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O24371

- LOX31_SOLTU

UniProt

O24371 - LOX31_SOLTU

Protein

Linoleate 13S-lipoxygenase 3-1, chloroplastic

Gene

LOX3.1

Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Required for the regulation of wound-induced gene expression, but is not involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids.2 Publications

    Catalytic activityi

    Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate.1 Publication
    Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate.1 Publication

    Cofactori

    Binds 1 iron ion per subunit.PROSITE-ProRule annotation

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi574 – 5741Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi579 – 5791Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi765 – 7651Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi769 – 7691Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi914 – 9141Iron; via carboxylate; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. linoleate 13S-lipoxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. oxylipin biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Linoleate 13S-lipoxygenase 3-1, chloroplastic (EC:1.13.11.12)
    Gene namesi
    Name:LOX3.1
    Synonyms:LOX-H3
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    ProteomesiUP000011115: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast stroma Source: UniProtKB-SubCell
    2. chloroplast thylakoid Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid, Thylakoid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8383ChloroplastSequence AnalysisAdd
    BLAST
    Chaini84 – 914831Linoleate 13S-lipoxygenase 3-1, chloroplasticPRO_0000412928Add
    BLAST

    Expressioni

    Tissue specificityi

    Expressed in roots and leaves. Detected in tubers and flower buds.1 Publication

    Inductioni

    Up-regulated localy and systemically 30 minutes after wounding. Up-regulated by jasmonate and abscisic acid treatment. Not induced by pathogen infection.3 Publications

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO24371.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini96 – 218123PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini221 – 914694LipoxygenasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the lipoxygenase family.Curated
    Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
    Contains 1 PLAT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KOiK00454.

    Family and domain databases

    Gene3Di2.60.60.20. 1 hit.
    4.10.372.10. 1 hit.
    InterProiIPR008976. Lipase_LipOase.
    IPR000907. LipOase.
    IPR013819. LipOase_C.
    IPR020834. LipOase_CS.
    IPR020833. LipOase_Fe_BS.
    IPR001246. LipOase_pln.
    IPR027433. Lipoxygenase_domain_3.
    IPR001024. PLAT/LH2_dom.
    [Graphical view]
    PANTHERiPTHR11771. PTHR11771. 1 hit.
    PfamiPF00305. Lipoxygenase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view]
    PRINTSiPR00087. LIPOXYGENASE.
    PR00468. PLTLPOXGNASE.
    SMARTiSM00308. LH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48484. SSF48484. 1 hit.
    SSF49723. SSF49723. 1 hit.
    PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
    PS00081. LIPOXYGENASE_2. 1 hit.
    PS51393. LIPOXYGENASE_3. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O24371-1 [UniParc]FASTAAdd to Basket

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    MALAKEIMGI SLLEKSSSFM NSSSMALFNP NNYHKENHLW FNQQFQGRRN    50
    LSRRKAFRQS TMAAISENLI KVVPEKAVRF KVRAVVTVRN KNKEDLKETI 100
    VKHLDAFTDK IGRNVTLELI STDMDPNTKG PKKSNQAVLK DWSKKSNLKT 150
    ERVNYTAEFI VDSNFGNPGA ITVTNKHQQE FFLESITIEG FACGPVHFPC 200
    NSWVQPKKDH PGKRIFFSNQ PYLPDETPAG LKSLRERELR DLRGDGKGVR 250
    KLSDRIYDYD IYNDLGNPDK GIDFARPKLG GDDNVPYPRR CRSGRVPTDT 300
    DISAESRVEK PNPTYVPRDE QFEESKMNTF STSRLKAVLH NLIPSLMASI 350
    SSNNHDFKGF SDIDNLYSKG LLLKLGLQDE VLKKLPLPKV VSSIKEGDLL 400
    KYDTPKILSK DKFAWLRDDE FARQAIAGVN PVSIEKLQFF PPVSKLDPEI 450
    YGPQESALKE EHILGHLNGM TVQEALDANK LFIVDHHDVY LPFLDRINAL 500
    DGRKAYATRT IFFLSDVGTL KPIAIELSLP QTGPSSRSKR VVTPPVCATG 550
    NWTWQIAKAH VCANDAGVHQ LVNHWLRTHA SLEPFILAAH RQLSAMHPIY 600
    KLLDPHMRYT LEINGLARQS LINADGVIEA CFTPGRYCME ISAAAYKNWR 650
    FDLEGLPADL IRRGMAVPDS TQPHGLKLLI EDYPYAADGL MIWGAIESWV 700
    RDYVNHYYPS SAQVCSDREL QAWYAETINV GHVDLRNEEW WPTLATPEDL 750
    ISILTTLIWL ASAQHAALNF GQYPYGGYVP NRPPLMRRLI PDENDPEYAV 800
    FLADPQKYFF SALPSLLQAT KFMAVVDTLS THSPDEEYLG ERHQPSTWTG 850
    DAEIVEAFYK FSAEIGRIEK EIDERNANTK LKNRCGAGVL PYELLAPSSG 900
    PGVTCRGVPN SVSI 914
    Length:914
    Mass (Da):103,089
    Last modified:January 1, 1998 - v1
    Checksum:i45BBC7D7180390E4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96406 mRNA. Translation: CAA65269.1.
    PIRiT07065.
    RefSeqiNP_001275115.1. NM_001288186.1.
    UniGeneiStu.213.

