[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-322. PubMed=2377602 [NCBI, ExPASy, EBI, Israel, Japan] Funk C.D., Furci L., Fitzgerald G.A.; "Molecular cloning, primary structure, and expression of the human platelet/erythroleukemia cell 12-lipoxygenase."; Proc. Natl. Acad. Sci. U.S.A. 87:5638-5642(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-261. PubMed=2217179 [NCBI, ExPASy, EBI, Israel, Japan] Izumi T., Hoshiko S., Raadmark O., Samuelsson B.; "Cloning of the cDNA for human 12-lipoxygenase."; Proc. Natl. Acad. Sci. U.S.A. 87:7477-7481(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-322. DOI=10.1016/0006-291X(90)91580-L; PubMed=2244907 [NCBI, ExPASy, EBI, Israel, Japan] Yoshimoto T., Yamamoto Y., Arakawa T., Suzuki H., Yamamoto S., Yokoyama C., Tanabe T., Toh H.; "Molecular cloning and expression of human arachidonate 12-lipoxygenase."; Biochem. Biophys. Res. Commun. 172:1230-1235(1990).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-261; SER-322 AND HIS-430. SeattleSNPs program for genomic applications; Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-261. 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).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112. PubMed=1447217 [NCBI, ExPASy, EBI, Israel, Japan] Yoshimoto T., Arakawa T., Hada T., Yamamoto S., Takahashi E.; "Structure and chromosomal localization of human arachidonate 12-lipoxygenase gene."; J. Biol. Chem. 267:24805-24809(1992).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45. PubMed=1570320 [NCBI, ExPASy, EBI, Israel, Japan] Funk C.D., Funk L.B., Fitzgerald G.A., Samuelsson B.; "Characterization of human 12-lipoxygenase genes."; Proc. Natl. Acad. Sci. U.S.A. 89:3962-3966(1992).
[8]	NUCLEOTIDE SEQUENCE [MRNA] OF 340-427. TISSUE=Skin; PubMed=8304420 [NCBI, ExPASy, EBI, Israel, Japan] Hussain H., Shornick L.P., Shannon V.R., Wilson J.D., Funk C.D., Pentland A.P., Holtzman M.J.; "Epidermis contains platelet-type 12-lipoxygenase that is overexpressed in germinal layer keratinocytes in psoriasis."; Am. J. Physiol. 266:C243-C253(1994).
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 531-663. Persson A.E., Lundeberg J., Uhlen M.; "EU-IMAGE: full-insert length sequencing of human cDNA clones."; Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[10]	VARIANT ARG-261. DOI=10.1093/carcin/bgh260; PubMed=15308583 [NCBI, ExPASy, EBI, Israel, Japan] Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.; "Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk."; Carcinogenesis 25:2467-2472(2004).

Comments

FUNCTION: Oxygenase and 14,15-leukotriene A4 synthase activity.
CATALYTIC ACTIVITY: Arachidonate + O₂ = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.
COFACTOR: Binds 1 iron ion per subunit.
PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis .
INTERACTION:
P16144:ITGB4; NbExp=2; IntAct=EBI-1633210, EBI-948678;
P13647:KRT5; NbExp=3; IntAct=EBI-1633210, EBI-702187;
P02545:LMNA; NbExp=3; IntAct=EBI-1633210, EBI-351935;
Q96RU8:TRIB1; NbExp=2; IntAct=EBI-1633210, EBI-492555;
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the lipoxygenase family.
SIMILARITY: Contains 1 lipoxygenase domain.
SIMILARITY: Contains 1 PLAT domain.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/alox12/";.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/ALOX12ID620ch17p13.html";.

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

M35418; AAA60056.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M58704; AAA59523.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M62982; AAA51533.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY527817; AAS00094.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069557; AAH69557.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D12638; BAA02162.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M87004; AAA51587.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S68587; AAD14020.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF143883; AAD32700.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A38283; A38283.

NP_000688.2; -.

3D structure databases

PDB

2ABU; Model; -; A=2-663.

[ExPASy / RCSB / EBI]

PDBsum

2ABU; -.

ModBase

P18054.

Protein-protein interaction databases

IntAct

P18054; -.

Organism-specific databases

HIX0039067; -.

HGNC:429; ALOX12.

HPA010691; -.

152391; gene. [NCBI / EBI]

PharmGKB

PA45; -.

GeneCards

P18054.

Gene expression databases

ArrayExpress

P18054; -.

CleanEx

HS_ALOX12; -.

