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Arachidonate 15-lipoxygenase (15-LOX) (15-LOX-1) (EC 1.13.11.33) (12/15-lipoxygenase) (Arachidonate 12-lipoxygenase, leukocyte-type) (12-LOX) (EC 1.13.11.31) (Arachidonate omega-6 lipoxygenase)

 LOX15_HUMAN             Reviewed;         662 AA.
P16050; A8K2P4; B7ZA11; Q8N6R7; Q99657;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 177.
RecName: Full=Arachidonate 15-lipoxygenase;
Short=15-LOX;
Short=15-LOX-1;
EC=1.13.11.33 {ECO:0000269|PubMed:17052953, ECO:0000269|PubMed:1944593};
AltName: Full=12/15-lipoxygenase;
AltName: Full=Arachidonate 12-lipoxygenase, leukocyte-type;
Short=12-LOX;
EC=1.13.11.31 {ECO:0000269|PubMed:1944593};
AltName: Full=Arachidonate omega-6 lipoxygenase;
Name=ALOX15; Synonyms=LOG15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
PubMed=3202857; DOI=10.1016/S0006-291X(88)80271-7;
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].
PubMed=9224951; DOI=10.1016/S0167-4781(97)00005-5;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-90; LYS-103 AND
GLN-205.
SeattleSNPs variation discovery resource;
Submitted (DEC-2003) 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] (ISOFORM 1), AND VARIANT
PRO-461.
TISSUE=Brain, and Lung;
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 1-46.
PubMed=9700053; DOI=10.1023/A:1006813009006;
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).
[8]
PROTEIN SEQUENCE OF 2-16.
PubMed=3356688;
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).
[9]
PROTEIN SEQUENCE OF 2-31; 38-45; 157-168 AND 626-631.
TISSUE=Eosinophil, and Leukocyte;
PubMed=1662607; DOI=10.1111/j.1432-1033.1991.tb16495.x;
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).
[10]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF MET-418.
PubMed=1944593; DOI=10.1038/354149a0;
Sloane D.L., Leung R., Craik C.S., Sigal E.;
"A primary determinant for lipoxygenase positional specificity.";
Nature 354:149-152(1991).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9414270;
Brinckmann R., Schnurr K., Heydeck D., Rosenbach T., Kolde G.,
Kuehn H.;
"Membrane translocation of 15-lipoxygenase in hematopoietic cells is
calcium-dependent and activates the oxygenase activity of the
enzyme.";
Blood 91:64-74(1998).
[12]
SUBCELLULAR LOCATION.
PubMed=11418015; DOI=10.1054/plef.2001.0263;
Hsi L.C., Kamitani H., Cornicelli J.A., Eling T.E.;
"Evaluation of the activity and localization of 15-lipoxygenase-1
after introduction into human colorectal carcinoma Caco-2 cells.";
Prostaglandins Leukot. Essent. Fatty Acids 64:217-225(2001).
[13]
LIPID-BINDING, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, AND
ENZYME REGULATION.
PubMed=17052953; DOI=10.1016/j.bbalip.2006.09.007;
Andersson E., Schain F., Svedling M., Claesson H.E., Forsell P.K.;
"Interaction of human 15-lipoxygenase-1 with phosphatidylinositol
bisphosphates results in increased enzyme activity.";
Biochim. Biophys. Acta 1761:1498-1505(2006).
[14]
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).
[15]
SUBCELLULAR LOCATION.
PubMed=19528634; DOI=10.1194/jlr.M900081-JLR200;
Weibel G.L., Joshi M.R., Wei C., Bates S.R., Blair I.A.,
Rothblat G.H.;
"15(S)-Lipoxygenase-1 associates with neutral lipid droplets in
macrophage foam cells: evidence of lipid droplet metabolism.";
J. Lipid Res. 50:2371-2376(2009).
[16]
FUNCTION IN IL13 SIGNALING, INTERACTION WITH PEBP1, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=21831839; DOI=10.1073/pnas.1018075108;
Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B.,
Wenzel S.E.;
"15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding
protein to regulate MAPK signaling in human airway epithelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2011).
