RDL6_ARATH
ID RDL6_ARATH Reviewed; 356 AA.
AC F4JNL3; O81748;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Probable cysteine protease RDL6 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=RD21A-like protease 6 {ECO:0000305};
DE Flags: Precursor;
GN Name=RDL6 {ECO:0000305};
GN OrderedLocusNames=At4g23520 {ECO:0000312|Araport:AT4G23520};
GN ORFNames=F16G20.220 {ECO:0000312|EMBL:CAB79307.1};
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=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).
CC -!- FUNCTION: Probable thiol protease. {ECO:0000250|UniProtKB:P43297}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20473.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79307.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL031326; CAA20473.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161559; CAB79307.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84771.1; -; Genomic_DNA.
DR PIR; T05390; T05390.
DR RefSeq; NP_567686.2; NM_118483.3.
DR AlphaFoldDB; F4JNL3; -.
DR SMR; F4JNL3; -.
DR STRING; 3702.AT4G23520.1; -.
DR MEROPS; C01.A22; -.
DR PaxDb; F4JNL3; -.
DR PRIDE; F4JNL3; -.
DR ProteomicsDB; 236434; -.
DR EnsemblPlants; AT4G23520.1; AT4G23520.1; AT4G23520.
DR GeneID; 828452; -.
DR Gramene; AT4G23520.1; AT4G23520.1; AT4G23520.
DR KEGG; ath:AT4G23520; -.
DR Araport; AT4G23520; -.
DR TAIR; locus:2117979; AT4G23520.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; F4JNL3; -.
DR OMA; MARNIQD; -.
DR OrthoDB; 1275401at2759; -.
DR PRO; PR:F4JNL3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JNL3; 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: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; 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; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..132
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436324"
FT CHAIN 133..356
FT /note="Probable cysteine protease RDL6"
FT /id="PRO_5005397739"
FT ACT_SITE 157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 154..195
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 188..229
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 288..339
FT /evidence="ECO:0000250|UniProtKB:P84346"
SQ SEQUENCE 356 AA; 39605 MW; 8F2281BCB42460CC CRC64;
MGFVRPVCMT ILFLLIVFVL SAPSSAMDLP ATSGGHNRSN EEVEFIFQMW MSKHGKTYTN
ALGEKERRFQ NFKDNLRFID QHNAKNLSYQ LGLTRFADLT VQEYRDLFPG SPKPKQRNLK
TSRRYVPLAG DQLPESVDWR QEGAVSEIKD QGTCNSCWAF STVAAVEGLN KIVTGELISL
SEQELVDCNL VNNGCYGSGL MDTAFQFLIN NNGLDSEKDY PYQGTQGSCN RKQSTSNKVI
TIDSYEDVPA NDEISLQKAV AHQPVSVGVD KKSQEFMLYR SCIYNGPCGT NLDHALVIVG
YGSENGQDYW IVRNSWGTTW GDAGYIKIAR NFEDPKGLCG IAMLASYPIK NSASNA
