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O24371 (LOX31_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 91. 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 3-1, chloroplastic

EC=1.13.11.12
Gene names
Name:LOX3.1
Synonyms:LOX-H3
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length914 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Required for the regulation of wound-induced gene expression, but is not 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. Ref.1 Ref.2

Catalytic activity

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

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

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 Ref.4 Ref.5.

Tissue specificity

Expressed in roots and leaves. Detected in tubers and flower buds. Ref.1

Induction

Up-regulated localy and systemically 30 minutes after wounding. Up-regulated by jasmonate and abscisic acid treatment. Not induced by pathogen infection. Ref.1 Ref.3 Ref.5

Miscellaneous

Depletion of LOX-H3 by co-suppression-mediated gene silencing leads to higher tuber yield, but has no effect on the number of tubers per plant.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8383Chloroplast Potential
Chain84 – 914831Linoleate 13S-lipoxygenase 3-1, chloroplastic
PRO_0000412928

Regions

Domain96 – 218123PLAT
Domain221 – 914694Lipoxygenase

Sites

Metal binding5741Iron; catalytic By similarity
Metal binding5791Iron; catalytic By similarity
Metal binding7651Iron; catalytic By similarity
Metal binding7691Iron; catalytic By similarity
Metal binding9141Iron; via carboxylate; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
O24371 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 45BBC7D7180390E4

FASTA914103,089
        10         20         30         40         50         60 
MALAKEIMGI SLLEKSSSFM NSSSMALFNP NNYHKENHLW FNQQFQGRRN LSRRKAFRQS 

        70         80         90        100        110        120 
TMAAISENLI KVVPEKAVRF KVRAVVTVRN KNKEDLKETI VKHLDAFTDK IGRNVTLELI 

       130        140        150        160        170        180 
STDMDPNTKG PKKSNQAVLK DWSKKSNLKT ERVNYTAEFI VDSNFGNPGA ITVTNKHQQE 

       190        200        210        220        230        240 
FFLESITIEG FACGPVHFPC NSWVQPKKDH PGKRIFFSNQ PYLPDETPAG LKSLRERELR 

       250        260        270        280        290        300 
DLRGDGKGVR KLSDRIYDYD IYNDLGNPDK GIDFARPKLG GDDNVPYPRR CRSGRVPTDT 

       310        320        330        340        350        360 
DISAESRVEK PNPTYVPRDE QFEESKMNTF STSRLKAVLH NLIPSLMASI SSNNHDFKGF 

       370        380        390        400        410        420 
SDIDNLYSKG LLLKLGLQDE VLKKLPLPKV VSSIKEGDLL KYDTPKILSK DKFAWLRDDE 

       430        440        450        460        470        480 
FARQAIAGVN PVSIEKLQFF PPVSKLDPEI YGPQESALKE EHILGHLNGM TVQEALDANK 

       490        500        510        520        530        540 
LFIVDHHDVY LPFLDRINAL DGRKAYATRT IFFLSDVGTL KPIAIELSLP QTGPSSRSKR 

       550        560        570        580        590        600 
VVTPPVCATG NWTWQIAKAH VCANDAGVHQ LVNHWLRTHA SLEPFILAAH RQLSAMHPIY 

       610        620        630        640        650        660 
KLLDPHMRYT LEINGLARQS LINADGVIEA CFTPGRYCME ISAAAYKNWR FDLEGLPADL 

       670        680        690        700        710        720 
IRRGMAVPDS TQPHGLKLLI EDYPYAADGL MIWGAIESWV RDYVNHYYPS SAQVCSDREL 

       730        740        750        760        770        780 
QAWYAETINV GHVDLRNEEW WPTLATPEDL ISILTTLIWL ASAQHAALNF GQYPYGGYVP 

       790        800        810        820        830        840 
NRPPLMRRLI PDENDPEYAV FLADPQKYFF SALPSLLQAT KFMAVVDTLS THSPDEEYLG 

       850        860        870        880        890        900 
ERHQPSTWTG DAEIVEAFYK FSAEIGRIEK EIDERNANTK LKNRCGAGVL PYELLAPSSG 

       910 
PGVTCRGVPN SVSI 

« 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.
Tissue: Leaf.
[2]"Antisense-mediated depletion of a potato lipoxygenase reduces wound induction of proteinase inhibitors and increases weight gain of insect pests."
Royo J., Leon J., Vancanneyt G., Albar J.P., Rosahl S., Ortego F., Castanera P., Sanchez-Serrano J.J.
Proc. Natl. Acad. Sci. U.S.A. 96:1146-1151(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"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.
[4]"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: SUBCELLULAR LOCATION.
[5]"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
X96406 mRNA. Translation: CAA65269.1.
PIRT07065.
RefSeqNP_001275115.1. NM_001288186.1.
UniGeneStu.213.

3D structure databases

ProteinModelPortalO24371.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102597498.
KEGGsot:102597498.

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 nameLOX31_SOLTU
AccessionPrimary (citable) accession number: O24371
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 91 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