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CDR1_ARATH
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   03-AUG-2022, entry version 133.
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.AT5G33340.1; -.
DR   MEROPS; A01.069; -.
DR   iPTMnet; Q6XBF8; -.
DR   PaxDb; Q6XBF8; -.
DR   PRIDE; Q6XBF8; -.
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; locus:2145954; AT5G33340.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_005738_1_3_1; -.
DR   InParanoid; Q6XBF8; -.
DR   OMA; LSLCYNA; -.
DR   OrthoDB; 753343at2759; -.
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:0005576; C:extracellular region; IBA:GO_Central.
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; -; 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   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   SUPFAM; SSF50630; SSF50630; 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
 
 
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