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O24379 (LOX12_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. 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 9S-lipoxygenase 2

EC=1.13.11.58
Alternative name(s):
Lipoxygenase 1-2
Gene names
Name:LOX1.2
Synonyms:LOX1, T8
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length861 AA.
Sequence statusComplete.
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. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linoleic acid is the preferred substrate, but is also active with linolenic and arachidonic acids. Ref.1

Catalytic activity

Linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate. Ref.1

Cofactor

Binds 1 iron ion per subunit. Iron is tightly bound By similarity.

Pathway

Lipid metabolism; oxylipin biosynthesis.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in tubers and roots. Detected in flower buds and leaves. Ref.1

Developmental stage

Expressed in stolons and increases during early stages of tuber development. Ref.1

Induction

Up-regulated in roots 2 hours after jasmonate treatment and 24 hours after wounding. Not induced in the leaves. Ref.1

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

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Oxylipin biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processoxylipin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

lipoxygenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 861861Linoleate 9S-lipoxygenase 2
PRO_0000412920

Regions

Domain29 – 160132PLAT
Domain163 – 861699Lipoxygenase
Compositional bias446 – 4516Poly-Thr

Sites

Metal binding5221Iron; catalytic By similarity
Metal binding5271Iron; catalytic By similarity
Metal binding7131Iron; catalytic By similarity
Metal binding7171Iron; catalytic By similarity
Metal binding8611Iron; via carboxylate; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
O24379 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 25783F32C69BFA26

FASTA86197,067
        10         20         30         40         50         60 
MIGQITSGLF GGPDDSKKLK GTVVMMNKNA LDFTDLAGSL TDKAFEFLGQ TVSFQLISSV 

        70         80         90        100        110        120 
QGDPTNGLQG KHSNPAYLEN SLFTLTPLTA GSETAFGVTF DWNEEFGVPG AFIIKNTHIN 

       130        140        150        160        170        180 
EFFLKSLTLE DVPNHGKVHF VCNSWVYPSF RYKSDRIFFV NQPYLPSKTP ELLRKYRENE 

       190        200        210        220        230        240 
LLTLRGDGTG KREAWDRIYD YDIYNDLGNP DEGKENVRTT LGGSAEYPYP RRGRTGRPPT 

       250        260        270        280        290        300 
RTDPKSESRI PLILSLDIYV PRDERFGHLK MSDFLTYALK SIVQFILPEL HALFDGTPNE 

       310        320        330        340        350        360 
FDSFEDVLRL YEGGIKLPQG PLFKALTAAI PLEMIRELLR TDGEGILRFP TPLVIKDSKT 

       370        380        390        400        410        420 
AWRTDEEFAR EMLAGVNPVI ISRLQEFPPK SKLDPEAYGN QNSTITAEHI EDKLDGLTVD 

       430        440        450        460        470        480 
EAMNNNKLFI LNHHDVLIPY LRRINTTTTK TYASRTLLFL QDNGSLKPLA IELSLPHPDG 

       490        500        510        520        530        540 
DQFGVTSKVY TPSDQGVESS IWQLAKAYVA VNDSGVHQLI SHWLNTHAVI EPFVIATNRQ 

       550        560        570        580        590        600 
LSVLHPIHKL LYPHFRDTMN INAMARQILI NAGGVLESTV FQSKFAMEMS AVVYKDWVFP 

       610        620        630        640        650        660 
DQALPADLVK RGVAVEDSSS PHGVRLLIED YPYAVDGLEI WSAIKSWVSD YCSFYYGSDE 

       670        680        690        700        710        720 
EILKDNELQA WWKELREVGH GDKKNEPWWP EMERPQELID SCTTIIWIAS ALHAAVNFGQ 

       730        740        750        760        770        780 
YPYAGYLPNR PTVSRRFMPE PGTPEYEELK KNPDKAFLKT ITAQLQTLLG VSLIEILSRH 

       790        800        810        820        830        840 
TTDEIYLGQR ESPEWTKDKE PLAAFDKFGK KLTDIEKQII QRNGDNILTN RSGPVNAPYT 

       850        860 
LLFPTSEGGL TGKGIPNSVS I 

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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, DEVELOPMENTAL STAGE, INDUCTION BY WOUNDING AND JASMONATE, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: cv. Desiree.
Tissue: Tuber.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95513 mRNA. Translation: CAA64766.1.

3D structure databases

HSSPHSSP built from PDB template 1FGT based on UniProtKB P08170.
ProteinModelPortalO24379.
SMRO24379. Positions 18-861.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12726.
UniPathwayUPA00382.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001024. LipOase_LH2.
IPR001246. LipOase_pln.
[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]
SUPFAMSSF49723. Lipase_LipOase. 1 hit.
SSF48484. Lipoxygenase. 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 nameLOX12_SOLTU
AccessionPrimary (citable) accession number: O24379
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families