NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Red Mexican;
TISSUE=Leaf;
PubMed=8400375 [NCBI, ExPASy, EBI, Israel, Japan]
Slusarenko A.J., Meier B.M., Shaw N.;
"Spatial and temporal accumulation of defense gene transcripts in bean (Phaseolus vulgaris) leaves in relation to bacteria-induced hypersensitive cell death.";
Mol. Plant Microbe Interact. 6:453-466(1993).

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. Iron is tightly bound (By similarity).
PATHWAY: Lipid metabolism; oxylipin biosynthesis .
SUBUNIT: Monomer.
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

X63521; CAA45086.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S18906; S18906.

3D structure databases

HSSP

P08170; 2SBL. [HSSP ENTRY / PDB]

ModBase

P27481.

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.

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 >741`	`>741`	`Lipoxygenase.`	`PRO_0000220716`
`DOMAIN`	`<1 53`	`>53`	`PLAT.`
`DOMAIN`	`56 741`	`686`	`Lipoxygenase.`
`METAL`	`407 407`		`Iron; catalytic (By similarity).`
`METAL`	`412 412`		`Iron; catalytic (By similarity).`
`METAL`	`598 598`		`Iron; catalytic (By similarity).`
`METAL`	`602 602`		`Iron; catalytic (By similarity).`
`NON_TER`	`1 1`
`NON_TER`	`741 741`

Sequence information

Length: 741 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 84197 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 2F2CDD5979606AC1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
IPGAFYIKNF MQVEFYLKSL TLEDIPNHGT IHFICNSWIY NSKVYKSDRI FFANNTYLPS 

        70         80         90        100        110        120 
ETPAPLLKYR EEELKNVRGD GSGERKEWDR VYDYDVYNDL GNPDKGAALA RPVLGGSTLP 

       130        140        150        160        170        180 
YPRRGRTGRP KTKKDPNSEK PSDFVYLPRD EAFGHLKSSD FLAYGLKSVS QDVLPVLTDA 

       190        200        210        220        230        240 
FDGNLLSLEF DNFAEVHKLY EGGVTLPTNF LSKYAPIPIV KEIFRSDGEQ FLKYPPPKVM 

       250        260        270        280        290        300 
QVNKSAWMTD EEFARETIAG VNPNVIKSLE EFPPRSKLDT QSFGDHTSII TKEHLEINLG 

       310        320        330        340        350        360 
GLTVEQAIQS KKLFILDHHD YLIPYLRRIN ASATKTYATR TIFFLKSDGT LAPLAIELSK 

       370        380        390        400        410        420 
PHPQGDEHGP VSEVYVPAYE GVEAYIWLLA KAYVVVNDSC YHQLVSHWLN THAVVEPFVL 

       430        440        450        460        470        480 
ATNRQLSVVH PVYKLLFPHY RDTMNINSLA RKSLVNADGI IEKTFLWGRY ALELSAVIYK 

       490        500        510        520        530        540 
DWSLHDQALP NDLVKRGVAV KDPSAPHGVK LVIEDYPYAS DGLEIWDAIK SWVVEYVAFY 

       550        560        570        580        590        600 
YKSDEVLQQD SELQAWWKEL VQVGHGDLKD KPWWPKMQSR ENLVEVSTTL IWIASALHAA 

       610        620        630        640        650        660 
VNFGQYPYGG LILNRPTISR RFMPEKGSAE YAALAKNPEK EFLKTITGKK ETLIDLTVIE 

       670        680        690        700        710        720 
ILSRHASDEI YLGERDGGDH WTSDAGPLEA FKRFGKKLAE IEKKLVQKNN DETLRNRTGP 

       730        740 
AKMPYTLLYP SSEEGLTFRG I

P27481 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