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Q9LNR3

- LOX3_ARATH

UniProt

Q9LNR3 - LOX3_ARATH

Protein

Lipoxygenase 3, chloroplastic

Gene

LOX3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    13S-lipoxygenase that can use linolenic acid as substrates. 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. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 iron ion per subunit.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi578 – 5781Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi583 – 5831Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi770 – 7701Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi774 – 7741Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi919 – 9191Iron; via carboxylate; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. anther dehiscence Source: TAIR
    2. anther development Source: TAIR
    3. lipid oxidation Source: TAIR
    4. oxylipin biosynthetic process Source: UniProtKB-UniPathway
    5. pollen development Source: TAIR
    6. response to fungus Source: TAIR
    7. response to high light intensity Source: UniProtKB
    8. response to jasmonic acid Source: UniProtKB
    9. response to wounding Source: UniProtKB
    10. stamen filament development Source: TAIR

    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:
    Lipoxygenase 3, chloroplastic (EC:1.13.11.12)
    Short name:
    AtLOX3
    Gene namesi
    Name:LOX3
    Ordered Locus Names:At1g17420
    ORF Names:F28G4.10
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G17420.

    Subcellular locationi

    Plastidchloroplast Curated

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5252ChloroplastSequence AnalysisAdd
    BLAST
    Chaini53 – 919867Lipoxygenase 3, chloroplasticPRO_0000380592Add
    BLAST

    Proteomic databases

    PaxDbiQ9LNR3.
    PRIDEiQ9LNR3.

    Expressioni

    Tissue specificityi

    Expressed in roots and leaves.1 Publication

    Developmental stagei

    First observed in lateral root primordia (LRP), from the first pericycle divisions. Later expressed in lateral roots. Expression is greatly increased in leaves during leaf senescence.2 Publications

    Inductioni

    Induced by methyl jasmonate (MeJA), bacterial pathogens (e.g. Pseudomonas syringae pv. tomato), high light and wounding.3 Publications

    Gene expression databases

    GenevestigatoriQ9LNR3.

    Interactioni

    Protein-protein interaction databases

    BioGridi23554. 1 interaction.
    IntActiQ9LNR3. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LNR3.
    SMRiQ9LNR3. Positions 108-919.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini86 – 222137PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini225 – 919695LipoxygenasePROSITE-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

    eggNOGiNOG69653.
    HOGENOMiHOG000230469.
    InParanoidiQ9LNR3.
    KOiK00454.
    OMAiLSKDKFA.
    PhylomeDBiQ9LNR3.

    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.

    Q9LNR3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALAKELMGY PLITERSSLV SSASHFKKRT QSTQFSINPF DRRPRKTKSG    50
    VVAAISEDLV KTLRFSTTTG DRKSEEEEKA AVKFKVRAVV TVRNKNKEDL 100
    KETLVKHLDA FADKIGRNIV LELISTQLDP KTKLPKKSNA AVLKDWSKKS 150
    KTKAERVHYT AEFTVDAAFG SPGAITVMNK HQKEFFLESI TIEGFALGPV 200
    HFPCNSWVQS QKDHPDKRIF FTNQPYLPNE TPSGLRVLRE KELKNLRGDG 250
    SGVRKLSDRI YDFDVYNDLG NPDKSSELSR PKLGGKEVPY PRRCRTGRQS 300
    TVSDKDAESR VEKPLPMYVP RDEQFEESKQ DTFAAGRLKA VLHHLIPSLK 350
    ASIVAEDFAD FGEIDRLYKE GLLLKLGFQD DIFKKFPLPK VVVDTLQEST 400
    KGLLKYDTPK ILSKDKNAWL RDDEFARQAI AGINPVNIER VKTFPPVSNL 450
    DPKIYGPQHS ALTDDHIIGH LDGFSVQQAL EENRLYMLDY HDIFLPFLDR 500
    INALDGRKAY ATRTIFFLTR LGTLKPVAIE LSLPPHGPKH RSKRVLTPPV 550
    DATSNWMWQL AKAHVSSNDA GVHQLVNHWL RTHACLEPFI LAAHRQLSAM 600
    HPIFKLLDPH MRYTLEINAL ARQSLISADG VIEGGFTAGA YGMEMSAAAY 650
    KSSWRFDMEG LPADLIRRGM AIPDATQPHG LKLLIEDYPY ANDGLLLWSA 700
    IQTWVRTYVE RYYPNPNLIK TDSELQSWYS ESINVGHADL RDADWWPELS 750
    TVDDLVSILT TLIWLASAQH AALNFGQYPY GGYVPNRPPL MRRLIPDESD 800
    PEYASFISHP EKYYFSSMPS LAQTSKFMAV VDTLSTHSPD EEYIGERQQP 850
    SIWTGDAEIV EAFYGFAAEI GRIEKEIEKR NADPDRRNRC GAGVLPYELL 900
    VPSSEPGVTC RGVPNSVSI 919
    Length:919
    Mass (Da):103,726
    Last modified:October 1, 2000 - v1
    Checksum:i194A0B150273E44C
    GO

