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Arachidonate 15-lipoxygenase (15-LOX) (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_RAT               Reviewed;         663 AA.
Q02759; F1MA51;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
16-OCT-2013, sequence version 3.
30-AUG-2017, entry version 139.
RecName: Full=Arachidonate 15-lipoxygenase;
Short=15-LOX;
EC=1.13.11.33 {ECO:0000269|PubMed:8117750, ECO:0000269|PubMed:8444196};
AltName: Full=12/15-lipoxygenase;
AltName: Full=Arachidonate 12-lipoxygenase, leukocyte-type {ECO:0000303|PubMed:8117750};
Short=12-LOX;
EC=1.13.11.31 {ECO:0000269|PubMed:8117750, ECO:0000269|PubMed:8444196};
AltName: Full=Arachidonate omega-6 lipoxygenase;
Name=Alox15; Synonyms=Alox12l;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=8444196; DOI=10.1111/j.1432-1033.1993.tb17699.x;
Watanabe T., Medina J.F., Haeggstroem J.Z., Raadmark O.P.,
Samuelsson B.;
"Molecular cloning of a 12-lipoxygenase cDNA from rat brain.";
Eur. J. Biochem. 212:605-612(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
SUBCELLULAR LOCATION.
TISSUE=Pineal gland;
PubMed=8117750; DOI=10.1016/0005-2760(94)90272-0;
Hada T., Hagiya H., Suzuki H., Arakawa T., Nakamura M., Matsuda S.,
Yoshimoto T., Yamamoto S., Azekawa T., Morita Y., Ishimura K.,
Kim H.Y.;
"Arachidonate 12-lipoxygenase of rat pineal glands: catalytic
properties and primary structure deduced from its cDNA.";
Biochim. Biophys. Acta 1211:221-228(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[4]
FUNCTION IN HEPOXILIN A3 SYNTHESIS.
PubMed=15123652; DOI=10.1074/jbc.M307576200;
Nigam S., Patabhiraman S., Ciccoli R., Ishdorj G., Schwarz K.,
Petrucev B., Kuehn H., Haeggstroem J.Z.;
"The rat leukocyte-type 12-lipoxygenase exhibits an intrinsic
hepoxilin A3 synthase activity.";
J. Biol. Chem. 279:29023-29030(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
FUNCTION.
PubMed=23382512; DOI=10.1096/fj.12-217414;
Gregus A.M., Dumlao D.S., Wei S.C., Norris P.C., Catella L.C.,
Meyerstein F.G., Buczynski M.W., Steinauer J.J., Fitzsimmons B.L.,
Yaksh T.L., Dennis E.A.;
"Systematic analysis of rat 12/15-lipoxygenase enzymes reveals
critical role for spinal eLOX3 hepoxilin synthase activity in
inflammatory hyperalgesia.";
FASEB J. 27:1939-1949(2013).
-!- 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:15123652, ECO:0000269|PubMed:23382512,
ECO:0000269|PubMed:8117750, ECO:0000269|PubMed:8444196}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-
12-hydroperoxyicosa-5,8,10,14-tetraenoate.
{ECO:0000269|PubMed:8117750, ECO:0000269|PubMed:8444196}.
-!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-
15-hydroperoxyicosa-5,8,11,13-tetraenoate.
{ECO:0000269|PubMed:8117750, ECO:0000269|PubMed:8444196}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Note=Binds 1 Fe cation per subunit.;
-!- 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:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:8117750}. Cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Lipid droplet
{ECO:0000250}. 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 (By similarity).
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in leukocytes, lung and aorta.
{ECO:0000269|PubMed:8444196}.
-!- DOMAIN: The PLAT domain can bind calcium ions; this promotes
association with membranes. {ECO:0000250}.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L06040; AAA41532.1; -; mRNA.
EMBL; S69383; AAB30132.1; -; mRNA.
EMBL; AABR06064408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; I52462; I52462.
PIR; S30051; S30051.
RefSeq; NP_112272.2; NM_031010.2.
UniGene; Rn.11318; -.
SMR; Q02759; -.
IntAct; Q02759; 1.
STRING; 10116.ENSRNOP00000026038; -.
BindingDB; Q02759; -.
ChEMBL; CHEMBL2741; -.
SwissLipids; SLP:000001609; -.
iPTMnet; Q02759; -.
PhosphoSitePlus; Q02759; -.
PaxDb; Q02759; -.
PRIDE; Q02759; -.
