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Protein

Aspartic proteinase CDR1

Gene

CDR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in salicylic acid-dependent inducible resistance responses. May release an endogenous peptide elicitor required for the activation of inducible resistance mechanisms. Possesses protease activity in vitro.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081PROSITE-ProRule annotation
Active sitei319 – 3191PROSITE-ProRule annotation

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: TAIR

GO - Biological processi

  • defense response to bacterium Source: TAIR
  • protein catabolic process Source: GO_Central
  • regulation of hydrogen peroxide metabolic process Source: TAIR
  • regulation of salicylic acid metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Keywords - Biological processi

Plant defense

Enzyme and pathway databases

BioCyciARA:AT5G33340-MONOMER.

Protein family/group databases

MEROPSiA01.069.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartic proteinase CDR1 (EC:3.4.23.-)
Alternative name(s):
Protein CONSTITUTIVE DISEASE RESISTANCE 1
Gene namesi
Name:CDR1
Ordered Locus Names:At5g33340
ORF Names:F19N2.60
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G33340.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Apoplast, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081D → N: Loss of function. 1 Publication
Mutagenesisi319 – 3191D → N: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Propeptidei26 – 7348Activation peptideSequence analysisPRO_0000420633Add
BLAST
Chaini74 – 437364Aspartic proteinase CDR1PRO_0000420634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ6XBF8.
PRIDEiQ6XBF8.

Expressioni

Gene expression databases

GenevisibleiQ6XBF8. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G33340.1.

Structurei

3D structure databases

ProteinModelPortaliQ6XBF8.
SMRiQ6XBF8. Positions 89-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 430341Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
HOGENOMiHOG000237482.
InParanoidiQ6XBF8.
OMAiTSNSGEY.
PhylomeDBiQ6XBF8.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR032799. TAXi_C.
IPR032861. TAXi_N.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF14541. TAXi_C. 1 hit.
PF14543. TAXi_N. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6XBF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLFSSVLL SLCLLSSLFL SNANAKPKLG FTADLIHRDS PKSPFYNPME
60 70 80 90 100
TSSQRLRNAI HRSVNRVFHF TEKDNTPQPQ IDLTSNSGEY LMNVSIGTPP
110 120 130 140 150
FPIMAIADTG SDLLWTQCAP CDDCYTQVDP LFDPKTSSTY KDVSCSSSQC
160 170 180 190 200
TALENQASCS TNDNTCSYSL SYGDNSYTKG NIAVDTLTLG SSDTRPMQLK
210 220 230 240 250
NIIIGCGHNN AGTFNKKGSG IVGLGGGPVS LIKQLGDSID GKFSYCLVPL
260 270 280 290 300
TSKKDQTSKI NFGTNAIVSG SGVVSTPLIA KASQETFYYL TLKSISVGSK
310 320 330 340 350
QIQYSGSDSE SSEGNIIIDS GTTLTLLPTE FYSELEDAVA SSIDAEKKQD
360 370 380 390 400
PQSGLSLCYS ATGDLKVPVI TMHFDGADVK LDSSNAFVQV SEDLVCFAFR
410 420 430
GSPSFSIYGN VAQMNFLVGY DTVSKTVSFK PTDCAKM
Length:437
Mass (Da):46,819
Last modified:July 5, 2004 - v1
Checksum:i67803435746BF3C0
GO

Sequence cautioni

The sequence ABK28718.1 differs from that shown. Reason: Erroneous termination at position 438. Translated as stop.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY243479 mRNA. Translation: AAP72988.1.
AC051625 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93896.1.
DQ446998 mRNA. Translation: ABE66189.1.
DQ653316 mRNA. Translation: ABK28718.1. Sequence problems.
BT026129 mRNA. Translation: ABG48485.1.
RefSeqiNP_198319.1. NM_122858.2.
UniGeneiAt.50488.

Genome annotation databases

EnsemblPlantsiAT5G33340.1; AT5G33340.1; AT5G33340.
GeneIDi833310.
GrameneiAT5G33340.1; AT5G33340.1; AT5G33340.
KEGGiath:AT5G33340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY243479 mRNA. Translation: AAP72988.1.
AC051625 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93896.1.
DQ446998 mRNA. Translation: ABE66189.1.
DQ653316 mRNA. Translation: ABK28718.1. Sequence problems.
BT026129 mRNA. Translation: ABG48485.1.
RefSeqiNP_198319.1. NM_122858.2.
UniGeneiAt.50488.

3D structure databases

ProteinModelPortaliQ6XBF8.
SMRiQ6XBF8. Positions 89-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G33340.1.

Protein family/group databases

MEROPSiA01.069.

Proteomic databases

PaxDbiQ6XBF8.
PRIDEiQ6XBF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G33340.1; AT5G33340.1; AT5G33340.
GeneIDi833310.
GrameneiAT5G33340.1; AT5G33340.1; AT5G33340.
KEGGiath:AT5G33340.

Organism-specific databases

TAIRiAT5G33340.

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
HOGENOMiHOG000237482.
InParanoidiQ6XBF8.
OMAiTSNSGEY.
PhylomeDBiQ6XBF8.

Enzyme and pathway databases

BioCyciARA:AT5G33340-MONOMER.

Miscellaneous databases

PROiQ6XBF8.

Gene expression databases

GenevisibleiQ6XBF8. AT.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR032799. TAXi_C.
IPR032861. TAXi_N.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF14541. TAXi_C. 1 hit.
PF14543. TAXi_N. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An extracellular aspartic protease functions in Arabidopsis disease resistance signaling."
    Xia Y., Suzuki H., Borevitz J., Blount J., Guo Z., Patel K., Dixon R.A., Lamb C.
    EMBO J. 23:980-988(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-108 AND ASP-319.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
    Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
    Plant Biotechnol. J. 4:317-324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Arabidopsis ORF clones."
    Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiCDR1_ARATH
AccessioniPrimary (citable) accession number: Q6XBF8
Secondary accession number(s): A0MFJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2013
Last sequence update: July 5, 2004
Last modified: April 13, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Gain-of-function mutant CDR1-D (T-DNA tagging) shows a dwarf phenotype with dark and curled leaves, constitutive expression of the pathogenesis-related genes PR1 and PR2, and resistance to virulent Pseudomonas syringae.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.