ID CDR1_ARATH Reviewed; 437 AA.
AC Q6XBF8; A0MFJ0;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Aspartic proteinase CDR1;
DE EC=3.4.23.-;
DE AltName: Full=Protein CONSTITUTIVE DISEASE RESISTANCE 1;
DE Flags: Precursor;
GN Name=CDR1; OrderedLocusNames=At5g33340; ORFNames=F19N2.60;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF ASP-108 AND ASP-319.
RX PubMed=14765119; DOI=10.1038/sj.emboj.7600086;
RA Xia Y., Suzuki H., Borevitz J., Blount J., Guo Z., Patel K., Dixon R.A.,
RA Lamb C.;
RT "An extracellular aspartic protease functions in Arabidopsis disease
RT resistance signaling.";
RL EMBO J. 23:980-988(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in salicylic acid-dependent inducible resistance
CC responses. May release an endogenous peptide elicitor required for the
CC activation of inducible resistance mechanisms. Possesses protease
CC activity in vitro. {ECO:0000269|PubMed:14765119}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:14765119}.
CC -!- MISCELLANEOUS: Gain-of-function mutant CDR1-D (T-DNA tagging) shows a
CC dwarf phenotype with dark and curled leaves, constitutive expression of
CC the pathogenesis-related genes PR1 and PR2, and resistance to virulent
CC Pseudomonas syringae. {ECO:0000305|PubMed:14765119}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28718.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY243479; AAP72988.1; -; mRNA.
DR EMBL; AC051625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93896.1; -; Genomic_DNA.
DR EMBL; DQ446998; ABE66189.1; -; mRNA.
DR EMBL; DQ653316; ABK28718.1; ALT_SEQ; mRNA.
DR EMBL; BT026129; ABG48485.1; -; mRNA.
DR RefSeq; NP_198319.1; NM_122858.3.
DR AlphaFoldDB; Q6XBF8; -.
DR SMR; Q6XBF8; -.
DR STRING; 3702.Q6XBF8; -.
DR MEROPS; A01.069; -.
DR GlyCosmos; Q6XBF8; 1 site, No reported glycans.
DR iPTMnet; Q6XBF8; -.
DR PaxDb; 3702-AT5G33340-1; -.
DR ProteomicsDB; 223971; -.
DR EnsemblPlants; AT5G33340.1; AT5G33340.1; AT5G33340.
DR GeneID; 833310; -.
DR Gramene; AT5G33340.1; AT5G33340.1; AT5G33340.
DR KEGG; ath:AT5G33340; -.
DR Araport; AT5G33340; -.
DR TAIR; AT5G33340; CDR1.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_1_3_1; -.
DR InParanoid; Q6XBF8; -.
DR OMA; VCFAFAP; -.
DR OrthoDB; 1212463at2759; -.
DR PhylomeDB; Q6XBF8; -.
DR PRO; PR:Q6XBF8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6XBF8; baseline and differential.
DR Genevisible; Q6XBF8; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IDA:TAIR.
DR GO; GO:0010337; P:regulation of salicylic acid metabolic process; IMP:TAIR.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034161; Pepsin-like_plant.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR47967:SF66; ASPARTIC PROTEINASE CDR1-RELATED; 1.
DR PANTHER; PTHR47967; OS07G0603500 PROTEIN-RELATED; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Apoplast; Aspartyl protease; Glycoprotein; Hydrolase; Plant defense;
KW Protease; Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..73
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420633"
FT CHAIN 74..437
FT /note="Aspartic proteinase CDR1"
FT /id="PRO_0000420634"
FT DOMAIN 90..430
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 108
FT /note="D->N: Loss of function."
FT /evidence="ECO:0000269|PubMed:14765119"
FT MUTAGEN 319
FT /note="D->N: Loss of function."
FT /evidence="ECO:0000269|PubMed:14765119"
SQ SEQUENCE 437 AA; 46819 MW; 67803435746BF3C0 CRC64;
MASLFSSVLL SLCLLSSLFL SNANAKPKLG FTADLIHRDS PKSPFYNPME TSSQRLRNAI
HRSVNRVFHF TEKDNTPQPQ IDLTSNSGEY LMNVSIGTPP FPIMAIADTG SDLLWTQCAP
CDDCYTQVDP LFDPKTSSTY KDVSCSSSQC TALENQASCS TNDNTCSYSL SYGDNSYTKG
NIAVDTLTLG SSDTRPMQLK NIIIGCGHNN AGTFNKKGSG IVGLGGGPVS LIKQLGDSID
GKFSYCLVPL TSKKDQTSKI NFGTNAIVSG SGVVSTPLIA KASQETFYYL TLKSISVGSK
QIQYSGSDSE SSEGNIIIDS GTTLTLLPTE FYSELEDAVA SSIDAEKKQD PQSGLSLCYS
ATGDLKVPVI TMHFDGADVK LDSSNAFVQV SEDLVCFAFR GSPSFSIYGN VAQMNFLVGY
DTVSKTVSFK PTDCAKM
//
