NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=cv. Nipponbare;
TISSUE=Seedling;
PubMed=1597177 [NCBI, ExPASy, EBI, Israel, Japan]
Ohta H., Shirano Y., Tanaka K., Morita Y., Shibata D.;
"cDNA cloning of rice lipoxygenase L-2 and characterization using an active enzyme expressed from the cDNA in Escherichia coli.";
Eur. J. Biochem. 206:331-336(1992).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
DOI=10.1101/gr.3869505; PubMed=16109971 [NCBI, ExPASy, EBI, Israel, Japan]
The rice chromosome 3 sequencing consortium;
Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.-I., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.;
"Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species.";
Genome Res. 15:1284-1291(2005).

Comments

FUNCTION: Plant lipoxygenase 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.
CATALYTIC ACTIVITY: Linoleate + O₂ = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate.
COFACTOR: Binds 1 iron ion per subunit. Iron is tightly bound (By similarity).
PATHWAY: Lipid metabolism; oxylipin biosynthesis .
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the lipoxygenase family.
SIMILARITY: Contains 1 lipoxygenase domain.
SIMILARITY: Contains 1 PLAT domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X64396; CAA45738.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC117988; AAP44707.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S23454; S23454.

NP_001051212.1; -.

3D structure databases

HSSP

P08170; 2SBL. [HSSP ENTRY / PDB]

ModBase

P29250.

Organism-specific databases

Gramene

P29250; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from Gramene).
GO:0016165;	Molecular function: lipoxygenase activity (inferred from direct assay from Gramene).
GO:0051707;	Biological process: response to other organism (inferred from direct assay from Gramene).
GO:0009611;	Biological process: response to wounding (inferred from direct assay from Gramene).
QuickGo view.

Family and domain databases

InterPro

IPR000907; LipOase.
IPR013819; LipOase_C.
IPR001024; LipOase_LH2.
IPR001246; LipOase_pln.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.60.20; Lipase_LipOase; 1.

PANTHER

PTHR11771; LipOase; 1.

Pfam

PF00305; Lipoxygenase; 1.
PF01477; PLAT; 1.
Pfam graphical view of domain structure.

PRINTS

PR00087; LIPOXYGENASE.
PR00468; PLTLPOXGNASE.

SMART

SM00308; LH2; 1.
SMART graphical view of domain structure.

PROSITE

PS00711; LIPOXYGENASE_1; 1.
PS00081; LIPOXYGENASE_2; 1.
PS51393; LIPOXYGENASE_3; 1.
PS50095; PLAT; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P29250.

Genome annotation databases

GeneID

4334049; -.

KEGG

osa:4334049; -.

Other

ProtoNet

P29250.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Iron; Lipid synthesis; Metal-binding; Oxidoreductase; Oxylipin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 870`	`870`	`Lipoxygenase 2.`	`PRO_0000220708`
`DOMAIN`	`32 158`	`127`	`PLAT.`
`DOMAIN`	`161 870`	`710`	`Lipoxygenase.`
`METAL`	`525 525`		`Iron; catalytic (By similarity).`
`METAL`	`530 530`		`Iron; catalytic (By similarity).`
`METAL`	`716 716`		`Iron; catalytic (By similarity).`
`METAL`	`720 720`		`Iron; catalytic (By similarity).`
`METAL`	`870 870`		`Iron; via carboxylate; catalytic (By similarity).`
`CONFLICT`	`40 41`		`DG -> ER (in Ref. 1; CAA45738).`
`CONFLICT`	`168 168`		`P -> A (in Ref. 1; CAA45738).`
`CONFLICT`	`336 336`		`Missing (in Ref. 1; CAA45738).`
`CONFLICT`	`385 387`		`RSR -> EP (in Ref. 1; CAA45738).`
`CONFLICT`	`464 464`		`Missing (in Ref. 1; CAA45738).`
`CONFLICT`	`492 500`		`RGGTGAGAV -> AAAPAPAL (in Ref. 1; CAA45738).`
`CONFLICT`	`566 566`		`A -> G (in Ref. 1; CAA45738).`
`CONFLICT`	`587 588`		`KH -> ND (in Ref. 1; CAA45738).`
`CONFLICT`	`617 619`		`AVP -> RT (in Ref. 1; CAA45738).`
`CONFLICT`	`644 646`		`WHA -> CTP (in Ref. 1; CAA45738).`
`CONFLICT`	`700 701`		`EL -> DV (in Ref. 1; CAA45738).`
`CONFLICT`	`740 740`		`P -> A (in Ref. 1; CAA45738).`

Sequence information

Length: 870 AA [This is the length of the unprocessed precursor]

Molecular weight: 97184 Da [This is the MW of the unprocessed precursor]

CRC64: 63344755867DA6E0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLGGIIGGLT GNKNARLKGS LVLMRKNALD INDFGATVID GISEFLGRGV TCQLVSSSLV 

        70         80         90        100        110        120 
DPNNGNRGRV GTEASLEQWL TSLPSLTTGE SKFGVTFEWE VEKMGIPGAI IVKNNHAAEF 

       130        140        150        160        170        180 
FLKTITLDNV PGHGAVVFVA NSWIYPASKY RYNRVFFSND TSLPSKMPAA LKPYRDDELR 

       190        200        210        220        230        240 
NLRGDDQQGP YQEHDRVYRY DVYNDLGEPD SGNPRPVLGG SPDRPYPRRG RTGRKPTKTD 

       250        260        270        280        290        300 
PTAESRLSLL ENIYVPRDER FGHLKMADFL GYSIKALVDG IVPAIRTYVD LTPGEFDSFK 

       310        320        330        340        350        360 
DILKLYEGGL KLPSIPALEE LRKRFPLQLV KDLIPAGGDY LLKLPMPHVI REDKKAWMTD 

       370        380        390        400        410        420 
DEFAREILAG VNPMVIARLT EFPPRSRLDP ARYGDQTSTI TAAHVERGLE GLTVQQAIDG 

       430        440        450        460        470        480 
NLLYVVDHHD HFMPYLLDIN SLDDNFIYAT RTLLFLRGDG TLAPLAIELS LPHLQDDGLI 

       490        500        510        520        530        540 
TARSTVYTPA ARGGTGAGAV EWWVWQLAKA YVNVNDYCWH QLISHWLNTH AVMEPFVIAT 

       550        560        570        580        590        600 
NRQLSVAHPV HKLLLPHYRD TMTINALARQ TLINGGGIFE MTVFPRKHAL AMSSAFYKDW 

       610        620        630        640        650        660 
SFADQALPDD LVKRGVAVPD PASPYKVRLL IEDYPYANDG LAVWHAIEQW ATEYLAIYYP 

       670        680        690        700        710        720 
NDGVLQGDAE LQAWWKEVRE VGHGDIKDAT WWPEMKTVAE LVKACATIIW IGSALHAAVN 

       730        740        750        760        770        780 
FGQYPYAGYL PNRPSVSRRP MPEPGTKEYD ELARDPEKVF VRTITKQMQA IVGISLLEIL 

       790        800        810        820        830        840 
SKHSSDEVYL GQRDTPEWTS DAKALEAFKR FGARLTEIES RVVAMNKDPH RKNRVGPTNF 

       850        860        870 
PYTLLYPNTS DLKGDAAGLS ARGIPNSISI

P29250 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools