[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). TISSUE=Skin; DOI=10.1073/pnas.94.12.6148; PubMed=9177185 [NCBI, ExPASy, EBI, Israel, Japan] Brash A.R., Boeglin W.E., Chang M.S.; "Discovery of a second 15S-lipoxygenase in humans."; Proc. Natl. Acad. Sci. U.S.A. 94:6148-6152(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1006/geno.2001.6519; PubMed=11350124 [NCBI, ExPASy, EBI, Israel, Japan] Krieg P., Marks F., Fuerstenberger G.; "A gene cluster encoding human epidermis-type lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression."; Genomics 73:323-330(2001).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D). DOI=10.1074/jbc.M111936200; PubMed=11839751 [NCBI, ExPASy, EBI, Israel, Japan] Tang S., Bhatia B., Maldonado C.J., Yang P., Newman R.A., Liu J., Chandra D., Traag J., Klein R.D., Fischer S.M., Chopra D., Shen J., Zhau H.E., Chung L.W.K., Tang D.G.; "Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells."; J. Biol. Chem. 277:16189-16201(2002).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). TISSUE=Skin; 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 337-484 (ISOFORM B). DOI=10.1046/j.1432-1327.1999.00818.x; PubMed=10542053 [NCBI, ExPASy, EBI, Israel, Japan] Kilty I., Logan A., Vickers P.J.; "Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase."; Eur. J. Biochem. 266:83-93(1999).

Comments

FUNCTION: Converts arachidonic acid exclusively to 15S-hydroperoxyeicosatetraenoic acid, while linoleic acid is less well metabolized.
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 (By similarity).

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	A
Isoform ID	O15296-1
This is the isoform sequence displayed in this entry.

Name	B
Synonyms	15-LOX2sv-b
Isoform ID	O15296-2
Features which should be applied to build the isoform sequence: VSP_003142, VSP_003143.

Name	C
Synonyms	15-LOX2sv-c
Isoform ID	O15296-3
Features which should be applied to build the isoform sequence: VSP_003144, VSP_003145.

Name	D
Synonyms	15-LOX2sv-a
Isoform ID	O15296-4
Features which should be applied to build the isoform sequence: VSP_003142.

TISSUE SPECIFICITY: Expressed in hair, prostate, lung and cornea.
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

U78294; AAB61706.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ305028; CAC34521.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ305029; CAC34521.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ305030; CAC34521.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ305031; CAC34521.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF468051; AAL76274.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF468052; AAL76275.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF468053; AAL76276.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF468054; AAL76277.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC035217; AAH35217.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063647; AAH63647.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF149095; AAD37786.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00005781; -.
IPI00220009; -.
IPI00220010; -.
IPI00470667; -.

RefSeq

NP_001034219.1; -.
NP_001034220.1; -.
NP_001132.2; -.

UniGene

Hs.111256

3D structure databases

HSSP

P12530; 1LOX. [HSSP ENTRY / PDB]

ModBase

O15296.

Enzyme and pathway databases

BRENDA

1.13.11.33; 247.

Organism-specific databases

GC17P007883; -.

HIX0027139; -.

HGNC:434; ALOX15B.

603697; gene. [NCBI / EBI]

PharmGKB

PA24725; -.

Gene expression databases

O15296; -.

O15296; -.

HS_ALOX15B; -.

ENSG00000179593; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0050473;	Molecular function: arachidonate 15-lipoxygenase activity (inferred from direct assay from UniProtKB).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016165;	Molecular function: lipoxygenase activity (traceable author statement from ProtInc).
GO:0006917;	Biological process: induction of apoptosis (traceable author statement from UniProtKB).
GO:0019370;	Biological process: leukotriene biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0045786;	Biological process: negative regulation of cell cycle (inferred from direct assay from UniProtKB).
GO:0030336;	Biological process: negative regulation of cell migration (traceable author statement from UniProtKB).
GO:0008285;	Biological process: negative regulation of cell proliferation (inferred from direct assay from UniProtKB).
GO:0045926;	Biological process: negative regulation of growth (inferred from direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0030850;	Biological process: prostate gland development (non-traceable author statement from UniProtKB).
GO:0030856;	Biological process: regulation of epithelial cell differentiation (non-traceable author statement from UniProtKB).
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).

