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Arachidonate 12-lipoxygenase, 12S-type (12S-LOX) (12S-lipoxygenase) (EC 1.13.11.31) (Lipoxin synthase 12-LO) (EC 3.3.2.-) (Platelet-type lipoxygenase 12)

 LOX12_HUMAN             Reviewed;         663 AA.
P18054; O95569; Q6ISF8; Q9UQM4;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 4.
18-JUL-2018, entry version 196.
RecName: Full=Arachidonate 12-lipoxygenase, 12S-type;
Short=12S-LOX;
Short=12S-lipoxygenase;
EC=1.13.11.31;
AltName: Full=Lipoxin synthase 12-LO;
EC=3.3.2.-;
AltName: Full=Platelet-type lipoxygenase 12;
Name=ALOX12; Synonyms=12LO, LOG12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-322.
PubMed=2244907; DOI=10.1016/0006-291X(90)91580-L;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-322.
PubMed=2377602; DOI=10.1073/pnas.87.15.5638;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-261.
PubMed=2217179; DOI=10.1073/pnas.87.19.7477;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-261; SER-322 AND
HIS-430.
SeattleSNPs variation discovery resource;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-261.
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
PubMed=1447217;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
PubMed=1570320; DOI=10.1073/pnas.89.9.3962;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 340-427.
TISSUE=Skin;
PubMed=8304420;
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).
[10]
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.
[11]
CATALYTIC ACTIVITY, KINETIC PARAMETERS, PATHWAY, AND SUBSTRATE
SPECIFICITY.
PubMed=1851637; DOI=10.1016/0005-2760(91)90128-5;
Hada T., Ueda N., Takahashi Y., Yamamoto S.;
"Catalytic properties of human platelet 12-lipoxygenase as compared
with the enzymes of other origins.";
Biochim. Biophys. Acta 1083:89-93(1991).
[12]
FUNCTION IN LIPOXIN SYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND REACTION MECHANISM.
PubMed=8250832; DOI=10.1042/bj2960127;
Romano M., Chen X.S., Takahashi Y., Yamamoto S., Funk C.D.,
Serhan C.N.;
"Lipoxin synthase activity of human platelet 12-lipoxygenase.";
Biochem. J. 296:127-133(1993).
[13]
CATALYTIC ACTIVITY, KINETIC PARAMETERS, PH DEPENDENCE, AND SUBCELLULAR
LOCATION.
PubMed=8319693; DOI=10.1111/j.1432-1033.1993.tb17988.x;
Chen X.S., Brash A.R., Funk C.D.;
"Purification and characterization of recombinant histidine-tagged
human platelet 12-lipoxygenase expressed in a baculovirus/insect cell
system.";
Eur. J. Biochem. 214:845-852(1993).
[14]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-355; HIS-360; HIS-365;
HIS-383; HIS-392; LYS-416; ALA-417; VAL-418 AND HIS-540.
PubMed=8500694;
Chen X.S., Funk C.D.;
"Structure-function properties of human platelet 12-lipoxygenase:
chimeric enzyme and in vitro mutagenesis studies.";
FASEB J. 7:694-701(1993).
[15]
SUBCELLULAR LOCATION, ENZYME REGULATION, AND INDUCTION.
PubMed=8912711; DOI=10.1006/excr.1996.0317;
Hagmann W., Gao X., Timar J., Chen Y.Q., Strohmaier A.R.,
Fahrenkopf C., Kagawa D., Lee M., Zacharek A., Honn K.V.;
"12-Lipoxygenase in A431 cells: genetic identity, modulation of
expression, and intracellular localization.";
Exp. Cell Res. 228:197-205(1996).
[16]
FUNCTION IN ANGIOGENESIS.
PubMed=9751607;
Nie D., Hillman G.G., Geddes T., Tang K., Pierson C., Grignon D.J.,
Honn K.V.;
"Platelet-type 12-lipoxygenase in a human prostate carcinoma
stimulates angiogenesis and tumor growth.";
Cancer Res. 58:4047-4051(1998).
[17]
FUNCTION IN ANGIOGENESIS.
PubMed=16638750; DOI=10.1074/jbc.M601887200;
Nie D., Krishnamoorthy S., Jin R., Tang K., Chen Y., Qiao Y.,
Zacharek A., Guo Y., Milanini J., Pages G., Honn K.V.;
"Mechanisms regulating tumor angiogenesis by 12-lipoxygenase in
prostate cancer cells.";
J. Biol. Chem. 281:18601-18609(2006).
[18]
INDUCTION BY UV.
PubMed=18755188; DOI=10.1016/j.febslet.2008.08.017;
Yoo H., Jeon B., Jeon M.S., Lee H., Kim T.Y.;
"Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation
in human keratinocytes.";
FEBS Lett. 582:3249-3253(2008).
[19]
FUNCTION IN CELL MIGRATION.
PubMed=22237009; DOI=10.1016/j.yexcr.2011.12.017;
Klampfl T., Bogner E., Bednar W., Mager L., Massudom D., Kalny I.,
Heinzle C., Berger W., Staettner S., Karner J., Klimpfinger M.,
Fuerstenberger G., Krieg P., Marian B.;
"Up-regulation of 12(S)-lipoxygenase induces a migratory phenotype in
colorectal cancer cells.";
Exp. Cell Res. 318:768-778(2012).
[20]
FUNCTION IN APOPTOTIC PROCESS, AND TISSUE SPECIFICITY.
PubMed=23578768; DOI=10.1016/j.yexcr.2013.04.001;
Weisinger G., Grafi-Cohen M., Hirsh M., Knoll E., Sharon O., Many A.,
Limor R., Stern N.;
"12S-Lipoxygenase is necessary for human vascular smooth muscle cell
survival.";
Exp. Cell Res. 319:1586-1593(2013).
[21]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 172-662 IN COMPLEX WITH IRON
IONS.
Structural genomics consortium (SGC);
"Crystal structure of the lipoxygenase domain of human arachidonate
12-lipoxygenase, 12s-type.";
Submitted (FEB-2009) to the PDB data bank.
[22]
VARIANT ARG-261.
PubMed=15308583; DOI=10.1093/carcin/bgh260;
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).
[23]
VARIANT ARG-261, AND INVOLVEMENT IN COLORECTAL CANCER.
PubMed=17151091; DOI=10.1093/carcin/bgl242;
Tan W., Wu J., Zhang X., Guo Y., Liu J., Sun T., Zhang B., Zhao D.,
Yang M., Yu D., Lin D.;
"Associations of functional polymorphisms in cyclooxygenase-2 and
platelet 12-lipoxygenase with risk of occurrence and advanced disease
status of colorectal cancer.";
Carcinogenesis 28:1197-1201(2007).
[24]
VARIANT ARG-261, AND INVOLVEMENT IN ESOPHAGEAL CANCER.
PubMed=17460548; DOI=10.1097/FPC.0b013e328010bda1;
Guo Y., Zhang X., Tan W., Miao X., Sun T., Zhao D., Lin D.;
"Platelet 12-lipoxygenase Arg261Gln polymorphism: functional
characterization and association with risk of esophageal squamous cell
carcinoma in combination with COX-2 polymorphisms.";
Pharmacogenet. Genomics 17:197-205(2007).
-!- FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the
stereo-specific peroxidation of free and esterified
polyunsaturated fatty acids generating a spectrum of bioactive
lipid mediators. Mainly converts arachidonic acid to (12S)-
hydroperoxyeicosatetraenoic acid/(12S)-HPETE but can also
metabolize linoleic acid. Has a dual activity since it also
converts leukotriene A4/LTA4 into both the bioactive lipoxin
A4/LXA4 and lipoxin B4/LXB4. Through the production of specific
bioactive lipids like (12S)-HPETE it regulates different
biological processes including platelet activation. It also
probably positively regulates angiogenesis through regulation of
the expression of the vascular endothelial growth factor. Plays a
role in apoptotic process, promoting the survival of vascular
smooth muscle cells for instance. May also play a role in the
control of cell migration and proliferation.
{ECO:0000269|PubMed:16638750, ECO:0000269|PubMed:22237009,
ECO:0000269|PubMed:23578768, ECO:0000269|PubMed:8250832,
ECO:0000269|PubMed:9751607}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-
12-hydroperoxyicosa-5,8,10,14-tetraenoate.
-!- CATALYTIC ACTIVITY: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-
7,9,11,14-tetraenoate + H(2)O = (5S,6R,15S)-trihydroxy-
(7E,9E,11Z,13E)-eicosatetraenoate.
-!- CATALYTIC ACTIVITY: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-
7,9,11,14-tetraenoate + H(2)O = (5S,14R,15S)-trihydroxy-
(6E,8Z,10E,12E)-eicosatetraenoate.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Note=Binds 1 Fe cation per subunit.;
-!- ENZYME REGULATION: Activated by EGF. {ECO:0000269|PubMed:8912711}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8 uM for arachidonate (at pH 7.0 and 37 degrees Celsius)
{ECO:0000269|PubMed:1851637};
KM=10 uM for arachidonate (at pH 8.0 and 25 degrees Celsius)
{ECO:0000269|PubMed:8319693};
KM=6.2 uM for arachidonate (at pH 7.4)
{ECO:0000269|PubMed:8250832};
KM=9 uM for linoleate (at pH 8.0 and 25 degrees Celsius)
{ECO:0000269|PubMed:8319693};
KM=7.9 uM for leukotriene A4 (at pH 7.4)
{ECO:0000269|PubMed:8250832};
KM=3 uM for eicosa-5,8,11,14,17-pentaenoate (at pH 7.0 and 37
degrees Celsius) {ECO:0000269|PubMed:1851637};
KM=35 uM for eicosa-8,11,14-trienoate (at pH 7.0 and 37 degrees
Celsius) {ECO:0000269|PubMed:1851637};
KM=14.3 uM for 5,6-epoxy-8,11,14-eicosatrienoate (at pH 7.4)
{ECO:0000269|PubMed:8250832};
Vmax=3 umol/min/mg enzyme with arachidonate as substrate (at pH
8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:8319693};
Vmax=1.057 umol/min/mg enzyme with arachidonate as substrate (at
pH 7.4) {ECO:0000269|PubMed:8250832};
Vmax=0.0375 umol/min/mg enzyme with linoleate as substrate (at
pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:8319693};
Vmax=0.025 umol/min/mg enzyme with leukotriene A4 as substrate
(at pH 7.4) {ECO:0000269|PubMed:8250832};
Vmax=0.985 umol/min/mg enzyme with 5,6-epoxy-8,11,14-
eicosatrienoate as substrate (at pH 7.4)
{ECO:0000269|PubMed:8250832};
pH dependence:
Optimum pH is 7.5-8.0 (for arachidonate 12-lipoxygenase
activity). {ECO:0000269|PubMed:8250832,
ECO:0000269|PubMed:8319693};
-!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
biosynthesis. {ECO:0000269|PubMed:1851637}.
-!- INTERACTION:
P13647:KRT5; NbExp=7; IntAct=EBI-1633210, EBI-702187;
P02545:LMNA; NbExp=4; IntAct=EBI-1633210, EBI-351935;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane. Note=Membrane
association is stimulated by EGF.
-!- TISSUE SPECIFICITY: Expressed in vascular smooth muscle cells.
{ECO:0000269|PubMed:23578768}.
-!- INDUCTION: Down-regulated upon starvation, by UV-irradiation and
15-lipoxygenase metabolites. {ECO:0000269|PubMed:18755188,
ECO:0000269|PubMed:8912711}.
-!- DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of
the esophagus. The most common types are esophageal squamous cell
carcinoma and adenocarcinoma. Cancer of the esophagus remains a
devastating disease because it is usually not detected until it
has progressed to an advanced incurable stage.
{ECO:0000269|PubMed:17460548}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry. Gln at position 261 may confer interindividual
susceptibility to esophageal cancer (PubMed:17460548).
{ECO:0000269|PubMed:17460548}.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of
the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
{ECO:0000269|PubMed:17151091}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry. Gln at position 261 may confer interindividual
susceptibility to colorectal cancer (PubMed:17460548).
{ECO:0000269|PubMed:17460548}.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
-!- 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";
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EMBL; M62982; AAA51533.1; -; mRNA.
EMBL; M35418; AAA60056.1; -; mRNA.
EMBL; M58704; AAA59523.1; -; mRNA.
