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Q9LNR3 (LOX3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 105. 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 3, chloroplastic

Short name=AtLOX3
EC=1.13.11.12
Gene names
Name:LOX3
Ordered Locus Names:At1g17420
ORF Names:F28G4.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length919 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.10

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 roots and leaves. Ref.6

Developmental stage

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. Ref.5 Ref.6

Induction

Induced by methyl jasmonate (MeJA), bacterial pathogens (e.g. Pseudomonas syringae pv. tomato), high light and wounding. Ref.7 Ref.8 Ref.9

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Sequence caution

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

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Oxylipin biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanther dehiscence

Inferred from genetic interaction PubMed 21052784. Source: TAIR

anther development

Inferred from genetic interaction PubMed 21052784. Source: TAIR

lipid oxidation

Inferred from direct assay PubMed 21372125. Source: TAIR

oxylipin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

pollen development

Inferred from genetic interaction PubMed 21052784. Source: TAIR

response to fungus

Inferred from expression pattern PubMed 19220788. Source: TAIR

response to high light intensity

Inferred from expression pattern Ref.7. Source: UniProtKB

response to jasmonic acid

Inferred from expression pattern Ref.9. Source: UniProtKB

response to wounding

Inferred from expression pattern Ref.8. Source: UniProtKB

stamen filament development

Inferred from genetic interaction PubMed 21052784. Source: TAIR

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

linoleate 13S-lipoxygenase activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Chloroplast Potential
Chain53 – 919867Lipoxygenase 3, chloroplastic
PRO_0000380592

Regions

Domain86 – 222137PLAT
Domain225 – 919695Lipoxygenase

Sites

Metal binding5781Iron; catalytic By similarity
Metal binding5831Iron; catalytic By similarity
Metal binding7701Iron; catalytic By similarity
Metal binding7741Iron; catalytic By similarity
Metal binding9191Iron; via carboxylate; catalytic By similarity

Experimental info

Sequence conflict3741L → P in CAB56692. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9LNR3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 194A0B150273E44C

FASTA919103,726
        10         20         30         40         50         60 
MALAKELMGY PLITERSSLV SSASHFKKRT QSTQFSINPF DRRPRKTKSG VVAAISEDLV 

        70         80         90        100        110        120 
KTLRFSTTTG DRKSEEEEKA AVKFKVRAVV TVRNKNKEDL KETLVKHLDA FADKIGRNIV 

       130        140        150        160        170        180 
LELISTQLDP KTKLPKKSNA AVLKDWSKKS KTKAERVHYT AEFTVDAAFG SPGAITVMNK 

       190        200        210        220        230        240 
HQKEFFLESI TIEGFALGPV HFPCNSWVQS QKDHPDKRIF FTNQPYLPNE TPSGLRVLRE 

       250        260        270        280        290        300 
KELKNLRGDG SGVRKLSDRI YDFDVYNDLG NPDKSSELSR PKLGGKEVPY PRRCRTGRQS 

       310        320        330        340        350        360 
TVSDKDAESR VEKPLPMYVP RDEQFEESKQ DTFAAGRLKA VLHHLIPSLK ASIVAEDFAD 

       370        380        390        400        410        420 
FGEIDRLYKE GLLLKLGFQD DIFKKFPLPK VVVDTLQEST KGLLKYDTPK ILSKDKNAWL 

       430        440        450        460        470        480 
RDDEFARQAI AGINPVNIER VKTFPPVSNL DPKIYGPQHS ALTDDHIIGH LDGFSVQQAL 

       490        500        510        520        530        540 
EENRLYMLDY HDIFLPFLDR INALDGRKAY ATRTIFFLTR LGTLKPVAIE LSLPPHGPKH 

       550        560        570        580        590        600 
RSKRVLTPPV DATSNWMWQL AKAHVSSNDA GVHQLVNHWL RTHACLEPFI LAAHRQLSAM 

       610        620        630        640        650        660 
HPIFKLLDPH MRYTLEINAL ARQSLISADG VIEGGFTAGA YGMEMSAAAY KSSWRFDMEG 

       670        680        690        700        710        720 
LPADLIRRGM AIPDATQPHG LKLLIEDYPY ANDGLLLWSA IQTWVRTYVE RYYPNPNLIK 

       730        740        750        760        770        780 
TDSELQSWYS ESINVGHADL RDADWWPELS TVDDLVSILT TLIWLASAQH AALNFGQYPY 

       790        800        810        820        830        840 
GGYVPNRPPL MRRLIPDESD PEYASFISHP EKYYFSSMPS LAQTSKFMAV VDTLSTHSPD 

       850        860        870        880        890        900 
EEYIGERQQP SIWTGDAEIV EAFYGFAAEI GRIEKEIEKR NADPDRRNRC GAGVLPYELL 

       910 
VPSSEPGVTC RGVPNSVSI 

« Hide

References

« Hide 'large scale' references
[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. 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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_564021.1. NM_101603.2.
UniGeneAt.20467.
At.64244.
At.67022.

3D structure databases

ProteinModelPortalQ9LNR3.
SMRQ9LNR3. Positions 108-919.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid23554. 1 interaction.
IntActQ9LNR3. 1 interaction.

Proteomic databases

PaxDbQ9LNR3.
PRIDEQ9LNR3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G17420.1; AT1G17420.1; AT1G17420.
GeneID838314.
KEGGath:AT1G17420.

Organism-specific databases

TAIRAT1G17420.

Phylogenomic databases

eggNOGNOG69653.
HOGENOMHOG000230469.
InParanoidQ9LNR3.
KOK00454.
OMALSKDKFA.
PhylomeDBQ9LNR3.

Enzyme and pathway databases

UniPathwayUPA00382.

Gene expression databases

GenevestigatorQ9LNR3.

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 nameLOX3_ARATH
AccessionPrimary (citable) accession number: Q9LNR3
Secondary accession number(s): Q9LQJ5, Q9SMW1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 105 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