RDL5_ARATH
ID RDL5_ARATH Reviewed; 371 AA.
AC Q9SUS9;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable cysteine protease RDL5 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Cysteine protease 2 {ECO:0000303|PubMed:23460027};
DE Short=AtCP2 {ECO:0000303|PubMed:23460027};
DE AltName: Full=Probable cysteine proteinase At4g11320 {ECO:0000305};
DE AltName: Full=RD21A-like protease 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=RDL5 {ECO:0000305}; Synonyms=CP2 {ECO:0000303|PubMed:23460027};
GN OrderedLocusNames=At4g11320; ORFNames=F8L21.110;
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=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 [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;
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING.
RX PubMed=23460027; DOI=10.1007/s11103-013-0030-7;
RA Mao Y.B., Xue X.Y., Tao X.Y., Yang C.Q., Wang L.J., Chen X.Y.;
RT "Cysteine protease enhances plant-mediated bollworm RNA interference.";
RL Plant Mol. Biol. 83:119-129(2013).
CC -!- FUNCTION: Possesses protease activity in vitro.
CC {ECO:0000269|PubMed:23460027}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescences and siliques.
CC {ECO:0000269|PubMed:23460027}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:23460027}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089}.
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DR EMBL; AL096882; CAB51416.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81233.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82996.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66783.1; -; Genomic_DNA.
DR EMBL; AY035055; AAK59560.1; -; mRNA.
DR EMBL; AY051062; AAK93739.1; -; mRNA.
DR PIR; T13023; T13023.
DR RefSeq; NP_001328659.1; NM_001340705.1.
DR RefSeq; NP_567377.1; NM_117203.4.
DR AlphaFoldDB; Q9SUS9; -.
DR SMR; Q9SUS9; -.
DR STRING; 3702.AT4G11320.1; -.
DR MEROPS; C01.A21; -.
DR PaxDb; Q9SUS9; -.
DR PRIDE; Q9SUS9; -.
DR ProteomicsDB; 235011; -.
DR EnsemblPlants; AT4G11320.1; AT4G11320.1; AT4G11320.
DR EnsemblPlants; AT4G11320.2; AT4G11320.2; AT4G11320.
DR GeneID; 826734; -.
DR Gramene; AT4G11320.1; AT4G11320.1; AT4G11320.
DR Gramene; AT4G11320.2; AT4G11320.2; AT4G11320.
DR KEGG; ath:AT4G11320; -.
DR Araport; AT4G11320; -.
DR TAIR; locus:2128253; AT4G11320.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9SUS9; -.
DR OMA; TLMFESW; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9SUS9; -.
DR PRO; PR:Q9SUS9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUS9; baseline and differential.
DR Genevisible; Q9SUS9; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
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; 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; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..143
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026465"
FT CHAIN 144..371
FT /note="Probable cysteine protease RDL5"
FT /id="PRO_0000026466"
FT ACT_SITE 168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 165..206
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 199..239
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 298..349
FT /evidence="ECO:0000250|UniProtKB:P84346"
SQ SEQUENCE 371 AA; 40711 MW; 6A8D5A5B8F7DD96D CRC64;
MGYAKSAMLI FLLALVIASC ATAMDMSVVS SNDNHHVTAG PGRRQGIFDA EATLMFESWM
VKHGKVYDSV AEKERRLTIF EDNLRFITNR NAENLSYRLG LNRFADLSLH EYGEICHGAD
PRPPRNHVFM TSSNRYKTSD GDVLPKSVDW RNEGAVTEVK DQGLCRSCWA FSTVGAVEGL
NKIVTGELVT LSEQDLINCN KENNGCGGGK VETAYEFIMN NGGLGTDNDY PYKALNGVCE
GRLKEDNKNV MIDGYENLPA NDEAALMKAV AHQPVTAVVD SSSREFQLYE SGVFDGTCGT
NLNHGVVVVG YGTENGRDYW IVKNSRGDTW GEAGYMKMAR NIANPRGLCG IAMRASYPLK
NSFSTDKVSV A
