[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/S0006-291X(88)80271-7; PubMed=3202857 [NCBI, ExPASy, EBI, Israel, Japan] Sigal E., Craik C.S., Highland E., Grunberger D., Costello L.L., Dixon R.A.F., Nadel J.A.; "Molecular cloning and primary structure of human 15-lipoxygenase."; Biochem. Biophys. Res. Commun. 157:457-464(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/S0167-4781(97)00005-5; PubMed=9224951 [NCBI, ExPASy, EBI, Israel, Japan] Kritzik M.R., Ziober A.F., Dicharry S., Conrad D.J., Sigal E.; "Characterization and sequence of an additional 15-lipoxygenase transcript and of the human gene."; Biochim. Biophys. Acta 1352:267-281(1997).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-90; LYS-103 AND GLN-205. SeattleSNPs program for genomic applications; Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-461. TISSUE=Brain, and Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46. DOI=10.1023/A:1006813009006; PubMed=9700053 [NCBI, ExPASy, EBI, Israel, Japan] Kelavkar U., Wang S., Montero A., Murtagh J., Shah K., Badr K.; "Human 15-lipoxygenase gene promoter: analysis and identification of DNA binding sites for IL-13-induced regulatory factors in monocytes."; Mol. Biol. Rep. 25:173-182(1998).
[6]	PROTEIN SEQUENCE OF 2-16. PubMed=3356688 [NCBI, ExPASy, EBI, Israel, Japan] Sigal E., Grunberger D., Craik C.S., Caughey G.H., Nadel J.A.; "Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases."; J. Biol. Chem. 263:5328-5332(1988).
[7]	PROTEIN SEQUENCE OF 2-31; 38-45; 157-168 AND 626-631. TISSUE=Eosinophil, and Leukocyte; PubMed=1662607 [NCBI, ExPASy, EBI, Israel, Japan] Izumi T., Raadmark O., Joernvall H., Samuelsson B.; "Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes."; Eur. J. Biochem. 202:1231-1238(1991).
[8]	MUTAGENESIS OF MET-418. DOI=10.1038/354149a0; PubMed=1944593 [NCBI, ExPASy, EBI, Israel, Japan] Sloane D.L., Leung R., Craik C.S., Sigal E.; "A primary determinant for lipoxygenase positional specificity."; Nature 354:149-152(1991).

Comments

FUNCTION: Converts arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid. Also acts on C-12 of arachidonate as well as on linoleic acid.
CATALYTIC ACTIVITY: Arachidonate + O₂ = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.
COFACTOR: Binds 1 iron ion per subunit (By similarity).
PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the lipoxygenase family.
SIMILARITY: Contains 1 lipoxygenase domain.
SIMILARITY: Contains 1 PLAT domain.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/ALOX15ID42986ch17p13.html";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/alox15/";.

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

M23892; AAA36182.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U88317; AAB49305.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY505111; AAR84235.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC029032; AAH29032.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U63384; AAC52118.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A31349; A31349.

NP_001131.3; -.

3D structure databases

PDB

2ABT; Model; -; A=2-662.

[ExPASy / RCSB / EBI]

2ABT; -.

P16050; 2-662.

Organism-specific databases

HIX0013446; -.

HGNC:433; ALOX15.

HPA013859; -.

152392; gene. [NCBI / EBI]

PharmGKB

PA48; -.

GeneCards

P16050.

Gene expression databases

ArrayExpress

P16050; -.

CleanEx

HS_ALOX15; -.

GermOnline

ENSG00000161905; Homo sapiens.

Ontologies

GO:0016165;	Molecular function: lipoxygenase activity (traceable author statement from ProtInc).
GO:0006954;	Biological process: inflammatory response (traceable author statement from ProtInc).
GO:0006629;	Biological process: lipid metabolic process (non-traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR000907; LipOase.
IPR013819; LipOase_C.
IPR001024; LipOase_LH2.
IPR001885; LipOase_mml.
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.
PR00467; MAMLPOXGNASE.

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).

BLOCKS

P16050.

Genome annotation databases

Ensembl

ENSG00000161905; Homo sapiens. [Contig view]

GeneID

246; -.

KEGG

hsa:246; -.

NMPDR

fig|9606.3.peg.12905; -.

Phylogenomic databases

HOGENOM

P16050; -.

HOVERGEN

P16050; -.

