RD21B_ARATH
ID RD21B_ARATH Reviewed; 463 AA.
AC Q9FMH8; Q0WM94;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable cysteine protease RD21B {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE Flags: Precursor;
GN Name=RD21B {ECO:0000305};
GN OrderedLocusNames=At5g43060 {ECO:0000312|Araport:AT5G43060};
GN ORFNames=MMG4.7 {ECO:0000312|EMBL:BAB08269.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 164-463.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH PRN2.
RX PubMed=24947605; DOI=10.1111/tpj.12602;
RA Zhang B., Tremousaygue D., Denance N., van Esse H.P., Hoerger A.C.,
RA Dabos P., Goffner D., Thomma B.P., van der Hoorn R.A., Tuominen H.;
RT "PIRIN2 stabilizes cysteine protease XCP2 and increases susceptibility to
RT the vascular pathogen Ralstonia solanacearum in Arabidopsis.";
RL Plant J. 79:1009-1019(2014).
RN [6]
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 PRN2 (PubMed:24947605). Interacts with WSCP.
CC {ECO:0000269|PubMed:24947605}.
CC -!- INTERACTION:
CC Q9FMH8; Q9XI01: PDIL1-1; NbExp=3; IntAct=EBI-1993115, EBI-449394;
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000305}.
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DR EMBL; AB008267; BAB08269.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94905.1; -; Genomic_DNA.
DR EMBL; AY062608; AAL32686.1; -; mRNA.
DR EMBL; AY114661; AAM47980.1; -; mRNA.
DR EMBL; AK229936; BAF01762.1; -; mRNA.
DR RefSeq; NP_568620.1; NM_123672.4.
DR AlphaFoldDB; Q9FMH8; -.
DR SMR; Q9FMH8; -.
DR IntAct; Q9FMH8; 2.
DR STRING; 3702.AT5G43060.1; -.
DR MEROPS; C01.A12; -.
DR MetOSite; Q9FMH8; -.
DR PaxDb; Q9FMH8; -.
DR PRIDE; Q9FMH8; -.
DR ProteomicsDB; 225926; -.
DR EnsemblPlants; AT5G43060.1; AT5G43060.1; AT5G43060.
DR GeneID; 834321; -.
DR Gramene; AT5G43060.1; AT5G43060.1; AT5G43060.
DR KEGG; ath:AT5G43060; -.
DR Araport; AT5G43060; -.
DR TAIR; locus:2167821; AT5G43060.
DR eggNOG; KOG1543; Eukaryota.
DR eggNOG; KOG4296; Eukaryota.
DR HOGENOM; CLU_012184_0_1_1; -.
DR InParanoid; Q9FMH8; -.
DR OMA; MERNLGN; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9FMH8; -.
DR PRO; PR:Q9FMH8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMH8; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..137
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436327"
FT CHAIN 138..353
FT /note="Probable cysteine protease RD21B"
FT /id="PRO_5006529477"
FT PROPEP 354..463
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436328"
FT ACT_SITE 162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 159..201
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 193..234
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 292..343
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 376..388
FT /evidence="ECO:0000250|UniProtKB:P25777"
FT DISULFID 382..403
FT /evidence="ECO:0000250|UniProtKB:P25777"
FT CONFLICT 312
FT /note="D -> G (in Ref. 4; BAF01762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 51204 MW; 699E9BC9B42A3652 CRC64;
MGFLKLSPMI LLLAMIGVSY AMDMSIISYD ENHHITTETS RSDSEVERIY EAWMVEHGKK
KMNQNGLGAE KDQRFEIFKD NLRFIDEHNT KNLSYKLGLT RFADLTNEEY RSMYLGAKPT
KRVLKTSDRY QARVGDALPD SVDWRKEGAV ADVKDQGSCG SCWAFSTIGA VEGINKIVTG
DLISLSEQEL VDCDTSYNQG CNGGLMDYAF EFIIKNGGID TEADYPYKAA DGRCDQNRKN
AKVVTIDSYE DVPENSEASL KKALAHQPIS VAIEAGGRAF QLYSSGVFDG LCGTELDHGV
VAVGYGTENG KDYWIVRNSW GNRWGESGYI KMARNIEAPT GKCGIAMEAS YPIKKGQNPP
NPGPSPPSPI KPPTTCDKYF SCPESNTCCC LYKYGKYCFG WGCCPLEAAT CCDDNSSCCP
HEYPVCDVNR GTCLMSKNSP FSVKALKRTP AIPFWAKSRK HIA