[17]
VARIANT MET-560, CHARACTERIZATION OF VARIANT MET-560, AND INVOLVEMENT
IN CORONARY ARTERY DISEASE.
PubMed=17959182; DOI=10.1016/j.atherosclerosis.2007.09.003;
Assimes T.L., Knowles J.W., Priest J.R., Basu A., Borchert A.,
Volcik K.A., Grove M.L., Tabor H.K., Southwick A., Tabibiazar R.,
Sidney S., Boerwinkle E., Go A.S., Iribarren C., Hlatky M.A.,
Fortmann S.P., Myers R.M., Kuhn H., Risch N., Quertermous T.;
"A near null variant of 12/15-LOX encoded by a novel SNP in ALOX15 and
the risk of coronary artery disease.";
Atherosclerosis 198:136-144(2008).
-!- 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. Converts arachidonic acid into 12-
hydroperoxyeicosatetraenoic acid/12-HPETE and 15-
hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic
acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-
hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin
A3. Probably plays an important role in the immune and
inflammatory responses. Through the oxygenation of membrane-bound
phosphatidylethanolamine in macrophages may favor clearance of
apoptotic cells during inflammation by resident macrophages and
prevent an autoimmune response associated with the clearance of
apoptotic cells by inflammatory monocytes. In parallel, may
regulate actin polymerization which is crucial for several
biological processes, including macrophage function. May also
regulate macrophage function through regulation of the peroxisome
proliferator activated receptor signaling pathway. Finally, it is
also involved in the cellular response to IL13/interleukin-13. In
addition to its role in the immune and inflammatory responses, may
play a role in epithelial wound healing in the cornea maybe
through production of lipoxin A4. May also play a role in
endoplasmic reticulum stress response and the regulation of bone
mass. {ECO:0000269|PubMed:17052953, ECO:0000269|PubMed:21831839}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-
12-hydroperoxyicosa-5,8,10,14-tetraenoate.
{ECO:0000269|PubMed:1944593}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-
15-hydroperoxyicosa-5,8,11,13-tetraenoate.
{ECO:0000269|PubMed:17052953, ECO:0000269|PubMed:1944593}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00726};
-!- ENZYME REGULATION: Activity is increased by binding
phosphatidylinositol phosphates, especially phosphatidylinositol
3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate.
{ECO:0000269|PubMed:17052953}.
-!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
biosynthesis.
-!- SUBUNIT: Interacts with PEBP1; in response to IL13/interleukin-13,
prevents the interaction of PEBP1 with RAF1 to activate the ERK
signaling cascade. {ECO:0000269|PubMed:21831839}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane;
Peripheral membrane protein. Lipid droplet. Note=Predominantly
cytosolic; becomes enriched at membranes upon calcium binding.
Translocates from the cytosol to the plasma membrane when
stimulated by IL13/interleukin-13 and in macrophages binding
apoptotic cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P16050-1; Sequence=Displayed;
Name=2;
IsoId=P16050-2; Sequence=VSP_056681;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in monocytes and eosinophils (at
protein level). Expressed in airway epithelial cells.
{ECO:0000269|PubMed:21831839, ECO:0000269|PubMed:9414270}.
-!- INDUCTION: Up-regulated by UV-irradiation.
{ECO:0000269|PubMed:18755188}.
-!- DOMAIN: The PLAT domain can bind calcium ions; this promotes
association with membranes. {ECO:0000250}.
-!- DISEASE: Note=Disease susceptibility may be associated with
variations affecting the gene represented in this entry. Met at
position 560 may confer interindividual susceptibility to coronary
artery disease (CAD) (PubMed:17959182).
{ECO:0000269|PubMed:17959182}.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
-!- 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/";
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EMBL; M23892; AAA36182.1; -; mRNA.
EMBL; U88317; AAB49305.1; -; Genomic_DNA.