GermOnline

ENSG00000108839; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0042383;	Cellular component: sarcolemma (inferred from direct assay from UniProtKB).
GO:0004052;	Molecular function: arachidonate 12-lipoxygenase activity (inferred from direct assay from UniProtKB).
GO:0047977;	Molecular function: hepoxilin-epoxide hydrolase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006916;	Biological process: anti-apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0006928;	Biological process: cell motion (inferred from mutant phenotype from UniProtKB).
GO:0019395;	Biological process: fatty acid oxidation (inferred from mutant phenotype from UniProtKB).
GO:0045785;	Biological process: positive regulation of cell adhesion (inferred from mutant phenotype from UniProtKB).
GO:0030307;	Biological process: positive regulation of cell growth (inferred from mutant phenotype from UniProtKB).
GO:0008284;	Biological process: positive regulation of cell proliferation (inferred from mutant phenotype from UniProtKB).
GO:0042554;	Biological process: superoxide release (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).

BLOCKS

P18054.

Genome annotation databases

Ensembl

ENSG00000108839; Homo sapiens. [Contig view]

GeneID

239; -.

KEGG

hsa:239; -.

NMPDR

fig|9606.3.peg.12986; -.

Phylogenomic databases

HOGENOM

P18054; -.

HOVERGEN

P18054; -.

Other

LinkHub

P18054; -.

SOURCE

ALOX12; Homo sapiens.

ProtoNet

P18054.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 663`	`662`	`Arachidonate 12-lipoxygenase, 12S-type.`	`PRO_0000220682`
`DOMAIN`	`2 114`	`113`	`PLAT.`
`DOMAIN`	`115 663`	`549`	`Lipoxygenase.`
`METAL`	`360 360`		`Iron; catalytic (By similarity).`
`METAL`	`365 365`		`Iron; catalytic (By similarity).`
`METAL`	`540 540`		`Iron; catalytic (By similarity).`
`METAL`	`544 544`		`Iron; catalytic (By similarity).`
`METAL`	`663 663`		`Iron; via carboxylate; catalytic (By similarity).`
`VARIANT`	`259 259`	`1`	`E -> K (in dbSNP:rs4987104 [NCBI]).`	`VAR_030471`
`VARIANT`	`261 261`	`1`	`Q -> R (in dbSNP:rs1126667 [NCBI]).`	`VAR_018743`
`VARIANT`	`298 298`	`1`	`A -> T.`	`VAR_004279`
`VARIANT`	`322 322`	`1`	`N -> S (in dbSNP:rs434473 [NCBI]).`	`VAR_018744`
`VARIANT`	`430 430`	`1`	`R -> H (in dbSNP:rs11571342 [NCBI]).`	`VAR_018745`
`CONFLICT`	`189 192`		`RVYT -> PCLH (in Ref. 3; AAA51533).`
`CONFLICT`	`345 345`		`S -> C (in Ref. 3; AAA51533).`
`CONFLICT`	`389 389`		`L -> P (in Ref. 1; AAA60056).`

Sequence information

Length: 663 AA [This is the length of the unprocessed precursor]

Molecular weight: 75694 Da [This is the MW of the unprocessed precursor]

CRC64: C4D6D5B320666A77 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGRYRIRVAT GAWLFSGSYN RVQLWLVGTR GEAELELQLR PARGEEEEFD HDVAEDLGLL 

        70         80         90        100        110        120 
QFVRLRKHHW LVDDAWFCDR ITVQGPGACA EVAFPCYRWV QGEDILSLPE GTARLPGDNA 

       130        140        150        160        170        180 
LDMFQKHREK ELKDRQQIYC WATWKEGLPL TIAADRKDDL PPNMRFHEEK RLDFEWTLKA 

       190        200        210        220        230        240 
GALEMALKRV YTLLSSWNCL EDFDQIFWGQ KSALAEKVRQ CWQDDELFSY QFLNGANPML 

       250        260        270        280        290        300 
LRRSTSLPSR LVLPSGMEEL QAQLEKELQN GSLFEADFIL LDGIPANVIR GEKQYLAAPL 

       310        320        330        340        350        360 
VMLKMEPNGK LQPMVIQIQP PNPSSPTPTL FLPSDPPLAW LLAKSWVRNS DFQLHEIQYH 

       370        380        390        400        410        420 
LLNTHLVAEV IAVATMRCLP GLHPIFKFLI PHIRYTMEIN TRARTQLISD GGIFDKAVST 

       430        440        450        460        470        480 
GGGGHVQLLR RAAAQLTYCS LCPPDDLADR GLLGLPGALY AHDALRLWEI IARYVEGIVH 

       490        500        510        520        530        540 
LFYQRDDIVK GDPELQAWCR EITEVGLCQA QDRGFPVSFQ SQSQLCHFLT MCVFTCTAQH 

       550        560        570        580        590        600 
AAINQGQLDW YAWVPNAPCT MRMPPPTTKE DVTMATVMGS LPDVRQACLQ MAISWHLSRR 

       610        620        630        640        650        660 
QPDMVPLGHH KEKYFSGPKP KAVLNQFRTD LEKLEKEITA RNEQLDWPYE YLKPSCIENS 


VTI

P18054 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