EMBL; AY527817; AAS00094.1; -; Genomic_DNA.
EMBL; AC040977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069557; AAH69557.1; -; mRNA.
EMBL; D12638; BAA02162.1; -; Genomic_DNA.
EMBL; M87004; AAA51587.1; -; Genomic_DNA.
EMBL; S68587; AAD14020.1; -; mRNA.
EMBL; AF143883; AAD32700.1; -; mRNA.
CCDS; CCDS11084.1; -.
PIR; A38283; A38283.
RefSeq; NP_000688.2; NM_000697.2.
UniGene; Hs.654431; -.
PDB; 2ABU; Model; -; A=2-663.
PDB; 3D3L; X-ray; 2.60 A; A/B=172-663.
PDBsum; 2ABU; -.
PDBsum; 3D3L; -.
ProteinModelPortal; P18054; -.
SMR; P18054; -.
BioGrid; 106740; 8.
IntAct; P18054; 5.
MINT; P18054; -.
STRING; 9606.ENSP00000251535; -.
BindingDB; P18054; -.
ChEMBL; CHEMBL3687; -.
GuidetoPHARMACOLOGY; 1387; -.
SwissLipids; SLP:000000670; -.
iPTMnet; P18054; -.
PhosphoSitePlus; P18054; -.
BioMuta; ALOX12; -.
DMDM; 125987838; -.
PaxDb; P18054; -.
PeptideAtlas; P18054; -.
PRIDE; P18054; -.
ProteomicsDB; 53540; -.
Ensembl; ENST00000251535; ENSP00000251535; ENSG00000108839.
GeneID; 239; -.
KEGG; hsa:239; -.
UCSC; uc002gdx.4; human.
CTD; 239; -.
DisGeNET; 239; -.
EuPathDB; HostDB:ENSG00000108839.11; -.
GeneCards; ALOX12; -.
H-InvDB; HIX0039067; -.
HGNC; HGNC:429; ALOX12.
HPA; CAB019287; -.
HPA; HPA010691; -.
MIM; 114500; phenotype.
MIM; 133239; phenotype.
MIM; 152391; gene.
neXtProt; NX_P18054; -.
OpenTargets; ENSG00000108839; -.
PharmGKB; PA45; -.
eggNOG; ENOG410IF0U; Eukaryota.
eggNOG; ENOG410YN4N; LUCA.
GeneTree; ENSGT00550000074415; -.
HOGENOM; HOG000234358; -.
HOVERGEN; HBG005150; -.
InParanoid; P18054; -.
KO; K00458; -.
OMA; MTITWHL; -.
OrthoDB; EOG091G04A4; -.
PhylomeDB; P18054; -.
TreeFam; TF105320; -.
BioCyc; MetaCyc:HS03167-MONOMER; -.
BRENDA; 1.13.11.31; 2681.
Reactome; R-HSA-2142696; Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
Reactome; R-HSA-2142700; Synthesis of Lipoxins (LX).
Reactome; R-HSA-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-HSA-9018677; Biosynthesis of DHA-derived SPMs.
Reactome; R-HSA-9025106; Biosynthesis of DPAn-6 SPMs.
Reactome; R-HSA-9026290; Biosynthesis of DPAn-3-derived maresins.
SABIO-RK; P18054; -.
UniPathway; UPA00881; -.
EvolutionaryTrace; P18054; -.
GeneWiki; ALOX12; -.
GenomeRNAi; 239; -.
PRO; PR:P18054; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108839; -.
CleanEx; HS_ALOX12; -.
ExpressionAtlas; P18054; baseline and differential.
Genevisible; P18054; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IDA:UniProtKB.
GO; GO:0051120; F:hepoxilin A3 synthase activity; TAS:Reactome.
GO; GO:0047977; F:hepoxilin-epoxide hydrolase activity; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:UniProtKB.
GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; TAS:Reactome.
GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
GO; GO:0019395; P:fatty acid oxidation; IMP:UniProtKB.
GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
GO; GO:0051121; P:hepoxilin metabolic process; TAS:Reactome.
GO; GO:1901751; P:leukotriene A4 metabolic process; IDA:UniProtKB.
GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB.
