Reviewed, UniProtKB/Swiss-Prot P29250 (LOX2_ORYSJ)

Names and origin

Protein names

Recommended name:
    Lipoxygenase 2
    EC=1.13.11.12
Alternative name(s):
    Lipoxygenase L-2

Gene names

Name:	LOX1.1
Ordered Locus Names:	Os03g0738600, LOC_Os03g52860
ORF Names:	OSJNBa0057G07.15

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	870 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (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. Ref.1
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 structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Oxylipin biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to other organism Ref.1 Inferred from direct assay. Source: Gramene response to wounding Ref.1 Inferred from direct assay. Source: Gramene
Cellular component	cytoplasm Ref.1 Inferred from direct assay. Source: Gramene
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW lipoxygenase activity Ref.1 Inferred from direct assay. Source: Gramene
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 870	870	Lipoxygenase 2		PRO_0000220708
Regions
	Domain	32 – 158	127	PLAT
	Domain	161 – 870	710	Lipoxygenase
Sites
	Metal binding	525	1	Iron; catalytic By similarity
	Metal binding	530	1	Iron; catalytic By similarity
	Metal binding	716	1	Iron; catalytic By similarity
	Metal binding	720	1	Iron; catalytic By similarity
	Metal binding	870	1	Iron; via carboxylate; catalytic By similarity
Experimental info
	Sequence conflict	40 – 41	2	DG → ER in CAA45738. Ref.1
	Sequence conflict	168	1	P → A in CAA45738. Ref.1
	Sequence conflict	336	1	Missing in CAA45738. Ref.1
	Sequence conflict	385 – 387	3	RSR → EP in CAA45738. Ref.1
	Sequence conflict	464	1	Missing in CAA45738. Ref.1
	Sequence conflict	492 – 500	9	RGGTGAGAV → AAAPAPAL in CAA45738. Ref.1
	Sequence conflict	566	1	A → G in CAA45738. Ref.1
	Sequence conflict	587 – 588	2	KH → ND in CAA45738. Ref.1
	Sequence conflict	617 – 619	3	AVP → RT in CAA45738. Ref.1
	Sequence conflict	644 – 646	3	WHA → CTP in CAA45738. Ref.1
	Sequence conflict	700 – 701	2	EL → DV in CAA45738. Ref.1
	Sequence conflict	740	1	P → A in CAA45738. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P29250-1 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 63344755867DA6E0	FASTA	870	97,184
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of rice lipoxygenase L-2 and characterization using an active enzyme expressed from the cDNA in Escherichia coli." Ohta H., Shirano Y., Tanaka K., Morita Y., Shibata D. Eur. J. Biochem. 206:331-336(1992) [PubMed: 1597177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: cv. Nipponbare. Tissue: Seedling.
[2]	"Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species." 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., 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. Genome Res. 15:1284-1291(2005) [PubMed: 16109971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X64396 mRNA. Translation: CAA45738.1. AC117988 Genomic DNA. Translation: AAP44707.1.
PIR	S23454.
RefSeq	NP_001051212.1.
UniGene	Os.53604
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4334049.
KEGG	osa:4334049.
Organism-specific databases
Gramene	P29250.
Family and domain databases
InterPro	IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. IPR001024. LipOase_LH2. IPR001246. LipOase_pln. [Graphical view]
Gene3D	G3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHER	PTHR11771. LipOase. 1 hit.
Pfam	PF00305. Lipoxygenase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PRINTS	PR00087. LIPOXYGENASE. PR00468. PLTLPOXGNASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
PROSITE	PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LOX2_ORYSJ

Accession

Primary (citable) accession number: P29250
Secondary accession number(s): Q7Y1F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	August 30, 2005
Last modified:	November 24, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)