RDL4_ARATH
ID RDL4_ARATH Reviewed; 364 AA.
AC Q9SUT0; Q42312; Q8RWI3;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable cysteine protease RDL4 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Cysteine protease 1 {ECO:0000303|PubMed:23460027};
DE Short=AtCP1 {ECO:0000303|PubMed:23460027};
DE AltName: Full=Probable cysteine proteinase At4g11310 {ECO:0000305};
DE AltName: Full=RD21A-like protease 4 {ECO:0000305};
DE Flags: Precursor;
GN Name=RDL4 {ECO:0000305}; Synonyms=CP1 {ECO:0000303|PubMed:23460027};
GN OrderedLocusNames=At4g11310; ORFNames=F8L21.100;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-105.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [5]
RP TISSUE SPECIFICITY.
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: Probable thiol protease. {ECO:0000250|UniProtKB:P43297}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences.
CC {ECO:0000269|PubMed:23460027}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM13065.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN15418.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL096882; CAB51415.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81232.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82995.1; -; Genomic_DNA.
DR EMBL; AY093066; AAM13065.1; ALT_INIT; mRNA.
DR EMBL; BT000099; AAN15418.1; ALT_INIT; mRNA.
DR EMBL; Z37253; CAA85532.1; -; mRNA.
DR PIR; T13022; T13022.
DR RefSeq; NP_567376.1; NM_117202.3.
DR AlphaFoldDB; Q9SUT0; -.
DR SMR; Q9SUT0; -.
DR BioGRID; 12032; 4.
DR IntAct; Q9SUT0; 3.
DR STRING; 3702.AT4G11310.1; -.
DR MEROPS; C01.A20; -.
DR iPTMnet; Q9SUT0; -.
DR PaxDb; Q9SUT0; -.
DR PRIDE; Q9SUT0; -.
DR ProteomicsDB; 234718; -.
DR EnsemblPlants; AT4G11310.1; AT4G11310.1; AT4G11310.
DR GeneID; 826733; -.
DR Gramene; AT4G11310.1; AT4G11310.1; AT4G11310.
DR KEGG; ath:AT4G11310; -.
DR Araport; AT4G11310; -.
DR TAIR; locus:2128243; AT4G11310.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9SUT0; -.
DR OMA; VFMTSSD; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9SUT0; -.
DR PRO; PR:Q9SUT0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUT0; baseline and differential.
DR Genevisible; Q9SUT0; 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: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..136
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026463"
FT CHAIN 137..364
FT /note="Probable cysteine protease RDL4"
FT /id="PRO_0000026464"
FT ACT_SITE 161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 158..199
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 192..232
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 291..342
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT CONFLICT 98
FT /note="A -> G (in Ref. 4; CAA85532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39925 MW; 5507664B2536F91A CRC64;
MGSAKSAMLI LLVAMVIASC ATAIDMSVVS YDDNNRLHSV FDAEASLIFE SWMVKHGKVY
GSVAEKERRL TIFEDNLRFI NNRNAENLSY RLGLTGFADL SLHEYKEVCH GADPRPPRNH
VFMTSSDRYK TSADDVLPKS VDWRNEGAVT EVKDQGHCRS CWAFSTVGAV EGLNKIVTGE
LVTLSEQDLI NCNKENNGCG GGKLETAYEF IMKNGGLGTD NDYPYKAVNG VCDGRLKENN
KNVMIDGYEN LPANDESALM KAVAHQPVTA VIDSSSREFQ LYESGVFDGS CGTNLNHGVV
VVGYGTENGR DYWLVKNSRG ITWGEAGYMK MARNIANPRG LCGIAMRASY PLKNSFSTDK
SSIA
