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Protein

Cysteine protease XCP2

Gene

XCP2

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

Functioni

Cysteine protease involved in xylem tracheary element (TE) autolysis during xylogenesis in roots. Participates in micro autolysis within the intact central vacuole before mega autolysis is initiated by tonoplast implosion (PubMed:18573193). Involved in susceptibility to the bacterial plant pathogen Ralstonia solanacearum (PubMed:24947605).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621PROSITE-ProRule annotation
Active sitei298 – 2981PROSITE-ProRule annotation
Active sitei318 – 3181PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • defense response Source: UniProtKB-KW
  • developmental programmed cell death Source: TAIR
  • proteolysis involved in cellular protein catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Plant defense

Enzyme and pathway databases

BioCyciARA:AT1G20850-MONOMER.

Protein family/group databases

MEROPSiC01.120.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine protease XCP2Curated (EC:3.4.22.-)
Alternative name(s):
Xylem cysteine peptidase 21 Publication
Short name:
AtXCP21 Publication
Gene namesi
Name:XCP21 Publication
Ordered Locus Names:At1g20850
ORF Names:F2D10.37, F9H16.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G20850.

Subcellular locationi

  • Vacuole By similarity
  • Cell membrane By similarity

  • Note: Predominantly vacuolar. May be associated to plasma membrane.By similarity

GO - Cellular componenti

  • cell wall Source: TAIR
  • extracellular space Source: GO_Central
  • lysosome Source: GO_Central
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Vacuole

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but mutant plants show increased resistance to infection by the bacterial wilt pathogen Ralstonia solanacearum.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Propeptidei27 – 137111Activation peptideCuratedPRO_0000026469Add
BLAST
Chaini138 – 356219Cysteine protease XCP2PRO_0000026470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi159 ↔ 201By similarity
Glycosylationi181 – 1811N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi193 ↔ 234By similarity
Disulfide bondi292 ↔ 343By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9LM66.
PRIDEiQ9LM66.

Expressioni

Tissue specificityi

Mostly expressed in roots, stems and flowers. Confined to tracheary elements, and specifically to xylem.2 Publications

Gene expression databases

ExpressionAtlasiQ9LM66. baseline and differential.
GenevisibleiQ9LM66. AT.

Interactioni

Subunit structurei

Interacts with PRN2.1 Publication

Protein-protein interaction databases

BioGridi23916. 2 interactions.
IntActiQ9LM66. 2 interactions.
STRINGi3702.AT1G20850.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LM66.
SMRiQ9LM66. Positions 41-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000230773.
InParanoidiQ9LM66.
KOiK16290.
OMAiLYKMASY.
PhylomeDBiQ9LM66.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9LM66-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSSPSRIL CFALALSAAS LSLSFASSHD YSIVGYSPED LESHDKLIEL
60 70 80 90 100
FENWISNFEK AYETVEEKFL RFEVFKDNLK HIDETNKKGK SYWLGLNEFA
110 120 130 140 150
DLSHEEFKKM YLGLKTDIVR RDEERSYAEF AYRDVEAVPK SVDWRKKGAV
160 170 180 190 200
AEVKNQGSCG SCWAFSTVAA VEGINKIVTG NLTTLSEQEL IDCDTTYNNG
210 220 230 240 250
CNGGLMDYAF EYIVKNGGLR KEEDYPYSME EGTCEMQKDE SETVTINGHQ
260 270 280 290 300
DVPTNDEKSL LKALAHQPLS VAIDASGREF QFYSGGVFDG RCGVDLDHGV
310 320 330 340 350
AAVGYGSSKG SDYIIVKNSW GPKWGEKGYI RLKRNTGKPE GLCGINKMAS

FPTKTK
Length:356
Mass (Da):39,708
Last modified:July 19, 2005 - v2
Checksum:i503696D19B14C2BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191028 mRNA. Translation: AAF25832.1.
AC007369 Genomic DNA. Translation: AAD30607.1.
AC069251 Genomic DNA. Translation: AAF80626.1.
CP002684 Genomic DNA. Translation: AEE30031.1.
BT004822 mRNA. Translation: AAO44088.1.
AK227749 mRNA. Translation: BAE99733.1.
PIRiA86341.
RefSeqiNP_564126.1. NM_101938.4.
UniGeneiAt.21316.

Genome annotation databases

EnsemblPlantsiAT1G20850.1; AT1G20850.1; AT1G20850.
GeneIDi838677.
GrameneiAT1G20850.1; AT1G20850.1; AT1G20850.
KEGGiath:AT1G20850.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191028 mRNA. Translation: AAF25832.1.
AC007369 Genomic DNA. Translation: AAD30607.1.
AC069251 Genomic DNA. Translation: AAF80626.1.
CP002684 Genomic DNA. Translation: AEE30031.1.
BT004822 mRNA. Translation: AAO44088.1.
AK227749 mRNA. Translation: BAE99733.1.
PIRiA86341.
RefSeqiNP_564126.1. NM_101938.4.
UniGeneiAt.21316.

3D structure databases

ProteinModelPortaliQ9LM66.
SMRiQ9LM66. Positions 41-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23916. 2 interactions.
IntActiQ9LM66. 2 interactions.
STRINGi3702.AT1G20850.1.

Protein family/group databases

MEROPSiC01.120.

Proteomic databases

PaxDbiQ9LM66.
PRIDEiQ9LM66.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G20850.1; AT1G20850.1; AT1G20850.
GeneIDi838677.
GrameneiAT1G20850.1; AT1G20850.1; AT1G20850.
KEGGiath:AT1G20850.

Organism-specific databases

TAIRiAT1G20850.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000230773.
InParanoidiQ9LM66.
KOiK16290.
OMAiLYKMASY.
PhylomeDBiQ9LM66.

Enzyme and pathway databases

BioCyciARA:AT1G20850-MONOMER.

Miscellaneous databases

PROiQ9LM66.

Gene expression databases

ExpressionAtlasiQ9LM66. baseline and differential.
GenevisibleiQ9LM66. AT.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Exploiting secondary growth in Arabidopsis. Construction of xylem and bark cDNA libraries and cloning of three xylem endopeptidases."
    Zhao C., Johnson B.J., Kositsup B., Beers E.P.
    Plant Physiol. 123:1185-1196(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Xylem.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "The Arabidopsis xylem peptidase XCP1 is a tracheary element vacuolar protein that may be a papain ortholog."
    Funk V., Kositsup B., Zhao C., Beers E.P.
    Plant Physiol. 128:84-94(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Cysteine proteases XCP1 and XCP2 aid micro-autolysis within the intact central vacuole during xylogenesis in Arabidopsis roots."
    Avci U., Petzold H.E., Ismail I.O., Beers E.P., Haigler C.H.
    Plant J. 56:303-315(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "PIRIN2 stabilizes cysteine protease XCP2 and increases susceptibility to the vascular pathogen Ralstonia solanacearum in Arabidopsis."
    Zhang B., Tremousaygue D., Denance N., van Esse H.P., Hoerger A.C., Dabos P., Goffner D., Thomma B.P., van der Hoorn R.A., Tuominen H.
    Plant J. 79:1009-1019(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRN2, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiXCP2_ARATH
AccessioniPrimary (citable) accession number: Q9LM66
Secondary accession number(s): Q0WT15, Q9SYQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 6, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.