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P38418 (LOX2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoxygenase 2, chloroplastic

Short name=AtLOX2
EC=1.13.11.12
Gene names
Name:LOX2
Ordered Locus Names:At3g45140
ORF Names:T14D3.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length896 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Required for the wound-induced synthesis of jasmonic acid (JA) in leaves. Ref.7 Ref.26

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. Iron is tightly bound By similarity.

Pathway

Lipid metabolism; oxylipin biosynthesis.

Subunit structure

Interacts with EIF4E2. Ref.9

Subcellular location

Plastidchloroplast. Cytoplasm. Note: The unprocessed form is cytoplasmic whereas the cleaved form is chloroplastic. Ref.7 Ref.9 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.25

Tissue specificity

In leaves and inflorescences but not abundant in seeds, roots and stems. Ref.22

Developmental stage

Expression is sharply reduced in leaves during leaf senescence. Ref.12

Induction

By methyl jasmonate (MeJA) and wounding, probably through nitric oxide-mediated (NO) induction. Slightly locally induced upon herbivors infestation such as aphids (Myzus persicae and Brevicoryne brassicae), or caterpillar (Spodoptera exigua). Induced by leaf-volatiles generated by herbivors-mediated wounding such as (E)-2-hexenal, (Z)-3-hexenal, (Z)-3-hexenol or allo-ocimene (2,6-dimethyl-2,4,6-octatriene). Increased levels by bacterial pathogens (e.g. P.viridiflava and P.syringae pv. tomato). Repressed by WRKY62. Ref.8 Ref.10 Ref.11 Ref.16 Ref.18 Ref.20 Ref.21 Ref.24

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Sequence caution

The sequence CAB72152.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from mutant phenotype Ref.7. Source: TAIR

lipid oxidation

Inferred from direct assay PubMed 21372125. Source: TAIR

oxylipin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to bacterium

Inferred from expression pattern Ref.21. Source: UniProtKB

response to fungus

Inferred from expression pattern PubMed 19220788. Source: TAIR

response to herbivore

Inferred from expression pattern Ref.10Ref.24. Source: UniProtKB

response to jasmonic acid

Inferred from expression pattern PubMed 15860010. Source: TAIR

response to wounding

Inferred from expression pattern Ref.10. Source: UniProtKB

   Cellular_componentchloroplast

Inferred from direct assay Ref.9. Source: UniProtKB

chloroplast envelope

Inferred from direct assay Ref.13. Source: TAIR

chloroplast stroma

Inferred from direct assay Ref.19PubMed 18633119PubMed 20061580. Source: TAIR

chloroplast thylakoid membrane

Inferred from direct assay Ref.17Ref.15. Source: TAIR

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

linoleate 13S-lipoxygenase activity

Inferred from direct assay Ref.26. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF(ISO)4EO046637EBI-1770437,EBI-1770425

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Chloroplast Potential
Chain57 – 896840Lipoxygenase 2, chloroplastic
PRO_0000018326

Regions

Domain79 – 199121PLAT
Domain202 – 896695Lipoxygenase
Region175 – 23258EIF4E2 binding

Sites

Metal binding5541Iron; catalytic By similarity
Metal binding5591Iron; catalytic By similarity
Metal binding7461Iron; catalytic By similarity
Metal binding7501Iron; catalytic By similarity
Metal binding8961Iron; via carboxylate; catalytic By similarity

Experimental info

Sequence conflict119 – 1257ITVEDYA → EYTFFFL in BAC43666. Ref.5
Sequence conflict6131W → C in AAL32689. Ref.4
Sequence conflict6461L → V in BAF01939. Ref.6
Sequence conflict7311L → F in BAF01939. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P38418 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F32822205C8F9F22

FASTA896102,046
        10         20         30         40         50         60 
MYCRESLSSL QTLNVAKSLS SLFPKQSALI NPISAGRRNN LPRPNLRRRC KVTASRANIE 

        70         80         90        100        110        120 
QEGNTVKEPI QNIKVKGYIT AQEEFLEGIT WSRGLDDIAD IRGRSLLVEL ISAKTDQRIT 

