RD19D_ARATH
ID RD19D_ARATH Reviewed; 367 AA.
AC Q8VYS0; Q3EAJ4; Q9SV42;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable cysteine protease RD19D {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE Flags: Precursor;
GN Name=RD19D {ECO:0000305};
GN OrderedLocusNames=At3g54940 {ECO:0000312|Araport:AT3G54940};
GN ORFNames=F28P10.80 {ECO:0000312|EMBL:CAB41090.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
CC -!- FUNCTION: Probable thiol protease. {ECO:0000250|UniProtKB:P43297}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41090.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049655; CAB41090.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79316.1; -; Genomic_DNA.
DR EMBL; AY070063; AAL49820.1; -; mRNA.
DR PIR; T06726; T06726.
DR RefSeq; NP_567010.5; NM_115351.7.
DR AlphaFoldDB; Q8VYS0; -.
DR SMR; Q8VYS0; -.
DR STRING; 3702.AT3G54940.2; -.
DR MEROPS; C01.A05; -.
DR PaxDb; Q8VYS0; -.
DR PRIDE; Q8VYS0; -.
DR ProteomicsDB; 225925; -.
DR EnsemblPlants; AT3G54940.2; AT3G54940.2; AT3G54940.
DR GeneID; 824659; -.
DR Gramene; AT3G54940.2; AT3G54940.2; AT3G54940.
DR KEGG; ath:AT3G54940; -.
DR Araport; AT3G54940; -.
DR TAIR; locus:2082687; AT3G54940.
DR eggNOG; KOG1542; Eukaryota.
DR HOGENOM; CLU_012184_1_3_1; -.
DR InParanoid; Q8VYS0; -.
DR OMA; RGHMQAC; -.
DR OrthoDB; 1264766at2759; -.
DR PhylomeDB; Q8VYS0; -.
DR PRO; PR:Q8VYS0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VYS0; 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; 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 Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..136
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436326"
FT CHAIN 137..367
FT /note="Probable cysteine protease RD19D"
FT /id="PRO_5006529416"
FT ACT_SITE 161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 158..208
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 192..241
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 297..352
FT /evidence="ECO:0000250|UniProtKB:P84346"
SQ SEQUENCE 367 AA; 40133 MW; A16E32F8DDF047CF CRC64;
MVAKALAQLI TCIILFCHVV ASVEDLTIRQ VTADNRRIRP NLLGTHTESK FRLFMSDYGK
NYSTREEYIH RLGIFAKNVL KAAEHQMMDP SAVHGVTQFS DLTEEEFKRM YTGVADVGGS
RGGTVGAEAP MVEVDGLPED FDWREKGGVT EVKNQGACGS CWAFSTTGAA EGAHFVSTGK
LLSLSEQQLV DCDQACDPKD KKACDNGCGG GLMTNAYEYL MEAGGLEEER SYPYTGKRGH
CKFDPEKVAV RVLNFTTIPL DENQIAANLV RHGPLAVGLN AVFMQTYIGG VSCPLICSKR
NVNHGVLLVG YGSKGFSILR LSNKPYWIIK NSWGKKWGEN GYYKLCRGHD ICGINSMVSA
VATQVSS
