Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoxygenase 4, chloroplastic

Gene

LOX4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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.PROSITE-ProRule annotation1 Publication

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

Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation

Pathway: oxylipin biosynthesis

This protein is involved in the pathway oxylipin biosynthesis, which is part of Lipid metabolism.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway oxylipin biosynthesis and in Lipid metabolism.

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

  • linoleate 13S-lipoxygenase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • anther dehiscence Source: TAIR
  • anther development Source: TAIR
  • lipid oxidation Source: TAIR
  • oxylipin biosynthetic process Source: UniProtKB-UniPathway
  • pollen development Source: TAIR
  • response to bacterium Source: UniProtKB
  • response to ozone Source: UniProtKB
  • response to wounding Source: UniProtKB
  • stamen filament development Source: TAIR
Complete GO annotation...

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

BRENDAi1.13.11.12. 399.
ReactomeiREACT_286810. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
REACT_290235. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_302288. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_319433. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_340430. Synthesis of Lipoxins (LX).
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 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G72520.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G72520.1.

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_plant.
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

        10         20         30         40         50
MALANEIMGS RLIFERSSSL ASPFHSRFSI KKKTQRTQFS INPFDPRPMR
60 70 80 90 100
AVNSSGVVAA ISEDLVKTLR ISTVGRKQEK EEEEEKSVKF KVRAVATVRN
110 120 130 140 150
KNKEDFKETL VKHLDAFTDK IGRNVVLELM STQVDPKTNE PKKSKAAVLK
160 170 180 190 200
DWSKKSNSKA ERVHYTAEFT VDSAFGSPGA ITVTNKHQKE FFLESITIEG
210 220 230 240 250
FACGPVHFPC NSWVQSQKDH PSKRILFTNQ PYLPSETPSG LRTLREKELE
260 270 280 290 300
NLRGNGKGER KLSDRIYDYD VYNDIGNPDI SRELARPTLG GREFPYPRRC
310 320 330 340 350
RTGRSSTDTD MMSERRVEKP LPMYVPRDEQ FEESKQNTFA ACRLKAVLHN
360 370 380 390 400
LIPSLKASIL AEDFANFGEI DSLYKEGLLL KLGFQDDMFK KFPLPKIVTT
410 420 430 440 450
LQKSSEGLLR YDTPKIVSKD KYAWLRDDEF ARQAIAGINP VNIERVTSYP
460 470 480 490 500
PVSNLDPEIY GPGLHSALTE DHIIGQLDGL TVQQALETNR LFMVDYHDIY
510 520 530 540 550
LPFLDRINAL DGRKAYATRT ILFLTRLGTL KPIAIELSLP SQSSSNQKSK
560 570 580 590 600
RVVTPPVDAT SNWMWQLAKA HVGSNDAGVH QLVNHWLRTH ACLEPFILAA
610 620 630 640 650
HRQLSAMHPI FKLLDPHMRY TLEINAVARQ TLISADGVIE SCFTAGQYGL
660 670 680 690 700
EISSAAYKNK WRFDMEGLPA DLIRRGMAVP DPTQPHGLKL LVEDYPYAND
710 720 730 740 750
GLLLWSAIQT WVRTYVERYY ANSNLIQTDT ELQAWYSESI NVGHADHRDA
760 770 780 790 800
EWWPKLSTVE DLVSVITTII WLASAQHAAL NFGQYPYGGY VPNRPPLMRR
810 820 830 840 850
LIPDESDPEF TSFIEDPQKY FFSSMPSLLQ TTKFMAVVDT LSTHSPDEEY
860 870 880 890 900
IGERQQPSIW TGDAEIVDAF YGFSAEIGRI EKEIDKRNRD PSRRNRCGAG
910 920
VLPYELMAPS SEPGVTCRGV PNSVSI
Length:926
Mass (Da):104,814
Last modified:March 1, 2001 - v1
Checksum:i3592FB6ECDCCC4A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi3702.AT1G72520.1.

Proteomic databases

PaxDbiQ9FNX8.
PRIDEiQ9FNX8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT1G72520.

Phylogenomic databases

eggNOGiNOG69653.
HOGENOMiHOG000230469.
InParanoidiQ9FNX8.
KOiK00454.
OMAiALANEIM.
PhylomeDBiQ9FNX8.

Enzyme and pathway databases

UniPathwayiUPA00382.
BRENDAi1.13.11.12. 399.
ReactomeiREACT_286810. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
REACT_290235. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_302288. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_319433. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_340430. Synthesis of Lipoxins (LX).

Miscellaneous databases

PROiQ9FNX8.

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_plant.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 112 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.