119, ECO:0000269|PubMed:24947605,
CC ECO:0000269|PubMed:26016527, ECO:0000269|PubMed:26160583,
CC ECO:0000269|PubMed:26978070}.
CC -!- INTERACTION:
CC P43297; Q9XI01: PDIL1-1; NbExp=4; IntAct=EBI-1993101, EBI-449394;
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:11577182,
CC ECO:0000269|PubMed:11743107, ECO:0000269|PubMed:23398119}. Golgi
CC apparatus {ECO:0000269|PubMed:22396764}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:26978070}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:26978070}. Note=Specifically accumulates in body
CC structures that directly bud from the endoplasmic reticulum and fuse
CC with the vacuole (PubMed:11577182). Passes through the Golgi on its
CC route to the vacuole (PubMed:22396764). {ECO:0000269|PubMed:11577182,
CC ECO:0000269|PubMed:22396764}.
CC -!- INDUCTION: By high salt conditions and drought stress.
CC {ECO:0000269|PubMed:8325504}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:22238602, PubMed:22396764). Mutant plants show
CC increased susceptibility to infection by the necrotrophic fungal
CC pathogen Botrytis cinerea (PubMed:22238602).
CC {ECO:0000269|PubMed:22238602, ECO:0000269|PubMed:22396764}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; D13043; BAA02374.1; -; Genomic_DNA.
DR EMBL; AC083835; AAG50628.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32135.1; -; Genomic_DNA.
DR EMBL; AY072130; AAL59952.1; -; mRNA.
DR EMBL; AY133781; AAM91715.1; -; mRNA.
DR PIR; JN0719; JN0719.
DR RefSeq; NP_564497.1; NM_103612.3.
DR AlphaFoldDB; P43297; -.
DR SMR; P43297; -.
DR BioGRID; 26347; 12.
DR IntAct; P43297; 1.
DR STRING; 3702.AT1G47128.1; -.
DR MEROPS; C01.064; -.
DR PaxDb; P43297; -.
DR PRIDE; P43297; -.
DR ProteomicsDB; 236213; -.
DR EnsemblPlants; AT1G47128.1; AT1G47128.1; AT1G47128.
DR GeneID; 841122; -.
DR Gramene; AT1G47128.1; AT1G47128.1; AT1G47128.
DR KEGG; ath:AT1G47128; -.
DR Araport; AT1G47128; -.
DR TAIR; locus:2825832; AT1G47128.
DR eggNOG; KOG1543; Eukaryota.
DR eggNOG; KOG4296; Eukaryota.
DR HOGENOM; CLU_012184_0_1_1; -.
DR InParanoid; P43297; -.
DR OMA; QSNTCCC; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; P43297; -.
DR PRO; PR:P43297; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P43297; baseline and differential.
DR Genevisible; P43297; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IPI:TAIR.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IPI:TAIR.
DR GO; GO:0000932; C:P-body; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IPI:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:TAIR.
DR GO; GO:0008233; F:peptidase activity; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0006508; P:proteolysis; IMP:TAIR.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:TAIR.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 2.10.25.160; -; 1.
DR InterPro; IPR000118; Granulin.
DR InterPro; IPR037277; Granulin_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF00396; Granulin; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00277; GRAN; 1.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase;
KW Protease; Reference proteome; Signal; Thiol protease; Vacuole.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..136
FT /note="Activation peptide"
FT /evidence="ECO:0000305|PubMed:22396764"
FT /id="PRO_0000026457"
FT CHAIN 137..352
FT /note="Cysteine proteinase RD21A"
FT /id="PRO_0000026458"
FT PROPEP 353..462
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:22396764"
FT /id="PRO_0000046018"
FT ACT_SITE 161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088,
FT ECO:0000269|PubMed:22396764"
FT ACT_SITE 297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089,
FT ECO:0000269|PubMed:22396764"
FT ACT_SITE 317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090,
FT ECO:0000269|PubMed:22396764"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 158..200
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 192..233
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 291..342
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 375..387
FT /evidence="ECO:0000250|UniProtKB:P25777"
FT DISULFID 381..402
FT /evidence="ECO:0000250|UniProtKB:P25777"
FT MUTAGEN 161
FT /note="C->A: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:22396764"
FT MUTAGEN 297
FT /note="H->A: Loss of protease activity."
FT /evidence="ECO:0000269|PubMed:22396764"
FT MUTAGEN 317
FT /note="N->A: Reduces protease activity."
FT /evidence="ECO:0000269|PubMed:22396764"
SQ SEQUENCE 462 AA; 50966 MW; 4C59955CCB95AA58 CRC64;
MGFLKPTMAI LFLAMVAVSS AVDMSIISYD EKHGVSTTGG RSEAEVMSIY EAWLVKHGKA
QSQNSLVEKD RRFEIFKDNL RFVDEHNEKN LSYRLGLTRF ADLTNDEYRS KYLGAKMEKK
GERRTSLRYE ARVGDELPES IDWRKKGAVA EVKDQGGCGS CWAFSTIGAV EGINQIVTGD
LITLSEQELV DCDTSYNEGC NGGLMDYAFE FIIKNGGIDT DKDYPYKGVD GTCDQIRKNA
KVVTIDSYED VPTYSEESLK KAVAHQPISI AIEAGGRAFQ LYDSGIFDGS CGTQLDHGVV
AVGYGTENGK DYWIVRNSWG KSWGESGYLR MARNIASSSG KCGIAIEPSY PIKNGENPPN
PGPSPPSPIK PPTQCDSYYT CPESNTCCCL FEYGKYCFAW GCCPLEAATC CDDNYSCCPH
EYPVCDLDQG TCLLSKNSPF SVKALKRKPA TPFWSQGRKN IA
