RDL2_ARATH
ID RDL2_ARATH Reviewed; 362 AA.
AC Q9LT77; Q8GT77;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable cysteine protease RDL2 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Probable cysteine proteinase At3g19400 {ECO:0000305};
DE AltName: Full=RD21A-like protease 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=RDL2 {ECO:0000305}; OrderedLocusNames=At3g19400; ORFNames=MLD14.13;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
CC -!- FUNCTION: Probable thiol protease. {ECO:0000250|UniProtKB:P43297}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LT77-1; Sequence=Displayed;
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; AB025624; BAB02464.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76236.1; -; Genomic_DNA.
DR EMBL; AK118509; BAC43113.1; -; mRNA.
DR RefSeq; NP_566634.2; NM_112827.3. [Q9LT77-1]
DR AlphaFoldDB; Q9LT77; -.
DR SMR; Q9LT77; -.
DR STRING; 3702.AT3G19400.1; -.
DR MEROPS; C01.029; -.
DR MEROPS; I29.003; -.
DR PaxDb; Q9LT77; -.
DR PRIDE; Q9LT77; -.
DR ProteomicsDB; 234750; -. [Q9LT77-1]
DR EnsemblPlants; AT3G19400.1; AT3G19400.1; AT3G19400. [Q9LT77-1]
DR GeneID; 821474; -.
DR Gramene; AT3G19400.1; AT3G19400.1; AT3G19400. [Q9LT77-1]
DR KEGG; ath:AT3G19400; -.
DR Araport; AT3G19400; -.
DR TAIR; locus:2090629; AT3G19400.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9LT77; -.
DR OMA; PRGDEMS; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9LT77; -.
DR PRO; PR:Q9LT77; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LT77; baseline and differential.
DR Genevisible; Q9LT77; 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; 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 Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..129
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026459"
FT CHAIN 130..362
FT /note="Probable cysteine protease RDL2"
FT /id="PRO_0000026460"
FT ACT_SITE 154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 151..194
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 185..228
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 287..338
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT CONFLICT 113
FT /note="T -> N (in Ref. 3; BAC43113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40290 MW; 56DFAA1FEE95A6B0 CRC64;
MAATPIRVIV SALVILSVLL LSSSLGVATE TEIERNETEV RLMYEQWLVE NRKNYNGLGE
KERRFKIFKD NLKFVDEHNS VPDRTFEVGL TRFADLTNEE FRAIYLRKKM ERTKDSVKTE
RYLYKEGDVL PDEVDWRANG AVVSVKDQGN CGSCWAFSAV GAVEGINQIT TGELISLSEQ
ELVDCDRGFV NAGCDGGIMN YAFEFIMKNG GIETDQDYPY NANDLGLCNA DKNNNTRVVT
IDGYEDVPRD DEKSLKKAVA HQPVSVAIEA SSQAFQLYKS GVMTGTCGIS LDHGVVVVGY
GSTSGEDYWI IRNSWGLNWG DSGYVKLQRN IDDPFGKCGI AMMPSYPTKS SFPSSFDLLS
EI
