XCP2_ARATH
ID XCP2_ARATH Reviewed; 356 AA.
AC Q9LM66; Q0WT15; Q9SYQ2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cysteine protease XCP2 {ECO:0000305};
DE EC=3.4.22.-;
DE AltName: Full=Xylem cysteine peptidase 2 {ECO:0000303|PubMed:10889267};
DE Short=AtXCP2 {ECO:0000303|PubMed:10889267};
DE Flags: Precursor;
GN Name=XCP2 {ECO:0000303|PubMed:10889267}; OrderedLocusNames=At1g20850;
GN ORFNames=F2D10.37, F9H16.17;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Xylem;
RX PubMed=10889267; DOI=10.1104/pp.123.3.1185;
RA Zhao C., Johnson B.J., Kositsup B., Beers E.P.;
RT "Exploiting secondary growth in Arabidopsis. Construction of xylem and bark
RT cDNA libraries and cloning of three xylem endopeptidases.";
RL Plant Physiol. 123:1185-1196(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11788755; DOI=10.1104/pp.010514;
RA Funk V., Kositsup B., Zhao C., Beers E.P.;
RT "The Arabidopsis xylem peptidase XCP1 is a tracheary element vacuolar
RT protein that may be a papain ortholog.";
RL Plant Physiol. 128:84-94(2002).
RN [7]
RP FUNCTION.
RX PubMed=18573193; DOI=10.1111/j.1365-313x.2008.03592.x;
RA Avci U., Petzold H.E., Ismail I.O., Beers E.P., Haigler C.H.;
RT "Cysteine proteases XCP1 and XCP2 aid micro-autolysis within the intact
RT central vacuole during xylogenesis in Arabidopsis roots.";
RL Plant J. 56:303-315(2008).
RN [8]
RP FUNCTION, INTERACTION WITH PRN2, AND DISRUPTION PHENOTYPE.
RX PubMed=24947605; DOI=10.1111/tpj.12602;
RA Zhang B., Tremousaygue D., Denance N., van Esse H.P., Hoerger A.C.,
RA Dabos P., Goffner D., Thomma B.P., van der Hoorn R.A., Tuominen H.;
RT "PIRIN2 stabilizes cysteine protease XCP2 and increases susceptibility to
RT the vascular pathogen Ralstonia solanacearum in Arabidopsis.";
RL Plant J. 79:1009-1019(2014).
CC -!- FUNCTION: Cysteine protease involved in xylem tracheary element (TE)
CC autolysis during xylogenesis in roots. Participates in micro autolysis
CC within the intact central vacuole before mega autolysis is initiated by
CC tonoplast implosion (PubMed:18573193). Involved in susceptibility to
CC the bacterial plant pathogen Ralstonia solanacearum (PubMed:24947605).
CC {ECO:0000269|PubMed:18573193, ECO:0000269|PubMed:24947605}.
CC -!- SUBUNIT: Interacts with PRN2. {ECO:0000269|PubMed:24947605}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:O65493}. Cell
CC membrane {ECO:0000250|UniProtKB:O65493}. Note=Predominantly vacuolar.
CC May be associated to plasma membrane. {ECO:0000250|UniProtKB:O65493}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, stems and flowers.
CC Confined to tracheary elements, and specifically to xylem.
CC {ECO:0000269|PubMed:10889267, ECO:0000269|PubMed:11788755}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show increased resistance to infection by
CC the bacterial wilt pathogen Ralstonia solanacearum.
CC {ECO:0000269|PubMed:24947605}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF191028; AAF25832.1; -; mRNA.
DR EMBL; AC007369; AAD30607.1; -; Genomic_DNA.
DR EMBL; AC069251; AAF80626.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30031.1; -; Genomic_DNA.
DR EMBL; BT004822; AAO44088.1; -; mRNA.
DR EMBL; AK227749; BAE99733.1; -; mRNA.
DR PIR; A86341; A86341.
DR RefSeq; NP_564126.1; NM_101938.5.
DR AlphaFoldDB; Q9LM66; -.
DR SMR; Q9LM66; -.
DR BioGRID; 23916; 2.
DR IntAct; Q9LM66; 2.
DR STRING; 3702.AT1G20850.1; -.
DR MEROPS; C01.065; -.
DR PaxDb; Q9LM66; -.
DR PRIDE; Q9LM66; -.
DR ProteomicsDB; 242775; -.
DR EnsemblPlants; AT1G20850.1; AT1G20850.1; AT1G20850.
DR GeneID; 838677; -.
DR Gramene; AT1G20850.1; AT1G20850.1; AT1G20850.
DR KEGG; ath:AT1G20850; -.
DR Araport; AT1G20850; -.
DR TAIR; locus:2030427; AT1G20850.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; Q9LM66; -.
DR OMA; PVGNEKA; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9LM66; -.
DR PRO; PR:Q9LM66; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LM66; baseline and differential.
DR Genevisible; Q9LM66; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:TAIR.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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; IPR025660; Pept_his_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.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Plant defense; Protease; Reference proteome; Signal; Thiol protease;
KW Vacuole; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..137
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026469"
FT CHAIN 138..356
FT /note="Cysteine protease XCP2"
FT /id="PRO_0000026470"
FT ACT_SITE 162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 159..201
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 193..234
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 292..343
FT /evidence="ECO:0000250|UniProtKB:P84346"
SQ SEQUENCE 356 AA; 39708 MW; 503696D19B14C2BF CRC64;
MALSSPSRIL CFALALSAAS LSLSFASSHD YSIVGYSPED LESHDKLIEL FENWISNFEK
AYETVEEKFL RFEVFKDNLK HIDETNKKGK SYWLGLNEFA DLSHEEFKKM YLGLKTDIVR
RDEERSYAEF AYRDVEAVPK SVDWRKKGAV AEVKNQGSCG SCWAFSTVAA VEGINKIVTG
NLTTLSEQEL IDCDTTYNNG CNGGLMDYAF EYIVKNGGLR KEEDYPYSME EGTCEMQKDE
SETVTINGHQ DVPTNDEKSL LKALAHQPLS VAIDASGREF QFYSGGVFDG RCGVDLDHGV
AAVGYGSSKG SDYIIVKNSW GPKWGEKGYI RLKRNTGKPE GLCGINKMAS FPTKTK