EMBL; AK290309; BAF82998.1; -; mRNA.
EMBL; AK316126; BAH14497.1; -; mRNA.
EMBL; AY505111; AAR84235.1; -; Genomic_DNA.
EMBL; AC118754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC029032; AAH29032.1; -; mRNA.
EMBL; U63384; AAC52118.1; -; Genomic_DNA.
CCDS; CCDS11049.1; -. [P16050-1]
PIR; A31349; A31349.
RefSeq; NP_001131.3; NM_001140.3. [P16050-1]
UniGene; Hs.73809; -.
PDB; 2ABT; Model; -; A=2-662.
PDBsum; 2ABT; -.
ProteinModelPortal; P16050; -.
SMR; P16050; -.
BioGrid; 106747; 4.
DIP; DIP-60388N; -.
IntAct; P16050; 1.
STRING; 9606.ENSP00000293761; -.
BindingDB; P16050; -.
ChEMBL; CHEMBL2903; -.
DrugBank; DB08492; (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID.
GuidetoPHARMACOLOGY; 1388; -.
SwissLipids; SLP:000000667; -.
iPTMnet; P16050; -.
PhosphoSitePlus; P16050; -.
BioMuta; ALOX15; -.
DMDM; 126396; -.
PaxDb; P16050; -.
PeptideAtlas; P16050; -.
PRIDE; P16050; -.
Ensembl; ENST00000293761; ENSP00000293761; ENSG00000161905. [P16050-1]
Ensembl; ENST00000570836; ENSP00000458832; ENSG00000161905. [P16050-1]
Ensembl; ENST00000574640; ENSP00000460483; ENSG00000161905. [P16050-2]
GeneID; 246; -.
KEGG; hsa:246; -.
UCSC; uc002fyh.4; human. [P16050-1]
CTD; 246; -.
DisGeNET; 246; -.
GeneCards; ALOX15; -.
HGNC; HGNC:433; ALOX15.
HPA; CAB004962; -.
HPA; CAB004963; -.
HPA; HPA013859; -.
MIM; 152392; gene.
neXtProt; NX_P16050; -.
OpenTargets; ENSG00000161905; -.
PharmGKB; PA48; -.
eggNOG; ENOG410IKAN; Eukaryota.
eggNOG; ENOG410YN4N; LUCA.
GeneTree; ENSGT00550000074415; -.
HOVERGEN; HBG005150; -.
InParanoid; P16050; -.
KO; K00460; -.
OMA; LTCWKDL; -.
OrthoDB; EOG091G04A4; -.
PhylomeDB; P16050; -.
TreeFam; TF105320; -.
BioCyc; MetaCyc:HS08621-MONOMER; -.
BRENDA; 1.13.11.33; 2681.
Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-HSA-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-HSA-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SABIO-RK; P16050; -.
UniPathway; UPA00881; -.
GeneWiki; ALOX15; -.
GenomeRNAi; 246; -.
PRO; PR:P16050; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000161905; -.
CleanEx; HS_ALOX15; -.
ExpressionAtlas; P16050; baseline and differential.
Genevisible; P16050; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IDA:UniProtKB.
GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; IDA:UniProtKB.
GO; GO:0097260; F:eoxin A4 synthase activity; TAS:Reactome.
GO; GO:0051120; F:hepoxilin A3 synthase activity; IEA:Ensembl.
GO; GO:0047977; F:hepoxilin-epoxide hydrolase activity; IEA:Ensembl.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB.
GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0035963; P:cellular response to interleukin-13; IMP:UniProtKB.
GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
GO; GO:2001303; P:lipoxin A4 biosynthetic process; ISS:UniProtKB.
GO; GO:0019372; P:lipoxygenase pathway; IDA:UniProtKB.
GO; GO:0002820; P:negative regulation of adaptive immune response; ISS:UniProtKB.
GO; GO:0001503; P:ossification; ISS:UniProtKB.
GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
GO; GO:1901074; P:regulation of engulfment of apoptotic cell; ISS:UniProtKB.