       130        140        150        160        170        180 
VEDYAQRVWA EAPDEKYECE FEMPEDFGPV GAIKIQNQYH RQLFLKGVEL KLPGGSITFT 

       190        200        210        220        230        240 
CESWVAPKSV DPTKRIFFSD KSYLPSQTPE PLKKYRKEEL ETLQGKNREE VGEFTKFERI 

       250        260        270        280        290        300 
YDYDVYNDVG DPDNDPELAR PVIGGLTHPY PRRCKTGRKP CETDPSSEQR YGGEFYVPRD 

       310        320        330        340        350        360 
EEFSTAKGTS FTGKAVLAAL PSIFPQIESV LLSPQEPFPH FKAIQNLFEE GIQLPKDAGL 

       370        380        390        400        410        420 
LPLLPRIIKA LGEAQDDILQ FDAPVLINRD RFSWLRDDEF ARQTLAGLNP YSIQLVEEWP 

       430        440        450        460        470        480 
LISKLDPAVY GDPTSLITWE IVEREVKGNM TVDEALKNKR LFVLDYHDLL LPYVNKVREL 

       490        500        510        520        530        540 
NNTTLYASRT LFFLSDDSTL RPVAIELTCP PNINKPQWKQ VFTPGYDATS CWLWNLAKTH 

       550        560        570        580        590        600 
AISHDAGYHQ LISHWLRTHA CTEPYIIAAN RQLSAMHPIY RLLHPHFRYT MEINARARQS 

       610        620        630        640        650        660 
LVNGGGIIET CFWPGKYALE LSSAVYGKLW RFDQEGLPAD LIKRGLAEED KTAEHGVRLT 

       670        680        690        700        710        720 
IPDYPFANDG LILWDAIKEW VTDYVKHYYP DEELITSDEE LQGWWSEVRN IGHGDKKDEP 

       730        740        750        760        770        780 
WWPVLKTQDD LIGVVTTIAW VTSGHHAAVN FGQYGYGGYF PNRPTTTRIR MPTEDPTDEA 

       790        800        810        820        830        840 
LKEFYESPEK VLLKTYPSQK QATLVMVTLD LLSTHSPDEE YIGEQQEASW ANEPVINAAF 

