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Q9FNX8 (LOX4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoxygenase 4, chloroplastic

Short name=AtLOX4
EC=1.13.11.12
Alternative name(s):
LOX3-like protein
Gene names
Name:LOX4
Synonyms:LOX3
Ordered Locus Names:At1g72520
ORF Names:F28P22.29, T10D10.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length926 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.9

Catalytic activity

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

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Pathway

Lipid metabolism; oxylipin biosynthesis.

Subcellular location

Plastidchloroplast Potential.

Tissue specificity

Expressed in leaves. Ref.7

Developmental stage

Expression is greatly increased in leaves during leaf senescence. Ref.5

Induction

Induced by bacterial pathogens (e.g. Pseudomonas syringae pv. tomato), ozone O3, and wounding. Ref.6 Ref.8

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5858Chloroplast Potential
Chain59 – 926868Lipoxygenase 4, chloroplastic
PRO_0000380593

Regions

Domain106 – 228123PLAT
Domain231 – 926696Lipoxygenase

Sites

Metal binding5851Iron; catalytic By similarity
Metal binding5901Iron; catalytic By similarity
Metal binding7771Iron; catalytic By similarity
Metal binding7811Iron; catalytic By similarity
Metal binding9261Iron; via carboxylate; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9FNX8 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 3592FB6ECDCCC4A4

FASTA926104,814
        10         20         30         40         50         60 
MALANEIMGS RLIFERSSSL ASPFHSRFSI KKKTQRTQFS INPFDPRPMR AVNSSGVVAA 

        70         80         90        100        110        120 
ISEDLVKTLR ISTVGRKQEK EEEEEKSVKF KVRAVATVRN KNKEDFKETL VKHLDAFTDK 

       130        140        150        160        170        180 
IGRNVVLELM STQVDPKTNE PKKSKAAVLK DWSKKSNSKA ERVHYTAEFT VDSAFGSPGA 

       190        200        210        220        230        240 
ITVTNKHQKE FFLESITIEG FACGPVHFPC NSWVQSQKDH PSKRILFTNQ PYLPSETPSG 

       250        260        270        280        290        300 
LRTLREKELE NLRGNGKGER KLSDRIYDYD VYNDIGNPDI SRELARPTLG GREFPYPRRC 

       310        320        330        340        350        360 
RTGRSSTDTD MMSERRVEKP LPMYVPRDEQ FEESKQNTFA ACRLKAVLHN LIPSLKASIL 

       370        380        390        400        410        420 
AEDFANFGEI DSLYKEGLLL KLGFQDDMFK KFPLPKIVTT LQKSSEGLLR YDTPKIVSKD 

       430        440        450        460        470        480 
KYAWLRDDEF ARQAIAGINP VNIERVTSYP PVSNLDPEIY GPGLHSALTE DHIIGQLDGL 

       490        500        510        520        530        540 
TVQQALETNR LFMVDYHDIY LPFLDRINAL DGRKAYATRT ILFLTRLGTL KPIAIELSLP 

       550        560        570        580        590        600 
SQSSSNQKSK RVVTPPVDAT SNWMWQLAKA HVGSNDAGVH QLVNHWLRTH ACLEPFILAA 

       610        620        630        640        650        660 
HRQLSAMHPI FKLLDPHMRY TLEINAVARQ TLISADGVIE SCFTAGQYGL EISSAAYKNK 

       670        680        690        700        710        720 
WRFDMEGLPA DLIRRGMAVP DPTQPHGLKL LVEDYPYAND GLLLWSAIQT WVRTYVERYY 

       730        740        750        760        770        780 
ANSNLIQTDT ELQAWYSESI NVGHADHRDA EWWPKLSTVE DLVSVITTII WLASAQHAAL 

       790        800        810        820        830        840 
NFGQYPYGGY VPNRPPLMRR LIPDESDPEF TSFIEDPQKY FFSSMPSLLQ TTKFMAVVDT 

       850        860        870        880        890        900 
LSTHSPDEEY IGERQQPSIW TGDAEIVDAF YGFSAEIGRI EKEIDKRNRD PSRRNRCGAG 

       910        920 
VLPYELMAPS SEPGVTCRGV PNSVSI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRE96749.
RefSeqNP_177396.1. NM_105911.4.
UniGeneAt.18241.
At.67292.

3D structure databases

ProteinModelPortalQ9FNX8.
SMRQ9FNX8. Positions 113-926.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9FNX8.
PRIDEQ9FNX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G72520.1; AT1G72520.1; AT1G72520.
GeneID843584.
KEGGath:AT1G72520.

Organism-specific databases

TAIRAT1G72520.

Phylogenomic databases

eggNOGNOG69653.
HOGENOMHOG000230469.
InParanoidQ9FNX8.
KOK00454.
OMAALANEIM.
PhylomeDBQ9FNX8.
ProtClustDBPLN02264.

Enzyme and pathway databases

UniPathwayUPA00382.

Gene expression databases

GenevestigatorQ9FNX8.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProIPR008976. 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]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLOX4_ARATH
AccessionPrimary (citable) accession number: Q9FNX8
Secondary accession number(s): Q9CAG9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names