XCP1_ARATH
ID XCP1_ARATH Reviewed; 355 AA.
AC O65493;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cysteine protease XCP1 {ECO:0000305};
DE EC=3.4.22.-;
DE AltName: Full=Xylem cysteine peptidase 1 {ECO:0000303|PubMed:10889267};
DE Short=AtXCP1 {ECO:0000303|PubMed:10889267};
DE Flags: Precursor;
GN Name=XCP1 {ECO:0000303|PubMed:10889267}; OrderedLocusNames=At4g35350;
GN ORFNames=F23E12.90;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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).
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. {ECO:0000269|PubMed:18573193}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:11788755}. Cell
CC membrane {ECO:0000269|PubMed:11788755}. Note=Predominantly vacuolar.
CC May be associated to plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O65493-1; Sequence=Displayed;
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 -!- PTM: Autocleaves.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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DR EMBL; AF191027; AAF25831.1; -; mRNA.
DR EMBL; AL022604; CAA18734.1; -; Genomic_DNA.
DR EMBL; AL161587; CAB80252.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86501.1; -; Genomic_DNA.
DR EMBL; AK117394; BAC42063.1; -; mRNA.
DR EMBL; BT005179; AAO50712.1; -; mRNA.
DR PIR; T06122; T06122.
DR RefSeq; NP_567983.1; NM_119701.4. [O65493-1]
DR AlphaFoldDB; O65493; -.
DR SMR; O65493; -.
DR STRING; 3702.AT4G35350.1; -.
DR MEROPS; C01.065; -.
DR MEROPS; I29.003; -.
DR PaxDb; O65493; -.
DR PRIDE; O65493; -.
DR ProteomicsDB; 242374; -. [O65493-1]
DR EnsemblPlants; AT4G35350.1; AT4G35350.1; AT4G35350. [O65493-1]
DR GeneID; 829688; -.
DR Gramene; AT4G35350.1; AT4G35350.1; AT4G35350. [O65493-1]
DR KEGG; ath:AT4G35350; -.
DR Araport; AT4G35350; -.
DR TAIR; locus:2122113; AT4G35350.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; O65493; -.
DR OMA; LYNVPNC; -.
DR PhylomeDB; O65493; -.
DR PRO; PR:O65493; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65493; baseline and differential.
DR Genevisible; O65493; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
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: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; 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; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autocatalytic cleavage; Cell membrane;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal; Thiol protease; Vacuole; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..136
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026467"
FT CHAIN 137..355
FT /note="Cysteine protease XCP1"
FT /id="PRO_0000026468"
FT ACT_SITE 161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 158..200
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 192..233
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 291..342
FT /evidence="ECO:0000250|UniProtKB:P84346"
SQ SEQUENCE 355 AA; 39618 MW; 0EB501744967A427 CRC64;
MAFSAPSLSK FSLLVAISAS ALLCCAFARD FSIVGYTPEH LTNTDKLLEL FESWMSEHSK
AYKSVEEKVH RFEVFRENLM HIDQRNNEIN SYWLGLNEFA DLTHEEFKGR YLGLAKPQFS
RKRQPSANFR YRDITDLPKS VDWRKKGAVA PVKDQGQCGS CWAFSTVAAV EGINQITTGN
LSSLSEQELI DCDTTFNSGC NGGLMDYAFQ YIISTGGLHK EDDYPYLMEE GICQEQKEDV
ERVTISGYED VPENDDESLV KALAHQPVSV AIEASGRDFQ FYKGGVFNGK CGTDLDHGVA
AVGYGSSKGS DYVIVKNSWG PRWGEKGFIR MKRNTGKPEG LCGINKMASY PTKTK
