NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
DOI=10.1093/pcp/pcg142; PubMed=14634153 [NCBI, ExPASy, EBI, Israel, Japan]
Mizuno K., Iida T., Takano A., Yokoyama M., Fujimura T.;
"A new 9-lipoxygenase cDNA from developing rice seeds.";
Plant Cell Physiol. 44:1168-1175(2003).

[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. This lipoxygenase introduces molecular oxygen exclusively into the C-9 position of linoleic and linolenic.
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).
DEVELOPMENTAL STAGE: Expressed in the embryo 1 day after inbibition, and at low levels in developing seeds between 3 and 20 days after flowering.
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

AB099850; BAD02945.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC097368; AAO38440.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC093017; AAX95631.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001050990.1; -.

UniGene

Os.18598

3D structure databases

HSSP

P08170; 2SBL. [HSSP ENTRY / PDB]

ModBase

Q76I22.

Organism-specific databases

Gramene

Q76I22; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016165;	Molecular function: lipoxygenase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0031408;	Biological process: oxylipin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
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).

Genome annotation databases

GeneID

4333818; -.

KEGG

osa:4333818; -.

Other

ProtoNet

Q76I22.

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`	`1 863`	`863`	`Lipoxygenase 1.`	`PRO_0000220707`
`DOMAIN`	`32 158`	`127`	`PLAT.`
`DOMAIN`	`161 863`	`703`	`Lipoxygenase.`
`METAL`	`518 518`		`Iron; catalytic (By similarity).`
`METAL`	`523 523`		`Iron; catalytic (By similarity).`
`METAL`	`709 709`		`Iron; catalytic (By similarity).`
`METAL`	`713 713`		`Iron; catalytic (By similarity).`
`METAL`	`863 863`		`Iron; via carboxylate; catalytic (By similarity).`
`CONFLICT`	`160 160`		`N -> I (in Ref. 1; BAD02945).`
`CONFLICT`	`163 163`		`L -> P (in Ref. 1; BAD02945).`
`CONFLICT`	`513 513`		`H -> R (in Ref. 1; BAD02945).`
`CONFLICT`	`527 527`		`E -> K (in Ref. 1; BAD02945).`
`CONFLICT`	`596 596`		`T -> A (in Ref. 1; BAD02945).`
`CONFLICT`	`663 663`		`E -> A (in Ref. 1; BAD02945).`

Sequence information

Length: 863 AA [This is the length of the unprocessed precursor]

Molecular weight: 97499 Da [This is the MW of the unprocessed precursor]

CRC64: AA8309F3DBCEC2F1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLGGLKDKLT GKNGNKIKGL AVLMSRKLLD PRDFTASLLD NVHEVFGNSI TCQLVSATVA 

        70         80         90        100        110        120 
DQNNEGRGIV GSEANLEQGL TDLPSVSQGE SKLTVRFNWE MDKHGVPGAI IIKNHHSTKF 

       130        140        150        160        170        180 
FLKTITLHDV PGCDTIVFVA NSWIYPVGKY HYNRIFFANN SYLPSQMPEA LRPYREDELR 

       190        200        210        220        230        240 
YLRGEDRQGP YQEHDRIYRY DVYNDLGEPD RDNPRPVLGG SQKHPYPRRG RTGRIPTKKD 

       250        260        270        280        290        300 
PNSESRLSLL EQIYVPSDER FAHLKMSDFA GYSIKAIVQG ILPAIRTYVD LTPGEFDSFE 

       310        320        330        340        350        360 
DILKLYRGGL KLPSIPALEE LRKSFPVQLI KDLLPVGGSY LLKFPKPDII KENEVAWRTD 

       370        380        390        400        410        420 
EEFAREILAG LNPMVIRRLT EFPPKSTLDP SKYGDQTSTI TPAHIEKNLE GLSVQQALDS 

       430        440        450        460        470        480 
NRLYILDHHD HFMPFLIDIN SLDGIFTYAT RTLLFLRDDD TLKPLAIELS LPHIEGNLTS 

       490        500        510        520        530        540 
AKSKVHTPAS SGIESWVWQL AKAYVAVNDS GWHQLISHWL NTHAVMEPFV IATNRQLSVT 

       550        560        570        580        590        600 
HPVYKLLQPH YRDTMTINAL ARQTLINGGG IFEQTVFPGK HALAMSSAVY KNWNFTEQGL 

       610        620        630        640        650        660 
PDDLIKRGIA IKDPSSPSKV KLLIKDYPYA TDGLAIWQAI EQWVTEYCAI YYPNDGVLQG 

       670        680        690        700        710        720 
DVELQAWWKE VREVGHGDLK DADWWPKMQS LPELTKACTT IIWIASALHA AVNFGQYPYA 

       730        740        750        760        770        780 
GYLPNRPTIS RRPMPEPGSK EYTELDENPE KFFIRTITSQ FQTILGVSLI EILSKHSADE 

       790        800        810        820        830        840 
IYLGQRDTPE WTSDPKALEA FKRFSRQLVE IESKVLNMNK DPLLKNRVGP ANFPYTLMFP 

       850        860 
NTSDNKGAAE GITARGIPNS ISI

Q76I22 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