    Sequence cautioni

    The sequence AAF97315.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti374 – 3741L → P in CAB56692. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ249794 mRNA. Translation: CAB56692.1.
    AC007843 Genomic DNA. Translation: AAF97315.1. Different initiation.
    AC022492 Genomic DNA. Translation: AAF79461.1.
    CP002684 Genomic DNA. Translation: AEE29585.1.
    AY075625 mRNA. Translation: AAL91636.1.
    BT006348 mRNA. Translation: AAP21156.1.
    RefSeqiNP_564021.1. NM_101603.2.
    UniGeneiAt.20467.
    At.64244.
    At.67022.

    Genome annotation databases

    EnsemblPlantsiAT1G17420.1; AT1G17420.1; AT1G17420.
    GeneIDi838314.
    KEGGiath:AT1G17420.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ249794 mRNA. Translation: CAB56692.1 .
    AC007843 Genomic DNA. Translation: AAF97315.1 . Different initiation.
    AC022492 Genomic DNA. Translation: AAF79461.1 .
    CP002684 Genomic DNA. Translation: AEE29585.1 .
    AY075625 mRNA. Translation: AAL91636.1 .
    BT006348 mRNA. Translation: AAP21156.1 .
    RefSeqi NP_564021.1. NM_101603.2.
    UniGenei At.20467.
    At.64244.
    At.67022.

    3D structure databases

    ProteinModelPortali Q9LNR3.
    SMRi Q9LNR3. Positions 108-919.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 23554. 1 interaction.
    IntActi Q9LNR3. 1 interaction.

    Proteomic databases

    PaxDbi Q9LNR3.
    PRIDEi Q9LNR3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G17420.1 ; AT1G17420.1 ; AT1G17420 .
    GeneIDi 838314.
    KEGGi ath:AT1G17420.

    Organism-specific databases

    TAIRi AT1G17420.

    Phylogenomic databases

    eggNOGi NOG69653.
    HOGENOMi HOG000230469.
    InParanoidi Q9LNR3.
    KOi K00454.
    OMAi LSKDKFA.
    PhylomeDBi Q9LNR3.

    Enzyme and pathway databases

    UniPathwayi UPA00382 .

    Gene expression databases

    Genevestigatori Q9LNR3.

    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. "The second chloroplastic jasmonate-inducible 13-LOX from Arabidopsis leaves."
      Fritsche K., Feussner I.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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. "Evidence supporting a role of jasmonic acid in Arabidopsis leaf senescence."
      He Y., Fukushige H., Hildebrand D.F., Gan S.
      Plant Physiol. 128:876-884(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    6. "Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade."
      Vellosillo T., Martinez M., Lopez M.A., Vicente J., Cascon T., Dolan L., Hamberg M., Castresana C.
      Plant Cell 19:831-846(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Systemic and intracellular responses to photooxidative stress in Arabidopsis."
      Rossel J.B., Wilson P.B., Hussain D., Woo N.S., Gordon M.J., Mewett O.P., Howell K.A., Whelan J., Kazan K., Pogson B.J.
      Plant Cell 19:4091-4110(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HIGH LIGHT.
    8. "Identification and characterization of COI1-dependent transcription factor genes involved in JA-mediated response to wounding in Arabidopsis plants."
      Wang Z., Cao G., Wang X., Miao J., Liu X., Chen Z., Qu L.-J., Gu H.
      Plant Cell Rep. 27:125-135(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY WOUNDING.
    9. "Mapping methyl jasmonate-mediated transcriptional reprogramming of metabolism and cell cycle progression in cultured Arabidopsis cells."
      Pauwels L., Morreel K., De Witte E., Lammertyn F., Van Montagu M., Boerjan W., Inze D., Goossens A.
      Proc. Natl. Acad. Sci. U.S.A. 105:1380-1385(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY JASMONATE.
    10. "Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana."
      Bannenberg G., Martinez M., Hamberg M., Castresana C.
      Lipids 44:85-95(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiLOX3_ARATH
    AccessioniPrimary (citable) accession number: Q9LNR3
    Secondary accession number(s): Q9LQJ5, Q9SMW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 106 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3