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

Linoleate 9S-lipoxygenase 1

Gene

LOX1

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

Functioni

9S-lipoxygenase that can use linoleic acid or 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. Function as regulators of root development by controlling the emergence of lateral roots.2 Publications

Catalytic activityi

Linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate.2 Publications

Cofactori

Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit. Iron is tightly bound.PROSITE-ProRule annotation

Pathwayi: 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 bindingi519 – 5191Iron; catalyticPROSITE-ProRule annotation
Metal bindingi524 – 5241Iron; catalyticPROSITE-ProRule annotation
Metal bindingi711 – 7111Iron; catalyticPROSITE-ProRule annotation
Metal bindingi715 – 7151Iron; catalyticPROSITE-ProRule annotation
Metal bindingi859 – 8591Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  • linoleate 9S-lipoxygenase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • lateral root formation Source: UniProtKB
  • lipid oxidation Source: TAIR
  • oxylipin biosynthetic process Source: UniProtKB-UniPathway
  • response to abscisic acid Source: UniProtKB
  • response to jasmonic acid Source: UniProtKB
  • root 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

BRENDAi1.13.11.58. 399.
ReactomeiR-ATH-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-ATH-2142696. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
R-ATH-2142700. Synthesis of Lipoxins (LX).
R-ATH-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.
R-ATH-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathwayiUPA00382.

Names & Taxonomyi

Protein namesi
Recommended name:
Linoleate 9S-lipoxygenase 1 (EC:1.13.11.58)
Alternative name(s):
Lipoxygenase 1
Short name:
AtLOX1
Gene namesi
Name:LOX1
Ordered Locus Names:At1g55020
ORF Names:F14C21.3, F14C21.54, T24C10.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G55020.

Subcellular locationi

GO - Cellular componenti

  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Increment in the number of lateral roots, and moderate increase in the length of the primary root.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859Linoleate 9S-lipoxygenase 1PRO_0000220703Add
BLAST

Proteomic databases

PaxDbiQ06327.
PRIDEiQ06327.

Expressioni

Tissue specificityi

Seedlings, roots, leaves, and flowers (at protein level).4 Publications

Developmental stagei

Transiently expressed during germination, within 1 day after imbibition, especially in the epidermis and the aleurone layer. Later present in the epidermis of the radicle and the adaxial side of the cotyledons. In roots, confined to the pericycle cells and in the lateral root primordia (LRP), and declined at the time of lateral root emergence. Expression is greatly increased in leaves during leaf senescence.3 Publications

Inductioni

By pathogens (e.g. Pseudomonas syringae), wounding, abscisic acid (ABA) and methyl jasmonate (MeJA). Higher levels in light than in dark conditions.2 Publications

Gene expression databases

GenevisibleiQ06327. AT.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi27169. 1 interaction.
MINTiMINT-8068008.
STRINGi3702.AT1G55020.1.

Structurei

3D structure databases

ProteinModelPortaliQ06327.
SMRiQ06327. Positions 20-859.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 161141PLATPROSITE-ProRule annotationAdd
BLAST
Domaini164 – 859696LipoxygenasePROSITE-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

Phylogenomic databases

eggNOGiENOG410IH0D. Eukaryota.
ENOG410YN4N. LUCA.
HOGENOMiHOG000230469.
InParanoidiQ06327.
KOiK15718.
OMAiNGDKFGA.
PhylomeDBiQ06327.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR000907. 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. 2 hits.
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.

Q06327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGELRDLLT GGGNETTTKK VKGTVVLMKK NVLDFNDFNA SFLDRLHEFL
60 70 80 90 100
GNKITLRLVS SDVTDSENGS KGKLGKAAHL EDWITTITSL TAGESAFKVT
110 120 130 140 150
FDYETDFGYP GAFLIRNSHF SEFLLKSLTL EDVPGHGRVH YICNSWIYPA
160 170 180 190 200
KHYTTDRVFF SNKTYLPHET PATLLKYREE ELVSLRGTGE GELKEWDRVY
210 220 230 240 250
DYAYYNDLGV PPKNPRPVLG GTQEYPYPRR GRTGRKPTKE DPQTESRLPI
260 270 280 290 300
TSSLDIYVPR DERFGHLKMS DFLAYALKAI AQFIQPALEA VFDDTPKEFD
310 320 330 340 350
SFEDVLKIYE EGIDLPNQAL IDSIVKNIPL EMLKEIFRTD GQKFLKFPVP
360 370 380 390 400
QVIKEDKTAW RTDEEFAREM LAGLNPVVIQ LLKEFPPKSK LDSESYGNQN
410 420 430 440 450
STITKSHIEH NLDGLTVEEA LEKERLFILD HHDTLMPYLG RVNTTTTKTY
460 470 480 490 500
ASRTLLFLKD DGTLKPLVIE LSLPHPNGDK FGAVSEVYTP GEGVYDSLWQ
510 520 530 540 550
LAKAFVGVND SGNHQLISHW MQTHASIEPF VIATNRQLSV LHPVFKLLEP
560 570 580 590 600
HFRDTMNINA LARQILINGG GIFEITVFPS KYAMEMSSFI YKNHWTFPDQ
610 620 630 640 650
ALPAELKKRG MAVEDPEAPH GLRLRIKDYP YAVDGLEVWY AIESWVRDYI
660 670 680 690 700
FLFYKIEEDI QTDTELQAWW KEVREEGHGD KKSEPWWPKM QTREELVESC
710 720 730 740 750
TIIIWVASAL HAAVNFGQYP VAGYLPNRPT ISRQYMPKEN TPEFEELEKN
760 770 780 790 800
PDKVFLKTIT AQLQTLLGIS LIEILSTHSS DEVYLGQRDS KEWAAEKEAL
810 820 830 840 850
EAFEKFGEKV KEIEKNIDER NDDETLKNRT GLVKMPYTLL FPSSEGGVTG