Ensembl; ENSRNOT00000026038; ENSRNOP00000026038; ENSRNOG00000019183.
GeneID; 81639; -.
KEGG; rno:81639; -.
UCSC; RGD:70493; rat.
CTD; 246; -.
RGD; 70493; Alox15.
eggNOG; ENOG410IKAN; Eukaryota.
eggNOG; ENOG410YN4N; LUCA.
GeneTree; ENSGT00550000074415; -.
HOGENOM; HOG000234358; -.
HOVERGEN; HBG005150; -.
InParanoid; Q02759; -.
KO; K00460; -.
OMA; LTCWKDL; -.
OrthoDB; EOG091G04A4; -.
TreeFam; TF105320; -.
BRENDA; 1.13.11.31; 5301.
Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-RNO-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-RNO-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathway; UPA00881; -.
PRO; PR:Q02759; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000019183; -.
Genevisible; Q02759; RN.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
GO; GO:0005811; C:lipid particle; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IDA:RGD.
GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; IDA:RGD.
GO; GO:0051120; F:hepoxilin A3 synthase activity; IDA:RGD.
GO; GO:0047977; F:hepoxilin-epoxide hydrolase activity; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
GO; GO:0019870; F:potassium channel inhibitor activity; TAS: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; ISS:UniProtKB.
GO; GO:0035963; P:cellular response to interleukin-13; ISS:UniProtKB.
GO; GO:0019395; P:fatty acid oxidation; ISS:UniProtKB.
GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB.
GO; GO:0046456; P:icosanoid biosynthetic process; NAS:UniProtKB.
GO; GO:2001303; P:lipoxin A4 biosynthetic process; ISS:UniProtKB.
GO; GO:0019372; P:lipoxygenase pathway; IDA:RGD.
GO; GO:0002820; P:negative regulation of adaptive immune response; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0045794; P:negative regulation of cell volume; TAS: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:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IMP:RGD.
GO; GO:1901074; P:regulation of engulfment of apoptotic cell; ISS:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; TAS: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;
Calcium; Cell membrane; Complete proteome; Cytoplasm; Dioxygenase;
Fatty acid metabolism; Iron; Lipid droplet; Lipid metabolism;
Lipid-binding; Membrane; Metal-binding; Oxidoreductase;
Phosphoprotein; Reference proteome.
CHAIN 1 663 Arachidonate 15-lipoxygenase.
/FTId=PRO_0000220687.
DOMAIN 2 115 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
DOMAIN 116 663 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 361 361 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 366 366 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 541 541 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 545 545 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 663 663 Iron; via carboxylate; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00726}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 55 55 E -> G (in Ref. 2; AAB30132).
{ECO:0000305}.
CONFLICT 371 371 V -> L (in Ref. 1; AAA41532).
{ECO:0000305}.
SEQUENCE 663 AA; 75378 MW; C732D3EB22CA0411 CRC64;
MGVYRIRVST GDSKYAGSNN EVYLWLVGQH GEASLGKLLR PCRDSEAEFK VDVSEYLGPL
LFVRVQKWHY LTDDAWFCNW ISVKGPGDQG SEYMFPCYRW VQGRSILSLP EGTGCTVVED
SQGLFRKHRE EELEERRSLY RWGNWKDGSI LNVAAASISD LPVDQRFRED KRIEFEASQV
IGVMDTVVNF PINTVTCWKS LDDFNCVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM
VLKRSTCLPA RLVFPPGMEK LQAQLNKELQ KGTLFEADFF LLDGIKANVI LCSQQYLAAP
LVMLKLMPDG QLLPIAIQLE LPKTGSTPPP IFTPSDPPMD WLLAKCWVRS SDLQLHELQA
HLLRGHLMAE VFAVATMRCL PSVHPVFKLL VPHLLYTMEI NVRARSDLIS ERGFFDKAMS
TGGGGHLDLL KQAGAFLTYC SLCPPDDLAE RGLLDIETCF YAKDALRLWQ IMNRYVVGMF
NLHYKTDKAV QDDYELQSWC REITDIGLQG AQDRGFPTSL QSRAQACYFI TMCIFTCTAQ
HSSVHLGQLD WFYWVPNAPC TMRLPPPTTK EATMEKLMAT LPNPNQSTLQ INVVWLLGRR
QAVMVPLGQH SEEHFPNPEA KAVLKKFREE LAALDKEIEI RNKSLDIPYE YLRPSMVENS
VAI


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