RD21C_ARATH
ID RD21C_ARATH Reviewed; 452 AA.
AC Q9LT78;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable cysteine protease RD21C {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE Flags: Precursor;
GN Name=RD21C {ECO:0000305};
GN OrderedLocusNames=At3g19390 {ECO:0000312|Araport:AT3G19390};
GN ORFNames=MLD14.12 {ECO:0000312|EMBL:BAB02463.1};
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=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=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 INTERACTION WITH WSCP.
RX PubMed=26160583; DOI=10.1093/jxb/erv327;
RA Boex-Fontvieille E., Rustgi S., Reinbothe S., Reinbothe C.;
RT "A Kunitz-type protease inhibitor regulates programmed cell death during
RT flower development in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:6119-6135(2015).
CC -!- FUNCTION: Probable thiol protease. {ECO:0000250|UniProtKB:P43297}.
CC -!- SUBUNIT: Interacts with WSCP. {ECO:0000269|PubMed:26160583}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB025624; BAB02463.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76234.1; -; Genomic_DNA.
DR EMBL; AY062725; AAL32803.1; -; mRNA.
DR EMBL; AY093350; AAM13349.1; -; mRNA.
DR RefSeq; NP_566633.1; NM_112826.4.
DR AlphaFoldDB; Q9LT78; -.
DR SMR; Q9LT78; -.
DR IntAct; Q9LT78; 3.
DR STRING; 3702.AT3G19390.1; -.
DR MEROPS; C01.029; -.
DR PaxDb; Q9LT78; -.
DR PRIDE; Q9LT78; -.
DR ProteomicsDB; 236222; -.
DR EnsemblPlants; AT3G19390.1; AT3G19390.1; AT3G19390.
DR GeneID; 821473; -.
DR Gramene; AT3G19390.1; AT3G19390.1; AT3G19390.
DR KEGG; ath:AT3G19390; -.
DR Araport; AT3G19390; -.
DR TAIR; locus:2090614; AT3G19390.
DR eggNOG; KOG1543; Eukaryota.
DR eggNOG; KOG4296; Eukaryota.
DR HOGENOM; CLU_012184_0_1_1; -.
DR InParanoid; Q9LT78; -.
DR OMA; CNTRAGT; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9LT78; -.
DR PRO; PR:Q9LT78; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LT78; 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 Gene3D; 2.10.25.160; -; 1.
DR InterPro; IPR000118; Granulin.
DR InterPro; IPR037277; Granulin_sf.
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; PF00396; Granulin; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00277; GRAN; 1.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..128
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436329"
FT CHAIN 129..345
FT /note="Probable cysteine protease RD21C"
FT /id="PRO_5006529498"
FT PROPEP 346..452
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436330"
FT ACT_SITE 153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 150..192
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 184..226
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 284..335
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 363..375
FT /evidence="ECO:0000250|UniProtKB:P25777"
FT DISULFID 369..390
FT /evidence="ECO:0000250|UniProtKB:P25777"
SQ SEQUENCE 452 AA; 49308 MW; CF1D2CAA957FC429 CRC64;
MATSIKSITL ALLIFSVLLI SLSLGSVTAT ETTRNEAEAR RMYERWLVEN RKNYNGLGEK
ERRFEIFKDN LKFVEEHSSI PNRTYEVGLT RFADLTNDEF RAIYLRSKME RTRVPVKGEK
YLYKVGDSLP DAIDWRAKGA VNPVKDQGSC GSCWAFSAIG AVEGINQIKT GELISLSEQE
LVDCDTSYND GCGGGLMDYA FKFIIENGGI DTEEDYPYIA TDVNVCNSDK KNTRVVTIDG
YEDVPQNDEK SLKKALANQP ISVAIEAGGR AFQLYTSGVF TGTCGTSLDH GVVAVGYGSE
GGQDYWIVRN SWGSNWGESG YFKLERNIKE SSGKCGVAMM ASYPTKSSGS NPPKPPAPSP
VVCDKSNTCP AKSTCCCLYE YNGKCYSWGC CPYESATCCD DGSSCCPQSY PVCDLKANTC
RMKGNSPLSI KALTRGPAIA TTKSTNMLVG SA