Genome annotation databases

Ensembl

ENSG00000179593; Homo sapiens. [Contig view]

GeneID

247; -.

KEGG

hsa:247; -.

Phylogenomic databases

HOVERGEN

O15296; -.

Other

NextBio

985; -.

SOURCE

ALOX15B; Homo sapiens.

ProtoNet

O15296.

UniRef

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

Keywords

Alternative splicing; Cytoplasm; Dioxygenase; Iron; Leukotriene biosynthesis; Metal-binding; Oxidoreductase; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 676`	`676`	`Arachidonate 15-lipoxygenase type II.`	`PRO_0000220700`
`DOMAIN`	`2 124`	`123`	`PLAT.`
`DOMAIN`	`125 676`	`552`	`Lipoxygenase.`
`METAL`	`373 373`		`Iron; catalytic (By similarity).`
`METAL`	`378 378`		`Iron; catalytic (By similarity).`
`METAL`	`553 553`		`Iron; catalytic (By similarity).`
`METAL`	`676 676`		`Iron; via carboxylate; catalytic (By similarity).`
`VAR_SEQ`	`401 429`		`Missing (in isoform B and isoform D).`	`VSP_003142`
`VAR_SEQ`	`483 527`		`Missing (in isoform B).`	`VSP_003143`
`VAR_SEQ`	`561 617`		`FDSCAWMPNLPPSMQLPPPTSKGLATCEGFIATLPPVNAT` `CDVILALWLLSKEPGDQ -> VRKGQRPRWQAGGDPAPQPHSALSAFSLTPVLGCPTCHPA` `CSCHHPPPKAWQHARAS (in isoform C).`	`VSP_003144`
`VAR_SEQ`	`618 676`		`Missing (in isoform C).`	`VSP_003145`
`VARIANT`	`647 647`	`1`	`I -> V (in dbSNP:rs7225107 [NCBI]).`	`VAR_035040`
`VARIANT`	`656 656`	`1`	`R -> Q (in dbSNP:rs4792147 [NCBI]).`	`VAR_024524`
`VARIANT`	`676 676`	`1`	`I -> V (in dbSNP:rs7225107 [NCBI]).`	`VAR_024525`
`CONFLICT`	`271 271`		`V -> L (in Ref. 1; AAB61706 and 2; CAC34521).`
`CONFLICT`	`338 338`		`G -> C (in Ref. 5; AAD37786).`
`CONFLICT`	`486 486`		`R -> H (in Ref. 3; AAL76274/AAL76275/AAL76277).`

Sequence information

Length: 676 AA [This is the length of the unprocessed precursor]

Molecular weight: 75885 Da [This is the MW of the unprocessed precursor]

CRC64: 4F641DF2FBB902C6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE EDFQVTLPED 

        70         80         90        100        110        120 
VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG HLLFPCYQWL EGAGTLVLQE 

       130        140        150        160        170        180 
GTAKVSWADH HPVLQQQRQE ELQARQEMYQ WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK 

       190        200        210        220        230        240 
NANFYLQAGS AFAEMKIKGL LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS 

       250        260        270        280        290        300 
QFLNGLNPVL IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 

       310        320        330        340        350        360 
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK WDWLLAKTWV 

       370        380        390        400        410        420 
RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK LLIPHTRYTL HINTLARELL 

       430        440        450        460        470        480 
IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI 

       490        500        510        520        530        540 
WGAVERFVSE IIGIYYPSDE SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ 

       550        560        570        580        590        600 
YVTMVIFTCS AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT 

       610        620        630        640        650        660 
CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG IQERNRGLVL 

       670 
PYTYLDPPLI ENSVSI

O15296 in FASTA 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