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O24370 (LOX21_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Linoleate 13S-lipoxygenase 2-1, chloroplastic

EC=1.13.11.12
Alternative name(s):
Lipoxygenase 2-1
Gene names
Name:LOX2.1
Synonyms:LOX-H1
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length899 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plant lipoxygenase involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence. May not be involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids. Has also some activity with phosphatidylglycerol, but not with galactolipids. Ref.1 Ref.3

Catalytic activity

Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate. Ref.1 Ref.3

Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate. Ref.1 Ref.3

Cofactor

Binds 1 iron ion per subunit By similarity.

Pathway

Lipid metabolism; oxylipin biosynthesis.

Subunit structure

Monomer By similarity.

Subcellular location

Plastidchloroplast stroma. Plastidchloroplast thylakoid. Note: Associated with the non-appressed part of the thylakoid membrane. Ref.3 Ref.4

Tissue specificity

Expressed in leaves and floral buds. Ref.1

Induction

Up-regulated by jasmonate and abscisic acid treatment. Up-regulated localy and systemically at the transcript levels 6 hours after wounding, but the protein levels remain constant. Not induced by pathogen infection. Ref.1 Ref.2 Ref.4

Miscellaneous

99% depletion of LOX-H1 by co-suppression-mediated gene silencing has no effect on the basal or wound-induced levels of jasmonates but results in a marked reduction in the production of volatile aliphatic C6 aldehydes.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Chloroplast Potential
Chain41 – 899859Linoleate 13S-lipoxygenase 2-1, chloroplastic
PRO_0000412927

Regions

Domain78 – 200123PLAT
Domain203 – 899697Lipoxygenase

Sites

Metal binding5571Iron; catalytic By similarity
Metal binding5621Iron; catalytic By similarity
Metal binding7491Iron; catalytic By similarity
Metal binding7531Iron; catalytic By similarity
Metal binding8991Iron; via carboxylate; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
O24370 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 43E9D512C0E808FF

FASTA899101,937
        10         20         30         40         50         60 
MLKPQLQQSS QSTKALIPSW NTNPLFLASF PINILNKNFR LKKKNNFRVH HNYNGASTTK 

        70         80         90        100        110        120 
AVLSSTEKAT GVKAVVTVQK QVNLNLSRGL DDIGDLLGKS LLLWIVAAEL DHKTGIEKPG 

       130        140        150        160        170        180 
IRAYAHRGRD VDGDTHYEAD FVIPQDFGEV GAILIENEHH KEMYVKNIVI DGFVHGKVEI 

       190        200        210        220        230        240 
TCNSWVHSKF DNPDKRIFFT NKSYLPSQTP SGVSRLREEE LVTLRGDGIG ERKVFERIYD 

       250        260        270        280        290        300 
YDVYNDLGEA DSNNDDAKRP VLGGKELPYP RRCKTGRPRS KKDPLSETRS TFVYVPRDEA 

       310        320        330        340        350        360 
FSEVKSVAFS GNTVYSVLHA VVPALESVVT DPNLGFPHFP AIDSLFNVGV DLPGLGDKKS 

       370        380        390        400        410        420 
GLFNVVPRLI KAISDTRKDV LLFESPQLVQ RDKFSWFRDV EFARQTLAGL NPYSIRLVTE 

       430        440        450        460        470        480 
WPLRSKLDPK VYGPPESEIT KELIEKEIGN YMTVEQAVQQ KKLFILDYHD LLLPYVNKVN 

       490        500        510        520        530        540 
ELKGSMLYGS RTIFFLTPQG TLKPLAIELT RPPVDDKPQW KEVYSPNDWN ATGAWLWKLA 

       550        560        570        580        590        600 
KAHVLSHDSG YHQLVSHWLR THCCTEPYII ASNRQLSAMH PIYRLLHPHF RYTMEINALA 

       610        620        630        640        650        660 
REALINANGV IESSFFPGKY AIELSSIAYG AEWRFDQEAL PQNLISRGLA VEDPNEPHGL 

       670        680        690        700        710        720 
KLAIEDYPFA NDGLVLWDIL KQWVTNYVNH YYPQTNLIES DKELQAWWSE IKNVGHGDKR 

       730        740        750        760        770        780 
DEPWWPELKT PNDLIGIITT IVWVTSGHHA AVNFGQYSYA GYFPNRPTVA RSKMPTEDPT 

       790        800        810        820        830        840 
AEEWEWFMNK PEEALLRCFP SQIQATKVMA ILDVLSNHSP DEEYIGEKIE PYWAEDPVIN 

       850        860        870        880        890 
AAFEVFSGKL KELEGIIDAR NNDSKLSNRN GAGVMPYELL KPYSEPGVTG KGVPYSISI 

« Hide

References

[1]"Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns."
Royo J., Vancanneyt G., Perez A.G., Sanz C., Stormann K., Rosahl S., Sanchez-Serrano J.J.
J. Biol. Chem. 271:21012-21019(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY WOUNDING; JASMONATE AND ABSCISIC ACID, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"A leaf lipoxygenase of potato induced specifically by pathogen infection."
Kolomiets M.V., Chen H., Gladon R.J., Braun E.J., Hannapel D.J.
Plant Physiol. 124:1121-1130(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY PATHOGEN.
[3]"Lipoxygenase H1 gene silencing reveals a specific role in supplying fatty acid hydroperoxides for aliphatic aldehyde production."
Leon J., Royo J., Vancanneyt G., Sanz C., Silkowski H., Griffiths G., Sanchez-Serrano J.J.
J. Biol. Chem. 277:416-423(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
[4]"Differential distribution of the lipoxygenase pathway enzymes within potato chloroplasts."
Farmaki T., Sanmartin M., Jimenez P., Paneque M., Sanz C., Vancanneyt G., Leon J., Sanchez-Serrano J.J.
J. Exp. Bot. 58:555-568(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION BY WOUNDING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96405 mRNA. Translation: CAA65268.1.
PIRT07062.
RefSeqNP_001274843.1. NM_001287914.1.
UniGeneStu.18313.

3D structure databases

ProteinModelPortalO24370.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102596122.
KEGGsot:102596122.

Phylogenomic databases

KOK00454.

Enzyme and pathway databases

UniPathwayUPA00382.

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 nameLOX21_SOLTU
AccessionPrimary (citable) accession number: O24370
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 92 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