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Q9FNX8

- LOX4_ARATH

UniProt

Q9FNX8 - LOX4_ARATH

Protein

Lipoxygenase 4, chloroplastic

Gene

LOX4

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 105 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure By similarity. 13S-lipoxygenase that can use linolenic acid as substrates.1 PublicationPROSITE-ProRule annotation

    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 bindingi585 – 5851Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi590 – 5901Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi777 – 7771Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi781 – 7811Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi926 – 9261Iron; 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 bacterium Source: UniProtKB
    7. response to ozone Source: UniProtKB
    8. response to wounding Source: UniProtKB
    9. 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 4, chloroplastic (EC:1.13.11.12)
    Short name:
    AtLOX4
    Alternative name(s):
    LOX3-like protein
    Gene namesi
    Name:LOX4
    Synonyms:LOX3
    Ordered Locus Names:At1g72520
    ORF Names:F28P22.29, T10D10.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G72520.

    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 – 5858ChloroplastSequence AnalysisAdd
    BLAST
    Chaini59 – 926868Lipoxygenase 4, chloroplasticPRO_0000380593Add
    BLAST

    Proteomic databases

    PaxDbiQ9FNX8.
    PRIDEiQ9FNX8.

    Expressioni

    Tissue specificityi

    Expressed in leaves.1 Publication

    Developmental stagei

    Expression is greatly increased in leaves during leaf senescence.1 Publication

    Inductioni

    Induced by bacterial pathogens (e.g. Pseudomonas syringae pv. tomato), ozone O3, and wounding.2 Publications

    Gene expression databases

    GenevestigatoriQ9FNX8.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FNX8.
    SMRiQ9FNX8. Positions 113-926.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini106 – 228123PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini231 – 926696LipoxygenasePROSITE-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.
    InParanoidiQ9FNX8.
    KOiK00454.
    OMAiALANEIM.
    PhylomeDBiQ9FNX8.

    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.

    Q9FNX8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALANEIMGS RLIFERSSSL ASPFHSRFSI KKKTQRTQFS INPFDPRPMR    50
    AVNSSGVVAA ISEDLVKTLR ISTVGRKQEK EEEEEKSVKF KVRAVATVRN 100
    KNKEDFKETL VKHLDAFTDK IGRNVVLELM STQVDPKTNE PKKSKAAVLK 150
    DWSKKSNSKA ERVHYTAEFT VDSAFGSPGA ITVTNKHQKE FFLESITIEG 200
    FACGPVHFPC NSWVQSQKDH PSKRILFTNQ PYLPSETPSG LRTLREKELE 250
    NLRGNGKGER KLSDRIYDYD VYNDIGNPDI SRELARPTLG GREFPYPRRC 300
    RTGRSSTDTD MMSERRVEKP LPMYVPRDEQ FEESKQNTFA ACRLKAVLHN 350
    LIPSLKASIL AEDFANFGEI DSLYKEGLLL KLGFQDDMFK KFPLPKIVTT 400
    LQKSSEGLLR YDTPKIVSKD KYAWLRDDEF ARQAIAGINP VNIERVTSYP 450
    PVSNLDPEIY GPGLHSALTE DHIIGQLDGL TVQQALETNR LFMVDYHDIY 500
    LPFLDRINAL DGRKAYATRT ILFLTRLGTL KPIAIELSLP SQSSSNQKSK 550
    RVVTPPVDAT SNWMWQLAKA HVGSNDAGVH QLVNHWLRTH ACLEPFILAA 600
    HRQLSAMHPI FKLLDPHMRY TLEINAVARQ TLISADGVIE SCFTAGQYGL 650
    EISSAAYKNK WRFDMEGLPA DLIRRGMAVP DPTQPHGLKL LVEDYPYAND 700
    GLLLWSAIQT WVRTYVERYY ANSNLIQTDT ELQAWYSESI NVGHADHRDA 750
    EWWPKLSTVE DLVSVITTII WLASAQHAAL NFGQYPYGGY VPNRPPLMRR 800
    LIPDESDPEF TSFIEDPQKY FFSSMPSLLQ TTKFMAVVDT LSTHSPDEEY 850
    IGERQQPSIW TGDAEIVDAF YGFSAEIGRI EKEIDKRNRD PSRRNRCGAG 900
    VLPYELMAPS SEPGVTCRGV PNSVSI 926
    Length:926
    Mass (Da):104,814
    Last modified:March 1, 2001 - v1
    Checksum:i3592FB6ECDCCC4A4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ302042 mRNA. Translation: CAC19364.1.
    AC010926 Genomic DNA. Translation: AAG51846.1.
    AC016529 Genomic DNA. Translation: AAG52571.1.
    CP002684 Genomic DNA. Translation: AEE35334.1.
    AY056166 mRNA. Translation: AAL07015.1.
    AY091193 mRNA. Translation: AAM14132.1.
    PIRiE96749.
    RefSeqiNP_177396.1. NM_105911.4.
    UniGeneiAt.18241.
    At.67292.

    Genome annotation databases

    EnsemblPlantsiAT1G72520.1; AT1G72520.1; AT1G72520.
    GeneIDi843584.
    KEGGiath:AT1G72520.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ302042 mRNA. Translation: CAC19364.1 .
    AC010926 Genomic DNA. Translation: AAG51846.1 .
    AC016529 Genomic DNA. Translation: AAG52571.1 .
    CP002684 Genomic DNA. Translation: AEE35334.1 .
    AY056166 mRNA. Translation: AAL07015.1 .
    AY091193 mRNA. Translation: AAM14132.1 .
    PIRi E96749.
    RefSeqi NP_177396.1. NM_105911.4.
    UniGenei At.18241.
    At.67292.

    3D structure databases

    ProteinModelPortali Q9FNX8.
    SMRi Q9FNX8. Positions 113-926.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q9FNX8.
    PRIDEi Q9FNX8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G72520.1 ; AT1G72520.1 ; AT1G72520 .
    GeneIDi 843584.
    KEGGi ath:AT1G72520.

    Organism-specific databases

    TAIRi AT1G72520.

    Phylogenomic databases

    eggNOGi NOG69653.
    HOGENOMi HOG000230469.
    InParanoidi Q9FNX8.
    KOi K00454.
    OMAi ALANEIM.
    PhylomeDBi Q9FNX8.

    Enzyme and pathway databases

    UniPathwayi UPA00382 .

    Gene expression databases

    Genevestigatori Q9FNX8.

    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. "AtLOX4, the third chloroplastic jasmonate-inducible 13-LOX from Arabidopsis leaves."
      Kunze S., Fritsche K., Feussner I.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.
    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. "Expression profiling of the host response to bacterial infection: the transition from basal to induced defence responses in RPM1-mediated resistance."
      de Torres M., Sanchez P., Fernandez-Delmond I., Grant M.
      Plant J. 33:665-676(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY BACTERIAL PATHOGENS AND WOUNDING.
    7. "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.
    8. "Nitric oxide modulates ozone-induced cell death, hormone biosynthesis and gene expression in Arabidopsis thaliana."
      Ahlfors R., Brosche M., Kollist H., Kangasjaervi J.
      Plant J. 58:1-12(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY OZONE.
    9. "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 nameiLOX4_ARATH
    AccessioniPrimary (citable) accession number: Q9FNX8
    Secondary accession number(s): Q9CAG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 105 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