[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Birte; PubMed=3140791 [NCBI, ExPASy, EBI, Israel, Japan] Ealing P.M., Casey R.; "The complete amino acid sequence of a pea (Pisum sativum) seed lipoxygenase predicted from a near full-length cDNA."; Biochem. J. 253:915-918(1988).
[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

X07807; CAA30666.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X78581; CAA55319.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S01142; S01142.

3D structure databases

HSSP

P08170; 1F8N. [HSSP ENTRY / PDB]

SMR

P09918; 39-861.

ModBase

P09918.

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`	`1 861`	`861`	`Seed lipoxygenase-3.`	`PRO_0000220714`
`DOMAIN`	`41 166`	`126`	`PLAT.`
`DOMAIN`	`169 861`	`693`	`Lipoxygenase.`
`METAL`	`522 522`		`Iron; catalytic (By similarity).`
`METAL`	`527 527`		`Iron; catalytic (By similarity).`
`METAL`	`713 713`		`Iron; catalytic (By similarity).`
`METAL`	`717 717`		`Iron; catalytic (By similarity).`
`METAL`	`861 861`		`Iron; via carboxylate; catalytic (By similarity).`

Sequence information

Length: 861 AA [This is the length of the unprocessed precursor]

Molecular weight: 97629 Da [This is the MW of the unprocessed precursor]

CRC64: 442510278225D750 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFSGVTGILN RGHKIKGTVV LMRKNVLDIN SLTTVGGVIG QGFDILGSTV DNLTAFLGRS 

        70         80         90        100        110        120 
VSLQLISATK PDATGKGKLG KATFLEGIIS SLPTLGAGQS AFKIHFEWDD DMGIPGAFYI 

       130        140        150        160        170        180 
KNFMQTEFFL VSLTLDDIPN HGSIYFVCNS WIYNAKHHKI DRIFFANQTY LPSETPAPLV 

       190        200        210        220        230        240 
HYREEELNNL RGDGTGERKE WERIYDYDVY NDLGNPDSGE NHARPVLGGS ETYPYPRRGR 

       250        260        270        280        290        300 
TGRKPTRKDP NSESRSDYVY LPRDEAFGHL KSSDFLTYGL KAVSQNVVPA LESVFFDLNF 

       310        320        330        340        350        360 
TPNEFDSFDE VHGLYEGGIK LPTNILSQIS PLPVLKEIFR TDGENTLKYP PPKVIQVSRS 

       370        380        390        400        410        420 
GWMTDEEFAR EMLAGVNPNV ICCLQEFPPR SKLDSQIYGD HTSKISKEHL EPNLEGLTVE 

       430        440        450        460        470        480 
EAIQNKKLFL LDHHDSIMPY LRRINSTSTK AYATRTILFL NNNQNLKPLA IELSLPHPQG 

       490        500        510        520        530        540 
DEHGAVSYVY QPALEGVESS IWLLAKAYVI VNDSCYHQLV SHWLNTHAVV EPFVIATNRH 

       550        560        570        580        590        600 
LSCLHPIYKL LYPHYRDTMN INSLARLSLV NDGGIIEKTF LWGRYSMEMS SKVYKNWVFT 

       610        620        630        640        650        660 
EQALPADLIK RGMAIEDPSS PCGVKLVVED YPYAVDGLEI WAIIKTWVQD YVSLYYTSDE 

       670        680        690        700        710        720 
KLRQDSELQA WWKELVEVGH GDKKNEPWWP KMQTREDLIE VCSIVIWTAS ALHAAVNFGQ 

       730        740        750        760        770        780 
YSYGGLILNR PTLSRRFMPE KGSAEFEELV KSPQKAYLKT ITPKFQTLID LSVIEILSRH 

       790        800        810        820        830        840 
ASDELYLGER DNPNWTSDKR ALEAFKKFGN KLAEIEKKLT QRNNDEKLRN RHGPVEMPYT 

       850        860 
LLYPSSKEGL TFRGIPNSIS I

P09918 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