GO; GO:2001303; P:lipoxin A4 biosynthetic process; IDA:UniProtKB.
GO; GO:2001306; P:lipoxin B4 biosynthetic process; IDA:UniProtKB.
GO; GO:2001301; P:lipoxin biosynthetic process; TAS:Reactome.
GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IMP:UniProtKB.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0042554; P:superoxide anion generation; NAS:UniProtKB.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR036226; LipOase_C_sf.
InterPro; IPR020834; LipOase_CS.
InterPro; IPR020833; LipOase_Fe_BS.
InterPro; IPR001885; LipOase_mml.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
PANTHER; PTHR11771; PTHR11771; 1.
Pfam; PF00305; Lipoxygenase; 1.
Pfam; PF01477; PLAT; 1.
PRINTS; PR00087; LIPOXYGENASE.
PRINTS; PR00467; MAMLPOXGNASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF48484; SSF48484; 1.
SUPFAM; SSF49723; SSF49723; 1.
PROSITE; PS00711; LIPOXYGENASE_1; 1.
PROSITE; PS00081; LIPOXYGENASE_2; 1.
PROSITE; PS51393; LIPOXYGENASE_3; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Dioxygenase;
Fatty acid metabolism; Hydrolase; Iron; Lipid metabolism; Membrane;
Metal-binding; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 663 Arachidonate 12-lipoxygenase, 12S-type.
/FTId=PRO_0000220682.
DOMAIN 2 114 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
DOMAIN 115 663 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 360 360 Iron; catalytic.
METAL 365 365 Iron; catalytic.
METAL 540 540 Iron; catalytic.
METAL 544 544 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 663 663 Iron; via carboxylate; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00726}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000250|UniProtKB:F1LQ70}.
VARIANT 259 259 E -> K (in dbSNP:rs4987104).
/FTId=VAR_030471.
VARIANT 261 261 Q -> R (in dbSNP:rs1126667).
{ECO:0000269|PubMed:15308583,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17151091,
ECO:0000269|PubMed:17460548,
ECO:0000269|PubMed:2217179,
ECO:0000269|Ref.4}.
/FTId=VAR_018743.
VARIANT 298 298 A -> T.
/FTId=VAR_004279.
VARIANT 322 322 N -> S (in dbSNP:rs434473).
{ECO:0000269|PubMed:2244907,
ECO:0000269|PubMed:2377602,
ECO:0000269|Ref.4}.
/FTId=VAR_018744.
VARIANT 430 430 R -> H (in dbSNP:rs11571342).
{ECO:0000269|Ref.4}.
/FTId=VAR_018745.
MUTAGEN 355 355 H->Q: No effect on catalytic activity.
{ECO:0000269|PubMed:8500694}.
MUTAGEN 360 360 H->Q,Y: Complete loss of catalytic
activity. {ECO:0000269|PubMed:8500694}.
MUTAGEN 365 365 H->Q: Complete loss of catalytic
activity. {ECO:0000269|PubMed:8500694}.
MUTAGEN 383 383 H->Q: Altered catalytic activity and
protein expression.
{ECO:0000269|PubMed:8500694}.
MUTAGEN 392 392 H->Q: No effect on catalytic activity.
{ECO:0000269|PubMed:8500694}.
MUTAGEN 416 416 K->Q: Reduced catalytic activity. No
effect on the stereoselectivity of the
oxygenation reaction.
{ECO:0000269|PubMed:8500694}.
MUTAGEN 417 417 A->I: Reduced catalytic activity. Alters
the stereoselectivity of the oxygenation
reaction. {ECO:0000269|PubMed:8500694}.
MUTAGEN 418 418 V->M: No effect on catalytic activity. No
effect on the stereoselectivity of the
oxygenation reaction.
{ECO:0000269|PubMed:8500694}.
MUTAGEN 540 540 H->Q: Complete loss of catalytic
activity. {ECO:0000269|PubMed:8500694}.
CONFLICT 189 192 RVYT -> PCLH (in Ref. 1; AAA51533).
{ECO:0000305}.
CONFLICT 345 345 S -> C (in Ref. 1; AAA51533).
{ECO:0000305}.
CONFLICT 389 389 L -> P (in Ref. 2; AAA60056).
{ECO:0000305}.