RGIPNSVSI
Length:859
Mass (Da):98,045
Last modified:June 1, 1994 - v1
Checksum:i49378EBACD5FF579
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04637 mRNA. Translation: AAA32827.1.
U01843 Genomic DNA. Translation: AAA17036.1.
AC064840 Genomic DNA. Translation: AAG00881.1.
AC069144 Genomic DNA. Translation: AAG51123.1.
CP002684 Genomic DNA. Translation: AEE33175.1.
AY093104 mRNA. Translation: AAM13103.1.
BT010358 mRNA. Translation: AAQ56801.1.
PIRiJQ2267.
RefSeqiNP_175900.1. NM_104376.2.
UniGeneiAt.19984.
At.67309.

Genome annotation databases

EnsemblPlantsiAT1G55020.1; AT1G55020.1; AT1G55020.
GeneIDi841944.
GrameneiAT1G55020.1; AT1G55020.1; AT1G55020.
KEGGiath:AT1G55020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04637 mRNA. Translation: AAA32827.1.
U01843 Genomic DNA. Translation: AAA17036.1.
AC064840 Genomic DNA. Translation: AAG00881.1.
AC069144 Genomic DNA. Translation: AAG51123.1.
CP002684 Genomic DNA. Translation: AEE33175.1.
AY093104 mRNA. Translation: AAM13103.1.
BT010358 mRNA. Translation: AAQ56801.1.
PIRiJQ2267.
RefSeqiNP_175900.1. NM_104376.2.
UniGeneiAt.19984.
At.67309.

3D structure databases

ProteinModelPortaliQ06327.
SMRiQ06327. Positions 20-859.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27169. 1 interaction.
MINTiMINT-8068008.
STRINGi3702.AT1G55020.1.

Proteomic databases

PaxDbiQ06327.
PRIDEiQ06327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G55020.1; AT1G55020.1; AT1G55020.
GeneIDi841944.
GrameneiAT1G55020.1; AT1G55020.1; AT1G55020.
KEGGiath:AT1G55020.

Organism-specific databases

TAIRiAT1G55020.

Phylogenomic databases

eggNOGiENOG410IH0D. Eukaryota.
ENOG410YN4N. LUCA.
HOGENOMiHOG000230469.
InParanoidiQ06327.
KOiK15718.
OMAiNGDKFGA.
PhylomeDBiQ06327.

Enzyme and pathway databases

UniPathwayiUPA00382.
BRENDAi1.13.11.58. 399.
ReactomeiR-ATH-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-ATH-2142696. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
R-ATH-2142700. Synthesis of Lipoxins (LX).
R-ATH-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.
R-ATH-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.

Miscellaneous databases

PROiQ06327.

Gene expression databases

GenevisibleiQ06327. AT.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR000907. 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. 2 hits.
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. "An Arabidopsis thaliana lipoxygenase gene can be induced by pathogens, abscisic acid, and methyl jasmonate."
    Melan M.A., Dong X., Endara M.E., Davis K.R., Ausubel F.M., Peterman T.K.
    Plant Physiol. 101:441-450(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY ABA; JA AND PATHOGEN, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
    Tissue: Root.
  2. "Structure and sequence of the Arabidopsis thaliana lipoxygenase 1 gene."
    Melan M.A., Nemhauser J.M., Peterman T.K.
    Biochim. Biophys. Acta 1210:377-380(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "The LOX1 gene of Arabidopsis is temporally and spatially regulated in germinating seedlings."
    Melan M.A., Enriquez A.L.D., Peterman T.K.
    Plant Physiol. 105:385-393(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY LIGHT, DEVELOPMENTAL STAGE.
  7. "Immunological characterization of Arabidopsis thaliana lipoxygenase: Expression of the LOX1 gene product in Escherichia coli and polyclonal antibody production."
    Peterman T.K., Rattigan E.M., Enriquez A., Melan M.A.
    Plant Physiol. Biochem. 32:443-450(1994)
    Cited for: TISSUE SPECIFICITY.
  8. "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.
  9. "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: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  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, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiLOX1_ARATH
AccessioniPrimary (citable) accession number: Q06327
Secondary accession number(s): Q9FZ30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 17, 2016
This is version 137 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

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 one 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.