[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Birte; PubMed=2515855 [NCBI, ExPASy, EBI, Israel, Japan] Ealing P.M., Casey R.; "The cDNA cloning of a pea (Pisum sativum) seed lipoxygenase. Sequence comparisons of the two major pea seed lipoxygenase isoforms."; Biochem. J. 264:929-932(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Birte; Casey R.; Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.

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. It 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 (By similarity).
PATHWAY: Lipid metabolism; oxylipin biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
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

X17061; CAA34906.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X78580; CAA55318.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S07075; S07075.

3D structure databases

HSSP

P08170; 2SBL. [HSSP ENTRY / PDB]

ModBase

P14856.

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).

Other

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`	`1 864`	`864`	`Seed lipoxygenase-2.`	`PRO_0000220713`
`DOMAIN`	`46 171`	`126`	`PLAT.`
`DOMAIN`	`174 864`	`691`	`Lipoxygenase.`
`METAL`	`524 524`		`Iron; catalytic (By similarity).`
`METAL`	`529 529`		`Iron; catalytic (By similarity).`
`METAL`	`716 716`		`Iron; catalytic (By similarity).`
`METAL`	`720 720`		`Iron; catalytic (By similarity).`
`METAL`	`864 864`		`Iron; via carboxylate; catalytic (By similarity).`
`CONFLICT`	`333 333`		`L -> I (in Ref. 2; CAA55318).`
`CONFLICT`	`562 562`		`Missing (in Ref. 2; CAA55318).`
`CONFLICT`	`578 578`		`L -> I (in Ref. 2; CAA55318).`

Sequence information

Length: 864 AA [This is the length of the unprocessed precursor]

Molecular weight: 97134 Da [This is the MW of the unprocessed precursor]

CRC64: 2919AF5FAF272CDF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFPNVTGLLN KGHKIRGTVV LMRKNVLDFN TIVSIGGGNV HGVIDSGINI IGSTLDGLTA 

        70         80         90        100        110        120 
FLGRSVSLQL ISATKSDANG KGKVGKDTFL EGVLASLPTL GAGESAFNIH FEWDHEMGIP 

       130        140        150        160        170        180 
GAFYIKNYMQ VEFFLKSLTL EDVPNHGTIR FVCNSWVYNS KLYKSPRIFF ANKSYLPSET 

       190        200        210        220        230        240 
PSPLVKYREE ELQTLRGDGT GERKLHERIY DYDVYNDLGN PDHGEHLARP ILGGSSTHPY 

       250        260        270        280        290        300 
PRRGRTGRYP TRKDPNSEKP ATETYVPRDE NFGHLKSSDF LAYGIKSVSQ CVVPAFESAF 

       310        320        330        340        350        360 
DLNFTPNEFD SFQDVRNLFE GGIKLPLDVI STLSPLPVVK EIFRTDGEQV LKFTPPHVIR 

       370        380        390        400        410        420 
VSKSAWMTDE EFAREMLAGV NPCMIRGLQE FPPKSNLDPA EYGDHTSKIS VDVLNLDGCT 

       430        440        450        460        470        480 
IDEALASGRL FILDYHDTFI PFLRRINETS AKAYATRTIL FLKENGTLKP VAIELSLPHP 

       490        500        510        520        530        540 
DGDKSGFVSK VILPADEGVE STIWLLAKAY VVVNDSCYHQ LMSHWLNTHA VIEPFVIATN 

       550        560        570        580        590        600 
RQLSVVHPIN KLLAPHYRDT MMNINALARD SLINANGLIE RSFLPSKYAV EMSSAVYKYW 

       610        620        630        640        650        660 
VFTDQALPND LIKRNMAVKD SSSPYGLRLL IEDYPYAVDG LEIWTAIKTW VQDYVSLYYA 

       670        680        690        700        710        720 
TDNDIKNDSE LQHWWKEVVE KGHGDLKDKP WWPKLQTFDE LVEVCTIIIW TASALHAAVN 

       730        740        750        760        770        780 
FGQYPYGGLI LNRPTLSRRL LPEEGTAEYD EMVKSSQKAY LRTITPKFQT LIDLSVIEIL 

       790        800        810        820        830        840 
SRHASDEVYL GQRENPHWTS DSKALQAFQK FGNKLAEIEA KLTNKNNDPS LYHRVGPVQL 

       850        860 
PYTLLHPSSK EGLTFRGIPN SISI

P14856 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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