RD19B_ARATH
ID RD19B_ARATH Reviewed; 361 AA.
AC P43295; Q058I7; Q680L1; Q9SJT5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable cysteine protease RD19B {ECO:0000305};
DE EC=3.4.22.-;
DE AltName: Full=RD19-like protein 1 {ECO:0000303|PubMed:18708476};
DE AltName: Full=Thiol protease A1494 {ECO:0000303|PubMed:8018874};
DE Flags: Precursor;
GN Name=RD19B {ECO:0000305}; Synonyms=RDL1 {ECO:0000303|PubMed:18708476};
GN OrderedLocusNames=At2g21430; ORFNames=F3K23.19;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-361, AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8018874; DOI=10.1007/bf00023242;
RA Williams J., Bulman M., Huttly A.K., Phillips A., Neill S.;
RT "Characterization of a cDNA from Arabidopsis thaliana encoding a potential
RT thiol protease whose expression is induced independently by wilting and
RT abscisic acid.";
RL Plant Mol. Biol. 25:259-270(1994).
RN [6]
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 [7]
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. {ECO:0000250|UniProtKB:P43297}.
CC -!- SUBCELLULAR LOCATION: Lytic vacuole {ECO:0000269|PubMed:18708476}.
CC Note=Predominantly vacuolar. From the Golgi apparatus, probably
CC transported to the lytic vacuole (LV) in clathrin-coated vesicles
CC (CCVs) via the prevacuolar compartment (PVC).
CC {ECO:0000269|PubMed:18708476}.
CC -!- INDUCTION: By wilting and abscisic acid (ABA) (PubMed:8018874). Induced
CC by drought stress (PubMed:12102506). {ECO:0000269|PubMed:12102506,
CC ECO:0000269|PubMed:8018874}.
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; AC006841; AAD23687.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07177.1; -; Genomic_DNA.
DR EMBL; AK175856; BAD43619.1; -; mRNA.
DR EMBL; BT029231; ABJ98563.1; -; mRNA.
DR EMBL; X74359; CAA52403.1; -; mRNA.
DR PIR; B84601; B84601.
DR RefSeq; NP_565512.1; NM_127715.4.
DR AlphaFoldDB; P43295; -.
DR SMR; P43295; -.
DR STRING; 3702.AT2G21430.1; -.
DR MEROPS; C01.A04; -.
DR PaxDb; P43295; -.
DR PRIDE; P43295; -.
DR ProteomicsDB; 225924; -.
DR EnsemblPlants; AT2G21430.1; AT2G21430.1; AT2G21430.
DR GeneID; 816682; -.
DR Gramene; AT2G21430.1; AT2G21430.1; AT2G21430.
DR KEGG; ath:AT2G21430; -.
DR Araport; AT2G21430; -.
DR TAIR; locus:2050145; AT2G21430.
DR eggNOG; KOG1542; Eukaryota.
DR HOGENOM; CLU_012184_1_3_1; -.
DR InParanoid; P43295; -.
DR OMA; CNETESC; -.
DR OrthoDB; 1264766at2759; -.
DR PhylomeDB; P43295; -.
DR PRO; PR:P43295; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P43295; baseline and differential.
DR Genevisible; P43295; 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:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Vacuole; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..131
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026453"
FT CHAIN 132..361
FT /note="Probable cysteine protease RD19B"
FT /id="PRO_0000026454"
FT ACT_SITE 156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 153..203
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 187..237
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 293..347
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT CONFLICT 49
FT /note="T -> A (in Ref. 5; CAA52403)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="G -> R (in Ref. 3; BAD43619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39819 MW; D09A2CE5654642DD CRC64;
MDYHLRVLFS VSLIFVFVSV SVCGDEDVLI RQVVDETEPK VLSSEDHFTL FKKKFGKVYG
SIEEHYYRFS VFKANLLRAM RHQKMDPSAR HGVTQFSDLT RSEFRRKHLG VKGGFKLPKD
ANQAPILPTQ NLPEEFDWRD RGAVTPVKNQ GSCGSCWSFS TTGALEGAHF LATGKLVSLS
EQQLVDCDHE CDPEEEGSCD SGCNGGLMNS AFEYTLKTGG LMREKDYPYT GTDGGSCKLD
RSKIVASVSN FSVVSINEDQ IAANLIKNGP LAVAINAAYM QTYIGGVSCP YICSRRLNHG
VLLVGYGSAG FSQARLKEKP YWIIKNSWGE SWGENGFYKI CKGRNICGVD SLVSTVAATT
S