GO; GO:0035358; P:regulation of peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; ISS:UniProtKB.
Gene3D; 2.60.60.20; -; 1.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR020834; LipOase_CS.
InterPro; IPR020833; LipOase_Fe_BS.
InterPro; IPR001885; LipOase_mml.
InterPro; IPR001024; PLAT/LH2_dom.
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; Alternative splicing; Calcium; Cell membrane;
Complete proteome; Cytoplasm; Dioxygenase; Direct protein sequencing;
Fatty acid metabolism; Iron; Lipid droplet; Lipid metabolism;
Lipid-binding; Membrane; Metal-binding; Oxidoreductase; Polymorphism;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1662607,
ECO:0000269|PubMed:3356688}.
CHAIN 2 662 Arachidonate 15-lipoxygenase.
/FTId=PRO_0000220697.
DOMAIN 2 114 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
DOMAIN 115 662 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 360 360 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 365 365 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 540 540 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 544 544 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 662 662 Iron; via carboxylate; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00726}.
VAR_SEQ 46 84 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056681.
VARIANT 90 90 D -> H (in dbSNP:rs11568142).
{ECO:0000269|Ref.4}.
/FTId=VAR_018746.
VARIANT 102 102 G -> V (in dbSNP:rs41439950).
/FTId=VAR_035036.
VARIANT 103 103 N -> K (in dbSNP:rs11568099).
{ECO:0000269|Ref.4}.
/FTId=VAR_018747.
VARIANT 205 205 R -> Q (in dbSNP:rs11568101).
{ECO:0000269|Ref.4}.
/FTId=VAR_018748.
VARIANT 239 239 V -> M (in dbSNP:rs3892408).
/FTId=VAR_035037.
VARIANT 461 461 A -> P (in dbSNP:rs17852628).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_035038.
VARIANT 560 560 T -> M (loss of catalytic activity;
dbSNP:rs34210653).
{ECO:0000269|PubMed:17959182}.
/FTId=VAR_035039.
MUTAGEN 418 418 M->V: Catalyzes 15- and 12-
lipoxygenation.
{ECO:0000269|PubMed:1944593}.
CONFLICT 46 46 E -> V (in Ref. 7; AAC52118).
{ECO:0000305}.
SEQUENCE 662 AA; 74804 MW; 9ACF7FE7863A045C CRC64;
MGLYRIRVST GASLYAGSNN QVQLWLVGQH GEAALGKRLW PARGKETELK VEVPEYLGPL
LFVKLRKRHL LKDDAWFCNW ISVQGPGAGD EVRFPCYRWV EGNGVLSLPE GTGRTVGEDP
QGLFQKHREE ELEERRKLYR WGNWKDGLIL NMAGAKLYDL PVDERFLEDK RVDFEVSLAK
GLADLAIKDS LNVLTCWKDL DDFNRIFWCG QSKLAERVRD SWKEDALFGY QFLNGANPVV
LRRSAHLPAR LVFPPGMEEL QAQLEKELEG GTLFEADFSL LDGIKANVIL CSQQHLAAPL
VMLKLQPDGK LLPMVIQLQL PRTGSPPPPL FLPTDPPMAW LLAKCWVRSS DFQLHELQSH
LLRGHLMAEV IVVATMRCLP SIHPIFKLII PHLRYTLEIN VRARTGLVSD MGIFDQIMST
GGGGHVQLLK QAGAFLTYSS FCPPDDLADR GLLGVKSSFY AQDALRLWEI IYRYVEGIVS
LHYKTDVAVK DDPELQTWCR EITEIGLQGA QDRGFPVSLQ ARDQVCHFVT MCIFTCTGQH
ASVHLGQLDW YSWVPNAPCT MRLPPPTTKD ATLETVMATL PNFHQASLQM SITWQLGRRQ
PVMVAVGQHE EEYFSGPEPK AVLKKFREEL AALDKEIEIR NAKLDMPYEY LRPSVVENSV
AI


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