RD19A_ARATH
ID RD19A_ARATH Reviewed; 368 AA.
AC P43296; Q0WWF3; Q8H7C0; Q8LAT5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cysteine protease RD19A {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Protein RESPONSIVE TO DEHYDRATION 19 {ECO:0000303|PubMed:8325504};
DE Short=RD19 {ECO:0000303|PubMed:8325504};
DE Flags: Precursor;
GN Name=RD19A {ECO:0000303|PubMed:8325504}; OrderedLocusNames=At4g39090;
GN ORFNames=F19H22.190;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-192.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION BY DROUGHT STRESS.
RX PubMed=12102506; DOI=10.1093/aob/mcf104;
RA Bray E.A.;
RT "Classification of genes differentially expressed during water-deficit
RT stress in Arabidopsis thaliana: an analysis using microarray and
RT differential expression data.";
RL Ann. Bot. 89:803-811(2002).
RN [9]
RP FUNCTION, INTERACTION WITH THE RALSTONIA SOLANACEARUM EFFECTOR POPP2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18708476; DOI=10.1105/tpc.108.058685;
RA Bernoux M., Timmers T., Jauneau A., Briere C., de Wit P.J., Marco Y.,
RA Deslandes L.;
RT "RD19, an Arabidopsis cysteine protease required for RRS1-R-mediated
RT resistance, is relocalized to the nucleus by the Ralstonia solanacearum
RT PopP2 effector.";
RL Plant Cell 20:2252-2264(2008).
CC -!- FUNCTION: Probable thiol protease (By similarity). Required for RRS1-
CC mediated resistance against Ralstonia solanacearum. Plays a crucial
CC role as host factor for PopP2-triggered RRS1-mediated resistance.
CC Interacts with the R.solanacearum type III effector PopP2 to form a
CC nuclear complex that is required for activation of the RRS1-mediated
CC resistance response (PubMed:18708476). {ECO:0000250|UniProtKB:P43297,
CC ECO:0000269|PubMed:18708476}.
CC -!- SUBUNIT: Interacts with the Ralstonia solanacearum type III effector
CC PopP2. {ECO:0000269|PubMed:18708476}.
CC -!- SUBCELLULAR LOCATION: Lytic vacuole {ECO:0000269|PubMed:18708476}.
CC Nucleus {ECO:0000269|PubMed:18708476}. Note=Predominantly vacuolar.
CC From the Golgi apparatus, probably transported to the lytic vacuole
CC (LV) in clathrin-coated vesicles (CCVs) via the prevacuolar compartment
CC (PVC). Relocalizes to the nucleus when associated in a complex with the
CC Ralstonia solanacearum type III effector PopP2.
CC {ECO:0000269|PubMed:18708476}.
CC -!- INDUCTION: By high salt conditions (PubMed:8325504). Induced by drought
CC stress (PubMed:8325504, PubMed:12102506). {ECO:0000269|PubMed:12102506,
CC ECO:0000269|PubMed:8325504}.
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; D13042; BAA02373.1; -; Genomic_DNA.
DR EMBL; AL035679; CAB38829.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80572.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87016.1; -; Genomic_DNA.
DR EMBL; AY080598; AAL85009.1; -; mRNA.
DR EMBL; AY133844; AAM91778.1; -; mRNA.
DR EMBL; AK226399; BAE98545.1; -; mRNA.
DR EMBL; AY087621; AAM65162.1; -; mRNA.
DR EMBL; AF083750; AAN60308.1; -; mRNA.
DR PIR; JN0718; JN0718.
DR RefSeq; NP_568052.1; NM_120069.5.
DR AlphaFoldDB; P43296; -.
DR SMR; P43296; -.
DR STRING; 3702.AT4G39090.1; -.
DR MEROPS; C01.022; -.
DR PaxDb; P43296; -.
DR PRIDE; P43296; -.
DR ProteomicsDB; 236539; -.
DR EnsemblPlants; AT4G39090.1; AT4G39090.1; AT4G39090.
DR GeneID; 830064; -.
DR Gramene; AT4G39090.1; AT4G39090.1; AT4G39090.
DR KEGG; ath:AT4G39090; -.
DR Araport; AT4G39090; -.
DR TAIR; locus:2120222; AT4G39090.
DR eggNOG; KOG1542; Eukaryota.
DR HOGENOM; CLU_012184_1_3_1; -.
DR InParanoid; P43296; -.
DR OMA; INAGYMQ; -.
DR OrthoDB; 1264766at2759; -.
DR PhylomeDB; P43296; -.
DR PRO; PR:P43296; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P43296; baseline and differential.
DR Genevisible; P43296; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0000323; C:lytic vacuole; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IGI:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR CDD; cd02248; Peptidase_C1A; 1.
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; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
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 Disulfide bond; Glycoprotein; Hydrolase; Nucleus; Protease;
KW Reference proteome; Signal; Thiol protease; Vacuole; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..134
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026455"
FT CHAIN 135..368
FT /note="Cysteine protease RD19A"
FT /id="PRO_0000026456"
FT ACT_SITE 159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 156..206
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 190..240
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 296..350
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT CONFLICT 19
FT /note="S -> L (in Ref. 7; AAN60308)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="Y -> H (in Ref. 6; AAM65162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 40419 MW; 9D64CF35E07F519D CRC64;
MDRLKLYFSV FVLSFFIVSV SSSDVNDGDD LVIRQVVGGA EPQVLTSEDH FSLFKRKFGK
VYASNEEHDY RFSVFKANLR RARRHQKLDP SATHGVTQFS DLTRSEFRKK HLGVRSGFKL
PKDANKAPIL PTENLPEDFD WRDHGAVTPV KNQGSCGSCW SFSATGALEG ANFLATGKLV
SLSEQQLVDC DHECDPEEAD SCDSGCNGGL MNSAFEYTLK TGGLMKEEDY PYTGKDGKTC
KLDKSKIVAS VSNFSVISID EEQIAANLVK NGPLAVAINA GYMQTYIGGV SCPYICTRRL
NHGVLLVGYG AAGYAPARFK EKPYWIIKNS WGETWGENGF YKICKGRNIC GVDSMVSTVA
ATVSTTAH