HELIX 182 195 {ECO:0000244|PDB:3D3L}.
STRAND 198 200 {ECO:0000244|PDB:3D3L}.
HELIX 203 207 {ECO:0000244|PDB:3D3L}.
HELIX 213 221 {ECO:0000244|PDB:3D3L}.
HELIX 225 234 {ECO:0000244|PDB:3D3L}.
HELIX 258 269 {ECO:0000244|PDB:3D3L}.
STRAND 273 277 {ECO:0000244|PDB:3D3L}.
HELIX 279 281 {ECO:0000244|PDB:3D3L}.
STRAND 300 305 {ECO:0000244|PDB:3D3L}.
STRAND 311 319 {ECO:0000244|PDB:3D3L}.
STRAND 325 327 {ECO:0000244|PDB:3D3L}.
HELIX 337 357 {ECO:0000244|PDB:3D3L}.
HELIX 358 364 {ECO:0000244|PDB:3D3L}.
HELIX 365 378 {ECO:0000244|PDB:3D3L}.
HELIX 384 389 {ECO:0000244|PDB:3D3L}.
HELIX 390 392 {ECO:0000244|PDB:3D3L}.
HELIX 426 434 {ECO:0000244|PDB:3D3L}.
TURN 438 441 {ECO:0000244|PDB:3D3L}.
HELIX 443 449 {ECO:0000244|PDB:3D3L}.
HELIX 459 482 {ECO:0000244|PDB:3D3L}.
HELIX 486 491 {ECO:0000244|PDB:3D3L}.
HELIX 493 503 {ECO:0000244|PDB:3D3L}.
TURN 504 508 {ECO:0000244|PDB:3D3L}.
HELIX 510 512 {ECO:0000244|PDB:3D3L}.
HELIX 522 536 {ECO:0000244|PDB:3D3L}.
HELIX 538 544 {ECO:0000244|PDB:3D3L}.
HELIX 547 551 {ECO:0000244|PDB:3D3L}.
HELIX 554 556 {ECO:0000244|PDB:3D3L}.
STRAND 567 571 {ECO:0000244|PDB:3D3L}.
HELIX 574 580 {ECO:0000244|PDB:3D3L}.
HELIX 584 597 {ECO:0000244|PDB:3D3L}.
HELIX 618 643 {ECO:0000244|PDB:3D3L}.
HELIX 654 656 {ECO:0000244|PDB:3D3L}.
STRAND 657 660 {ECO:0000244|PDB:3D3L}.
SEQUENCE 663 AA; 75694 MW; C4D6D5B320666A77 CRC64;
MGRYRIRVAT GAWLFSGSYN RVQLWLVGTR GEAELELQLR PARGEEEEFD HDVAEDLGLL
QFVRLRKHHW LVDDAWFCDR ITVQGPGACA EVAFPCYRWV QGEDILSLPE GTARLPGDNA
LDMFQKHREK ELKDRQQIYC WATWKEGLPL TIAADRKDDL PPNMRFHEEK RLDFEWTLKA
GALEMALKRV YTLLSSWNCL EDFDQIFWGQ KSALAEKVRQ CWQDDELFSY QFLNGANPML
LRRSTSLPSR LVLPSGMEEL QAQLEKELQN GSLFEADFIL LDGIPANVIR GEKQYLAAPL
VMLKMEPNGK LQPMVIQIQP PNPSSPTPTL FLPSDPPLAW LLAKSWVRNS DFQLHEIQYH
LLNTHLVAEV IAVATMRCLP GLHPIFKFLI PHIRYTMEIN TRARTQLISD GGIFDKAVST
GGGGHVQLLR RAAAQLTYCS LCPPDDLADR GLLGLPGALY AHDALRLWEI IARYVEGIVH
LFYQRDDIVK GDPELQAWCR EITEVGLCQA QDRGFPVSFQ SQSQLCHFLT MCVFTCTAQH
AAINQGQLDW YAWVPNAPCT MRMPPPTTKE DVTMATVMGS LPDVRQACLQ MAISWHLSRR
QPDMVPLGHH KEKYFSGPKP KAVLNQFRTD LEKLEKEITA RNEQLDWPYE YLKPSCIENS
VTI


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