RDL3_ARATH
ID RDL3_ARATH Reviewed; 376 AA.
AC Q9LXW3; Q8LAC2;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable cysteine protease RDL3 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Probable cysteine proteinase At3g43960 {ECO:0000305};
DE AltName: Full=RD21A-like protease 3 {ECO:0000305};
DE Flags: Precursor;
GN Name=RDL3 {ECO:0000305}; OrderedLocusNames=At3g43960; ORFNames=T15B3_100;
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=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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21248074; DOI=10.1104/pp.110.166520;
RA Lin W.D., Liao Y.Y., Yang T.J., Pan C.Y., Buckhout T.J., Schmidt W.;
RT "Coexpression-based clustering of Arabidopsis root genes predicts
RT functional modules in early phosphate deficiency signaling.";
RL Plant Physiol. 155:1383-1402(2011).
CC -!- FUNCTION: Probable thiol protease. {ECO:0000250|UniProtKB:P43297}.
CC -!- TISSUE SPECIFICITY: Expressed in root hairs.
CC {ECO:0000269|PubMed:21248074}.
CC -!- DISRUPTION PHENOTYPE: Decreased root hair length under phosphate
CC deficiency. {ECO:0000269|PubMed:21248074}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; AL163975; CAB88124.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77849.1; -; Genomic_DNA.
DR EMBL; AK118634; BAC43231.1; -; mRNA.
DR EMBL; AY087918; AAM65468.1; -; mRNA.
DR PIR; T48950; T48950.
DR RefSeq; NP_566867.1; NM_114264.3.
DR AlphaFoldDB; Q9LXW3; -.
DR SMR; Q9LXW3; -.
DR STRING; 3702.AT3G43960.1; -.
DR MEROPS; C01.A18; -.
DR MEROPS; I29.003; -.
DR PaxDb; Q9LXW3; -.
DR PRIDE; Q9LXW3; -.
DR ProteomicsDB; 235075; -.
DR EnsemblPlants; AT3G43960.1; AT3G43960.1; AT3G43960.
DR GeneID; 823513; -.
DR Gramene; AT3G43960.1; AT3G43960.1; AT3G43960.
DR KEGG; ath:AT3G43960; -.
DR Araport; AT3G43960; -.
DR TAIR; locus:2097104; AT3G43960.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9LXW3; -.
DR OMA; EQWLMEN; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9LXW3; -.
DR PRO; PR:Q9LXW3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXW3; baseline and differential.
DR Genevisible; Q9LXW3; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
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 GO; GO:0048767; P:root hair elongation; IMP:TAIR.
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; 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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..126
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026461"
FT CHAIN 127..376
FT /note="Probable cysteine protease RDL3"
FT /id="PRO_0000026462"
FT ACT_SITE 152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 149..192
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 183..226
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 283..336
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT CONFLICT 36
FT /note="E -> G (in Ref. 4; AAM65468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41541 MW; 414AAD5C2701A655 CRC64;
MAISFRTLAL LTLSVLLISI SLGVVTATES QRNEGEVLTM YEQWLVENGK NYNGLGEKER
RFKIFKDNLK RIEEHNSDPN RSYERGLNKF SDLTADEFQA SYLGGKMEKK SLSDVAERYQ
YKEGDVLPDE VDWRERGAVV PRVKRQGECG SCWAFAATGA VEGINQITTG ELVSLSEQEL
IDCDRGNDNF GCAGGGAVWA FEFIKENGGI VSDEVYGYTG EDTAACKAIE MKTTRVVTIN
GHEVVPVNDE MSLKKAVAYQ PISVMISAAN MSDYKSGVYK GACSNLWGDH NVLIVGYGTS
SDEGDYWLIR NSWGPEWGEG GYLRLQRNFH EPTGKCAVAV APVYPIKSNS SSHLLSPSVF
KLVVLFVFQL ISLALL
