Arachidonate 12-lipoxygenase, 12S-type

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Reviewed, UniProtKB/Swiss-Prot P18054 (LOX12_HUMAN)

Last modified June 16, 2009. Version 108. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Arachidonate 12-lipoxygenase, 12S-type
      Short name=12-LOX
    EC=1.13.11.31
Alternative name(s):
    Platelet-type lipoxygenase 12

Gene names

Name:	ALOX12
Synonyms:	LOG12

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (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.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.

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Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from mutant phenotype. Source: UniProtKB cell motion Inferred from mutant phenotype. Source: UniProtKB fatty acid oxidation Inferred from mutant phenotype. Source: UniProtKB leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell adhesion Inferred from mutant phenotype. Source: UniProtKB positive regulation of cell growth Inferred from mutant phenotype. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype. Source: UniProtKB superoxide release Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB sarcolemma Inferred from direct assay. Source: UniProtKB
Molecular function	arachidonate 12-lipoxygenase activity Ref.1 Ref.2 Inferred from direct assay. Source: UniProtKB hepoxilin-epoxide hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW lipoxygenase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ITGB4	P16144	2	EBI-1633210,EBI-948678
KRT5	P13647	3	EBI-1633210,EBI-702187
LMNA	P02545	3	EBI-1633210,EBI-351935
TRIB1	Q96RU8	2	EBI-1633210,EBI-492555

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 663

662

Arachidonate 12-lipoxygenase, 12S-type

PRO_0000220682

Regions

Domain

2 – 114

113

PLAT

Domain

115 – 663

549

Lipoxygenase

Sites

Metal binding

360

Iron; catalytic

Metal binding

365

Iron; catalytic

Metal binding

540

Iron; catalytic

Metal binding

544

Iron; catalytic By similarity

Metal binding

663

Iron; via carboxylate; catalytic By similarity

Natural variations

Natural variant

259

E → K: dbSNP rs4987104.

VAR_030471

Natural variant

261

Q → R: dbSNP rs1126667. Ref.2 Ref.4 Ref.5 Ref.11

VAR_018743

Natural variant

298

A → T

VAR_004279

Natural variant

322

N → S: dbSNP rs434473. Ref.4 Ref.1 Ref.3

VAR_018744

Natural variant

430

R → H: dbSNP rs11571342. Ref.4

VAR_018745

Experimental info

Sequence conflict

189 – 192

RVYT → PCLH in AAA51533. Ref.3

Sequence conflict

345

S → C in AAA51533. Ref.3

Sequence conflict

389

L → P in AAA60056. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P18054-1 [UniParc].

Last modified February 6, 2007. Version 4.
Checksum: C4D6D5B320666A77
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FASTA

663

75,694

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, primary structure, and expression of the human platelet/erythroleukemia cell 12-lipoxygenase." Funk C.D., Furci L., Fitzgerald G.A. Proc. Natl. Acad. Sci. U.S.A. 87:5638-5642(1990) [PubMed: 2377602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-322.
[2]	"Cloning of the cDNA for human 12-lipoxygenase." Izumi T., Hoshiko S., Raadmark O., Samuelsson B. Proc. Natl. Acad. Sci. U.S.A. 87:7477-7481(1990) [PubMed: 2217179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-261.
[3]	"Molecular cloning and expression of human arachidonate 12-lipoxygenase." Yoshimoto T., Yamamoto Y., Arakawa T., Suzuki H., Yamamoto S., Yokoyama C., Tanabe T., Toh H. Biochem. Biophys. Res. Commun. 172:1230-1235(1990) [PubMed: 2244907] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-322.
[4]	SeattleSNPs variation discovery resource Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-261; SER-322 AND HIS-430.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-261.
[6]	"Structure and chromosomal localization of human arachidonate 12-lipoxygenase gene." Yoshimoto T., Arakawa T., Hada T., Yamamoto S., Takahashi E. J. Biol. Chem. 267:24805-24809(1992) [PubMed: 1447217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
[7]	"Characterization of human 12-lipoxygenase genes." Funk C.D., Funk L.B., Fitzgerald G.A., Samuelsson B. Proc. Natl. Acad. Sci. U.S.A. 89:3962-3966(1992) [PubMed: 1570320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
[8]	"Epidermis contains platelet-type 12-lipoxygenase that is overexpressed in germinal layer keratinocytes in psoriasis." Hussain H., Shornick L.P., Shannon V.R., Wilson J.D., Funk C.D., Pentland A.P., Holtzman M.J. Am. J. Physiol. 266:C243-C253(1994) [PubMed: 8304420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 340-427. Tissue: Skin.
[9]	"EU-IMAGE: full-insert length sequencing of human cDNA clones." Persson A.E., Lundeberg J., Uhlen M. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 531-663.
[10]	"Crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12s-type." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 172-662 IN COMPLEX WITH IRON IONS.
[11]	"Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk." Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C. Carcinogenesis 25:2467-2472(2004) [PubMed: 15308583] [Abstract] Cited for: VARIANT ARG-261.
+	Additional computationally mapped references.

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Web resources

SeattleSNPs

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases

M35418 mRNA. Translation: AAA60056.1.
M58704 mRNA. Translation: AAA59523.1.
M62982 mRNA. Translation: AAA51533.1.
AY527817 Genomic DNA. Translation: AAS00094.1.
BC069557 mRNA. Translation: AAH69557.1.
D12638 Genomic DNA. Translation: BAA02162.1.
M87004 Genomic DNA. Translation: AAA51587.1.
S68587 mRNA. Translation: AAD14020.1.
AF143883 mRNA. Translation: AAD32700.1.

IPI

IPI00218915.

PIR

A38283.

RefSeq

NP_000688.2.

UniGene

Hs.654431

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ABU	model	-	A	2-663	[»]
3D3L	X-ray	2.60	A/B	172-662	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P18054. 4 interactions.

Proteomic databases

PRIDE

P18054.

Genome annotation databases

Ensembl

ENSG00000108839. Homo sapiens. [Contig view]

GeneID

239.

KEGG

hsa:239.

NMPDR

fig|9606.3.peg.12986.

Organism-specific databases

GeneCards

GC17P006840.

H-InvDB

HIX0039067.

HGNC

HGNC:429. ALOX12.

HPA

HPA010691.

MIM

152391. gene.

PharmGKB

PA45.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P18054.

HOVERGEN

P18054.

OMA

P18054. ACLQMAI.

Enzyme and pathway databases

BRENDA

1.13.11.31. 247.

Gene expression databases

ArrayExpress

P18054.

Bgee

P18054.

CleanEx

HS_ALOX12.

GermOnline

ENSG00000108839. Homo sapiens.

Family and domain databases

InterPro

IPR000907. LipOase.
IPR013819. LipOase_C.
IPR001024. LipOase_LH2.
IPR001885. LipOase_mml.
[Graphical view]

Gene3D

G3DSA:2.60.60.20. Lipase_LipOase. 1 hit.

PANTHER

PTHR11771. LipOase. 1 hit.

Pfam

PF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]

PRINTS

PR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.

SMART

SM00308. LH2. 1 hit.
[Graphical view]

PROSITE

PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

952.

SOURCE

Search...

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Entry information

Entry name

LOX12_HUMAN

Accession

Primary (citable) accession number: P18054
Secondary accession number(s): O95569, Q6ISF8, Q9UQM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents