[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Desiree; TISSUE=Tuber; DOI=10.1104/pp.107.1.265; PubMed=7870815 [NCBI, ExPASy, EBI, Israel, Japan] Casey R.; "Sequence of a cDNA clone encoding a potato (Solanum tuberosum) tuber lipoxygenase."; Plant Physiol. 107:265-266(1995).

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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

X79107; CAA55724.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S44940; S44940.

3D structure databases

HSSP

P08170; 1FGT. [HSSP ENTRY / PDB]

ModBase

P37831.

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`	`Lipoxygenase 1.`	`PRO_0000220722`
`DOMAIN`	`29 160`	`132`	`PLAT.`
`DOMAIN`	`163 861`	`699`	`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: 96967 Da [This is the MW of the unprocessed precursor]

CRC64: 09732A6751DEE20D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIGQITSGLF GGHDDSKKVK GTVVMMNKNV LDFTDLAGSL TGKIFDVLGQ KVSFQLISSV 

        70         80         90        100        110        120 
QGDPTNGLQG KHSNPAYLEN SLFTLTPLTA GSETAFGVTF DWNEEFGVPG AFIIKNMHIN 

       130        140        150        160        170        180 
EFFLKSLTLE DVPNHGKVHF VCNSWVYPSL NYKSDRIFFA NQPYLPSETP ELLRKYRENE 

       190        200        210        220        230        240 
LLTLRGDGTG KREAWDRIYD YDIYNDLGNP DQGKENVRTT LGGSAEYPYP RRGRTGRPPT 

       250        260        270        280        290        300 
RTDPKSESRI PLILSLDIYV PRDERFGHLK MSDFLTYALK SIVQFILPEL HALFDGTPNE 

       310        320        330        340        350        360 
FDSFEDVLRL YEGGIKLPQG PLFKALTAAI PLEMIRELLR TDGEGILRFP TPLVIKDSKT 

       370        380        390        400        410        420 
AWRTDEEFAR EMLAGVNPVI ISRLQEFPPK SKLDPEAYGN QNSTITAEHI EDKLDGLTVD 

       430        440        450        460        470        480 
EAMNNNKLFI LNHHDVIIPY LRRINTTITK AYASRTLLFL QDNGSLKPLA IELSFPHPDG 

       490        500        510        520        530        540 
DQFGVTSKVY TPSDQGVESS IWQLAKAYVA VNDVGVHQLI SHWLNTHAVI EPFVIATNRQ 

       550        560        570        580        590        600 
LSVLHPIHKL LYPHFRDTMN INASARQLLV NAGGVLESTV FQSKFAMEMS AVVYKDWVFP 

       610        620        630        640        650        660 
DQALPADLVK RGVAVEDSSS PHGVRLLIED YPYAVDGLEI WSAIKSWVTD YCSFYYGSDE 

       670        680        690        700        710        720 
EILKDNELQA WWKELREVGH GDKKNEPWWP EMETPQELID SCTTIIWIAS ALHAAVNFGQ 

       730        740        750        760        770        780 
YPYAGYLPNR PTVSRRFMPE PGTPEYEELK RNPDKAFLKT ITAQLQTLLG VSLVEILSRH 

       790        800        810        820        830        840 
TTDEIYLGQR ESPEWTKDKE PLAAFDRFGK KLTDIEKQII QRNGDNILTN RSGPVNAPYT 

       850        860 
LLFPTSEGGL TGKGIPNSVS I

P37831 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