Other

DrugBank

DB01188; Ciclopirox.
DB00179; Masoprocol.
DB00744; Zileuton.

LinkHub

P16050; -.

SOURCE

ALOX15; Homo sapiens.

ProtoNet

P16050.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Dioxygenase; Direct protein sequencing; Iron; Leukotriene biosynthesis; Metal-binding; Oxidoreductase; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 662`	`661`	`Arachidonate 15-lipoxygenase.`	`PRO_0000220697`
`DOMAIN`	`2 114`	`113`	`PLAT.`
`DOMAIN`	`115 662`	`548`	`Lipoxygenase.`
`METAL`	`360 360`		`Iron; catalytic (By similarity).`
`METAL`	`365 365`		`Iron; catalytic (By similarity).`
`METAL`	`540 540`		`Iron; catalytic (By similarity).`
`METAL`	`662 662`		`Iron; via carboxylate; catalytic (By similarity).`
`VARIANT`	`90 90`	`1`	`D -> H (in dbSNP:rs11568142 [NCBI]).`	`VAR_018746 [3D]`
`VARIANT`	`102 102`	`1`	`G -> V (in dbSNP:rs41439950 [NCBI]).`	`VAR_035036 [3D]`
`VARIANT`	`103 103`	`1`	`N -> K (in dbSNP:rs11568099 [NCBI]).`	`VAR_018747 [3D]`
`VARIANT`	`205 205`	`1`	`R -> Q (in dbSNP:rs11568101 [NCBI]).`	`VAR_018748 [3D]`
`VARIANT`	`239 239`	`1`	`V -> M (in dbSNP:rs3892408 [NCBI]).`	`VAR_035037 [3D]`
`VARIANT`	`461 461`	`1`	`A -> P (in dbSNP:rs17852628 [NCBI]).`	`VAR_035038 [3D]`
`VARIANT`	`560 560`	`1`	`T -> M (in dbSNP:rs34210653 [NCBI]).`	`VAR_035039 [3D]`
`MUTAGEN`	`418 418`		`M->V: Catalyzes 15- and 12-lipoxygenation.`
`CONFLICT`	`46 46`		`E -> V (in Ref. 5; AAC52118).`

Sequence information

Length: 662 AA [This is the length of the unprocessed precursor]

Molecular weight: 74804 Da [This is the MW of the unprocessed precursor]

CRC64: 9ACF7FE7863A045C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLYRIRVST GASLYAGSNN QVQLWLVGQH GEAALGKRLW PARGKETELK VEVPEYLGPL 

        70         80         90        100        110        120 
LFVKLRKRHL LKDDAWFCNW ISVQGPGAGD EVRFPCYRWV EGNGVLSLPE GTGRTVGEDP 

       130        140        150        160        170        180 
QGLFQKHREE ELEERRKLYR WGNWKDGLIL NMAGAKLYDL PVDERFLEDK RVDFEVSLAK 

       190        200        210        220        230        240 
GLADLAIKDS LNVLTCWKDL DDFNRIFWCG QSKLAERVRD SWKEDALFGY QFLNGANPVV 

       250        260        270        280        290        300 
LRRSAHLPAR LVFPPGMEEL QAQLEKELEG GTLFEADFSL LDGIKANVIL CSQQHLAAPL 

       310        320        330        340        350        360 
VMLKLQPDGK LLPMVIQLQL PRTGSPPPPL FLPTDPPMAW LLAKCWVRSS DFQLHELQSH 

       370        380        390        400        410        420 
LLRGHLMAEV IVVATMRCLP SIHPIFKLII PHLRYTLEIN VRARTGLVSD MGIFDQIMST 

       430        440        450        460        470        480 
GGGGHVQLLK QAGAFLTYSS FCPPDDLADR GLLGVKSSFY AQDALRLWEI IYRYVEGIVS 

       490        500        510        520        530        540 
LHYKTDVAVK DDPELQTWCR EITEIGLQGA QDRGFPVSLQ ARDQVCHFVT MCIFTCTGQH 

       550        560        570        580        590        600 
ASVHLGQLDW YSWVPNAPCT MRLPPPTTKD ATLETVMATL PNFHQASLQM SITWQLGRRQ 

       610        620        630        640        650        660 
PVMVAVGQHE EEYFSGPEPK AVLKKFREEL AALDKEIEIR NAKLDMPYEY LRPSVVENSV 


AI

P16050 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