RD19C_ARATH
ID RD19C_ARATH Reviewed; 373 AA.
AC Q9SUL1;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable cysteine protease RD19C {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=RD19-like protein 2 {ECO:0000303|PubMed:18708476};
DE Flags: Precursor;
GN Name=RD19C {ECO:0000305}; Synonyms=RDL2 {ECO:0000303|PubMed:18708476};
GN OrderedLocusNames=At4g16190 {ECO:0000312|Araport:AT4G16190};
GN ORFNames=dl4135w {ECO:0000312|EMBL:CAB10398.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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 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 drought stress. {ECO:0000269|PubMed:12102506}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000305}.
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DR EMBL; Z97340; CAB10398.1; -; Genomic_DNA.
DR EMBL; AL161543; CAB78661.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83713.1; -; Genomic_DNA.
DR EMBL; AY039556; AAK62611.1; -; mRNA.
DR EMBL; AY129473; AAM91059.1; -; mRNA.
DR EMBL; AY136316; AAM96982.1; -; mRNA.
DR EMBL; BT000733; AAN31875.1; -; mRNA.
DR EMBL; AK226366; BAE98514.1; -; mRNA.
DR PIR; D71428; D71428.
DR RefSeq; NP_567489.1; NM_117715.3.
DR AlphaFoldDB; Q9SUL1; -.
DR SMR; Q9SUL1; -.
DR STRING; 3702.AT4G16190.1; -.
DR MEROPS; C01.A06; -.
DR PaxDb; Q9SUL1; -.
DR PRIDE; Q9SUL1; -.
DR ProteomicsDB; 225945; -.
DR EnsemblPlants; AT4G16190.1; AT4G16190.1; AT4G16190.
DR GeneID; 827311; -.
DR Gramene; AT4G16190.1; AT4G16190.1; AT4G16190.
DR KEGG; ath:AT4G16190; -.
DR Araport; AT4G16190; -.
DR TAIR; locus:2130180; AT4G16190.
DR eggNOG; KOG1542; Eukaryota.
DR HOGENOM; CLU_012184_1_3_1; -.
DR InParanoid; Q9SUL1; -.
DR OMA; KNSCDAG; -.
DR OrthoDB; 1264766at2759; -.
DR PhylomeDB; Q9SUL1; -.
DR PRO; PR:Q9SUL1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUL1; baseline and differential.
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:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
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; 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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Vacuole; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..139
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436325"
FT CHAIN 140..373
FT /note="Probable cysteine protease RD19C"
FT /id="PRO_5006529509"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 161..211
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 195..245
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 301..356
FT /evidence="ECO:0000250|UniProtKB:P84346"
SQ SEQUENCE 373 AA; 41264 MW; 5BE23F0AD631DD7B CRC64;
MDRVVFFFLI AATLLAGSLG STVISGEVTD GFVNPIRQVV PEENDEQLLN AEHHFTLFKS
KYEKTYATQV EHDHRFRVFK ANLRRARRNQ LLDPSAVHGV TQFSDLTPKE FRRKFLGLKR
RGFRLPTDTQ TAPILPTSDL PTEFDWREQG AVTPVKNQGM CGSCWSFSAI GALEGAHFLA
TKELVSLSEQ QLVDCDHECD PAQANSCDSG CSGGLMNNAF EYALKAGGLM KEEDYPYTGR
DHTACKFDKS KIVASVSNFS VVSSDEDQIA ANLVQHGPLA IAINAMWMQT YIGGVSCPYV
CSKSQDHGVL LVGFGSSGYA PIRLKEKPYW IIKNSWGAMW GEHGYYKICR GPHNMCGMDT
MVSTVAAVHT SPK
