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O65493

- XCP1_ARATH

UniProt

O65493 - XCP1_ARATH

Protein

Xylem cysteine proteinase 1

Gene

XCP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Probable thiol protease.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei161 – 1611By similarity
    Active sitei297 – 2971By similarity
    Active sitei317 – 3171By similarity

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. developmental programmed cell death Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BioCyciARA:AT4G35350-MONOMER.
    ARA:GQT-1554-MONOMER.

    Protein family/group databases

    MEROPSiC01.065.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xylem cysteine proteinase 1 (EC:3.4.22.-)
    Short name:
    AtXCP1
    Gene namesi
    Name:XCP1
    Ordered Locus Names:At4g35350
    ORF Names:F23E12.90
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G35350.

    Subcellular locationi

    Vacuole 1 Publication. Cell membrane 1 Publication
    Note: Predominantly vacuolar. May be associated to plasma membrane.

    GO - Cellular componenti

    1. nucleus Source: TAIR
    2. plant-type vacuole Source: TAIR
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 355Xylem cysteine proteinase 1PRO_0000026468
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Propeptidei29 – ?Activation peptideBy similarityPRO_0000026467

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi158 ↔ 200By similarity
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi192 ↔ 233By similarity
    Disulfide bondi291 ↔ 342By similarity

    Post-translational modificationi

    Autocleaves.

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiO65493.
    PRIDEiO65493.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO65493.
    GenevestigatoriO65493.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G35350.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliO65493.
    SMRiO65493. Positions 41-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000230773.
    InParanoidiO65493.
    KOiK16290.
    OMAiPRNNEQA.
    PhylomeDBiO65493.

    Family and domain databases

    InterProiIPR000169. 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]
    PROSITEiPS00139. 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.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: O65493-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAFSAPSLSK FSLLVAISAS ALLCCAFARD FSIVGYTPEH LTNTDKLLEL    50
    FESWMSEHSK AYKSVEEKVH RFEVFRENLM HIDQRNNEIN SYWLGLNEFA 100
    DLTHEEFKGR YLGLAKPQFS RKRQPSANFR YRDITDLPKS VDWRKKGAVA 150
    PVKDQGQCGS CWAFSTVAAV EGINQITTGN LSSLSEQELI DCDTTFNSGC 200
    NGGLMDYAFQ YIISTGGLHK EDDYPYLMEE GICQEQKEDV ERVTISGYED 250
    VPENDDESLV KALAHQPVSV AIEASGRDFQ FYKGGVFNGK CGTDLDHGVA 300
    AVGYGSSKGS DYVIVKNSWG PRWGEKGFIR MKRNTGKPEG LCGINKMASY 350
    PTKTK 355
    Length:355
    Mass (Da):39,618
    Last modified:August 1, 1998 - v1
    Checksum:i0EB501744967A427
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191027 mRNA. Translation: AAF25831.1.
    AL022604 Genomic DNA. Translation: CAA18734.1.
    AL161587 Genomic DNA. Translation: CAB80252.1.
    CP002687 Genomic DNA. Translation: AEE86501.1.
    AK117394 mRNA. Translation: BAC42063.1.
    BT005179 mRNA. Translation: AAO50712.1.
    PIRiT06122.
    RefSeqiNP_567983.1. NM_119701.3. [O65493-1]
    UniGeneiAt.2280.
    At.67622.

    Genome annotation databases

    EnsemblPlantsiAT4G35350.1; AT4G35350.1; AT4G35350. [O65493-1]
    GeneIDi829688.
    KEGGiath:AT4G35350.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191027 mRNA. Translation: AAF25831.1 .
    AL022604 Genomic DNA. Translation: CAA18734.1 .
    AL161587 Genomic DNA. Translation: CAB80252.1 .
    CP002687 Genomic DNA. Translation: AEE86501.1 .
    AK117394 mRNA. Translation: BAC42063.1 .
    BT005179 mRNA. Translation: AAO50712.1 .
    PIRi T06122.
    RefSeqi NP_567983.1. NM_119701.3. [O65493-1 ]
    UniGenei At.2280.
    At.67622.

    3D structure databases

    ProteinModelPortali O65493.
    SMRi O65493. Positions 41-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G35350.1-P.

    Protein family/group databases

    MEROPSi C01.065.

    Proteomic databases

    PaxDbi O65493.
    PRIDEi O65493.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G35350.1 ; AT4G35350.1 ; AT4G35350 . [O65493-1 ]
    GeneIDi 829688.
    KEGGi ath:AT4G35350.

    Organism-specific databases

    GeneFarmi 5033.
    TAIRi AT4G35350.

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000230773.
    InParanoidi O65493.
    KOi K16290.
    OMAi PRNNEQA.
    PhylomeDBi O65493.

    Enzyme and pathway databases

    BioCyci ARA:AT4G35350-MONOMER.
    ARA:GQT-1554-MONOMER.

    Gene expression databases

    ArrayExpressi O65493.
    Genevestigatori O65493.

    Family and domain databases

    InterProi IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "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.
    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, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiXCP1_ARATH
    AccessioniPrimary (citable) accession number: O65493
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 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

    External Data

    Dasty 3