       850        860        870        880        890 
ERFKGKLQYL EGVIDERNVN ITLKNRAGAG VVKYELLKPT SEHGVTGMGV PYSISI 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of an Arabidopsis lipoxygenase gene responsive to methyl jasmonate and wounding."
Bell E., Mullet J.E.
Plant Physiol. 103:1133-1137(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(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]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-125.
Strain: cv. Columbia.
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-896.
Strain: cv. Columbia.
[7]"A chloroplast lipoxygenase is required for wound-induced jasmonic acid accumulation in Arabidopsis."
Bell E., Creelman R.A., Mullet J.E.
Proc. Natl. Acad. Sci. U.S.A. 92:8675-8679(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Involvement of phospholipase D in wound-induced accumulation of jasmonic acid in arabidopsis."
Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X.
Plant Cell 12:2237-2246(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY WOUNDING.
[9]"Plant lipoxygenase 2 is a translation initiation factor-4E-binding protein."
Freire M.A., Tourneur C., Granier F., Camonis J., El Amrani A., Browning K.S., Robaglia C.
Plant Mol. Biol. 44:129-140(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4E2, SUBCELLULAR LOCATION.
[10]"Molecular responses to aphid feeding in Arabidopsis in relation to plant defense pathways."
Moran P.J., Thompson G.A.
Plant Physiol. 125:1074-1085(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY APHIDS AND WOUNDING.
[11]"Fusion genetic analysis of jasmonate-signalling mutants in Arabidopsis."
Jensen A.B., Raventos D., Mundy J.
Plant J. 29:595-606(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY JASMONATE.
[12]"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.
[13]"Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis."
Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S.
J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy."
Peltier J.-B., Ytterberg A.J., Sun Q., van Wijk K.J.
J. Biol. Chem. 279:49367-49383(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"Nitric oxide is induced by wounding and influences jasmonic acid signaling in Arabidopsis thaliana."
Huang X., Stettmaier K., Michel C., Hutzler P., Mueller M.J., Durner J.
Planta 218:938-946(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY NITRIC OXIDE.
[17]"In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database."
Friso G., Giacomelli L., Ytterberg A.J., Peltier J.-B., Rudella A., Sun Q., van Wijk K.J.
Plant Cell 16:478-499(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[18]"Volatile C6-aldehydes and allo-ocimene activate defense genes and induce resistance against Botrytis cinerea in Arabidopsis thaliana."
Kishimoto K., Matsui K., Ozawa R., Takabayashi J.
Plant Cell Physiol. 46:1093-1102(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY LEAF VOLATILES.
[19]"The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts."
Peltier J.-B., Cai Y., Sun Q., Zabrouskov V., Giacomelli L., Rudella A., Ytterberg A.J., Rutschow H., van Wijk K.J.
Mol. Cell. Proteomics 5:114-133(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[20]"Transcriptional responses of Arabidopsis thaliana ecotypes with different glucosinolate profiles after attack by polyphagous Myzus persicae and oligophagous Brevicoryne brassicae."
Kusnierczyk A., Winge P., Midelfart H., Armbruster W.S., Rossiter J.T., Bones A.M.
J. Exp. Bot. 58:2537-2552(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY MYZUS PERSICAE AND BREVICORYNE BRASSICAE.
[21]"The role of pectate lyase and the jasmonic acid defense response in Pseudomonas viridiflava virulence."
Jakob K., Kniskern J.M., Bergelson J.
Mol. Plant Microbe Interact. 20:146-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY BACTERIAL PATHOGENS.
[22]"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.
[23]"WRKY62 transcription factor acts downstream of cytosolic NPR1 and negatively regulates jasmonate-responsive gene expression."
Mao P., Duan M., Wei C., Li Y.
Plant Cell Physiol. 48:833-842(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REPRESSION BY WRKY62.
[24]"Caterpillar saliva interferes with induced Arabidopsis thaliana defence responses via the systemic acquired resistance pathway."
Weech M.-H., Chapleau M., Pan L., Ide C., Bede J.C.
J. Exp. Bot. 59:2437-2448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY CATERPILLAR.
[25]"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[26]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L23968 mRNA. Translation: AAA32749.1.
AL138649 Genomic DNA. Translation: CAB72152.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE77997.1.
AY062611 mRNA. Translation: AAL32689.1.
AK119093 mRNA. Translation: BAC43666.1.
AK222075 mRNA. Translation: BAD94917.1.
AK230124 mRNA. Translation: BAF01939.1.
PIRJQ2391.
T47454.
RefSeqNP_566875.1. NM_114383.2.
UniGeneAt.22079.
At.75027.

3D structure databases

ProteinModelPortalP38418.
SMRP38418. Positions 132-896.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid8970. 2 interactions.
IntActP38418. 4 interactions.

2D gel databases

SWISS-2DPAGEP38418.

Proteomic databases

PaxDbP38418.
PRIDEP38418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G45140.1; AT3G45140.1; AT3G45140.
GeneID823650.
KEGGath:AT3G45140.

Organism-specific databases

TAIRAT3G45140.

Phylogenomic databases

eggNOGNOG69653.
HOGENOMHOG000230469.
InParanoidP38418.
KOK00454.
OMATEMFLED.
PhylomeDBP38418.
ProtClustDBCLSN2917374.

Enzyme and pathway databases

BioCycMetaCyc:AT3G45140-MONOMER.
UniPathwayUPA00382.

Gene expression databases

GenevestigatorP38418.

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 nameLOX2_ARATH
AccessionPrimary (citable) accession number: P38418
Secondary accession number(s): Q0WLR8 expand/collapse secondary AC list , Q56WG6, Q8GW45, Q8W4E4, Q9M1U5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 128 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