    Genome annotation databases

    GeneIDi102597498.
    KEGGisot:102597498.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96406 mRNA. Translation: CAA65269.1 .
    PIRi T07065.
    RefSeqi NP_001275115.1. NM_001288186.1.
    UniGenei Stu.213.

    3D structure databases

    ProteinModelPortali O24371.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 102597498.
    KEGGi sot:102597498.

    Phylogenomic databases

    KOi K00454.

    Enzyme and pathway databases

    UniPathwayi UPA00382 .

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    4.10.372.10. 1 hit.
    InterProi IPR008976. Lipase_LipOase.
    IPR000907. LipOase.
    IPR013819. LipOase_C.
    IPR020834. LipOase_CS.
    IPR020833. LipOase_Fe_BS.
    IPR001246. LipOase_pln.
    IPR027433. Lipoxygenase_domain_3.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11771. PTHR11771. 1 hit.
    Pfami PF00305. Lipoxygenase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PRINTSi PR00087. LIPOXYGENASE.
    PR00468. PLTLPOXGNASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48484. SSF48484. 1 hit.
    SSF49723. SSF49723. 1 hit.
    PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
    PS00081. LIPOXYGENASE_2. 1 hit.
    PS51393. LIPOXYGENASE_3. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns."
      Royo J., Vancanneyt G., Perez A.G., Sanz C., Stormann K., Rosahl S., Sanchez-Serrano J.J.
      J. Biol. Chem. 271:21012-21019(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY WOUNDING; JASMONATE AND ABSCISIC ACID, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Leaf.
    2. "Antisense-mediated depletion of a potato lipoxygenase reduces wound induction of proteinase inhibitors and increases weight gain of insect pests."
      Royo J., Leon J., Vancanneyt G., Albar J.P., Rosahl S., Ortego F., Castanera P., Sanchez-Serrano J.J.
      Proc. Natl. Acad. Sci. U.S.A. 96:1146-1151(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    3. "A leaf lipoxygenase of potato induced specifically by pathogen infection."
      Kolomiets M.V., Chen H., Gladon R.J., Braun E.J., Hannapel D.J.
      Plant Physiol. 124:1121-1130(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY PATHOGEN.
    4. "Lipoxygenase H1 gene silencing reveals a specific role in supplying fatty acid hydroperoxides for aliphatic aldehyde production."
      Leon J., Royo J., Vancanneyt G., Sanz C., Silkowski H., Griffiths G., Sanchez-Serrano J.J.
      J. Biol. Chem. 277:416-423(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. "Differential distribution of the lipoxygenase pathway enzymes within potato chloroplasts."
      Farmaki T., Sanmartin M., Jimenez P., Paneque M., Sanz C., Vancanneyt G., Leon J., Sanchez-Serrano J.J.
      J. Exp. Bot. 58:555-568(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION BY WOUNDING.

    Entry informationi

    Entry nameiLOX31_SOLTU
    AccessioniPrimary (citable) accession number: O24371
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Depletion of LOX-H3 by co-suppression-mediated gene silencing leads to higher tuber yield, but has no effect on the number of tubers per plant.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3