ID   LOXE3_RAT               Reviewed;         711 AA.
AC   D3ZKX9;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Hydroperoxide isomerase ALOXE3 {ECO:0000305};
DE   AltName: Full=Epidermis-type lipoxygenase 3 {ECO:0000250|UniProtKB:Q9WV07};
DE            Short=Epidermal LOX-3;
DE            Short=e-LOX-3 {ECO:0000250|UniProtKB:Q9WV07};
DE            Short=eLOX-3;
DE   AltName: Full=Hydroperoxy dehydratase ALOXE3 {ECO:0000305};
DE   AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE            EC=4.2.1.152 {ECO:0000250|UniProtKB:Q9WV07};
DE   AltName: Full=Hydroperoxy icosatetraenoate isomerase;
DE            EC=5.4.4.7 {ECO:0000250|UniProtKB:Q9WV07};
GN   Name=Aloxe3 {ECO:0000312|RGD:1306252};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION IN ALGESIA.
RX   PubMed=23382512; DOI=10.1096/fj.12-217414;
RA   Gregus A.M., Dumlao D.S., Wei S.C., Norris P.C., Catella L.C.,
RA   Meyerstein F.G., Buczynski M.W., Steinauer J.J., Fitzsimmons B.L.,
RA   Yaksh T.L., Dennis E.A.;
RT   "Systematic analysis of rat 12/15-lipoxygenase enzymes reveals critical
RT   role for spinal eLOX3 hepoxilin synthase activity in inflammatory
RT   hyperalgesia.";
RL   FASEB J. 27:1939-1949(2013).
CC   -!- FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in
CC       that it displays a prominent hydroperoxide isomerase activity and a
CC       reduced lipoxygenases activity. The hydroperoxide isomerase activity
CC       catalyzes the isomerization of hydroperoxides, derived from arachidonic
CC       and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and
CC       ketones. In presence of oxygen, oxygenates polyunsaturated fatty acids,
CC       including arachidonic acid, to produce fatty acid hydroperoxides. In
CC       the skin, acts downstream of ALOX12B on the linoleate moiety of
CC       esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an
CC       epoxy-ketone derivative, a crucial step in the conjugation of omega-
CC       hydroxyceramide to membrane proteins. Therefore plays a crucial role in
CC       the synthesis of corneocytes lipid envelope and the establishment of
CC       the skin barrier to water loss. In parallel, it may have a signaling
CC       function in barrier formation through the production of hepoxilins
CC       metabolites (By similarity). Also plays a role in adipocyte
CC       differentiation through hepoxilin A3 and hepoxilin B3 production which
CC       in turn activate PPARG (By similarity). Through the production of
CC       hepoxilins in the spinal cord, it may regulate inflammatory tactile
CC       allodynia (PubMed:23382512). {ECO:0000250|UniProtKB:Q9BYJ1,
CC       ECO:0000250|UniProtKB:Q9WV07, ECO:0000269|PubMed:23382512}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxyeicosatetraenoate = a hydroxy-epoxy-
CC         eicosatetraenoate; Xref=Rhea:RHEA:55560, ChEBI:CHEBI:59720,
CC         ChEBI:CHEBI:137328; EC=5.4.4.7;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55561;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxyeicosatetraenoate = an oxoeicosatetraenoate +
CC         H2O; Xref=Rhea:RHEA:55556, ChEBI:CHEBI:15377, ChEBI:CHEBI:59720,
CC         ChEBI:CHEBI:131859; EC=4.2.1.152;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55557;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8R)-
CC         hydroxy-(11R,12R)-epoxy-(5Z,9E,14Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:37939, ChEBI:CHEBI:75230, ChEBI:CHEBI:75232;
CC         EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37940;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8R)-
CC         hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:37955, ChEBI:CHEBI:57444, ChEBI:CHEBI:75233;
CC         EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37956;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (10R)-
CC         hydroxy-(11S,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:37951, ChEBI:CHEBI:57444, ChEBI:CHEBI:75234;
CC         EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37952;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = (13R)-
CC         hydroxy-(14S,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:37959, ChEBI:CHEBI:57446, ChEBI:CHEBI:75235;
CC         EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37960;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 7R-
CC         hydroxy-5S,6S-epoxy-(8Z,11Z,14Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:41251, ChEBI:CHEBI:57450, ChEBI:CHEBI:77919;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41252;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 11-hydroxy-
CC         (12S,13S)-epoxy-(9Z)-octadecenoate; Xref=Rhea:RHEA:50212,
CC         ChEBI:CHEBI:57466, ChEBI:CHEBI:132064;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50213;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-[omega-(9R)-hydroperoxy-(10E,12Z)-octadecadienoyloxy]acyl-
CC         beta-D-glucosyl-(1<->1)-octadecasphing-4E-enine = N-[omega-(9R,10R)-
CC         epoxy-(13R)-hydroxy-(11E)-octadecadienoyloxy]acyl-beta-D-glucosyl-
CC         (1<->1)-octadecasphing-4E-enine; Xref=Rhea:RHEA:40503,
CC         ChEBI:CHEBI:134624, ChEBI:CHEBI:134626;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40504;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acyl (9R)-hydroperoxy-(10E,12Z)-octadecadienoate
CC         octadecasphing-4E-enine = N-acyl-(9R,10R)-epoxy-(13R)-hydroxy-(11E)-
CC         octadecenoate (4E)-octadecasphin-4-enine; Xref=Rhea:RHEA:41243,
CC         ChEBI:CHEBI:77889, ChEBI:CHEBI:77891;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41244;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-
CC         (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37943,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:75230, ChEBI:CHEBI:75231;
CC         EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37944;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-
CC         (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231;
CC         EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-
CC         (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-
CC         octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57466, ChEBI:CHEBI:90781;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYJ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = (10R)-
CC         hydroxy-(8S,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:37931, ChEBI:CHEBI:75322, ChEBI:CHEBI:75327;
CC         EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9WV07};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37932;
CC         Evidence={ECO:0000250|UniProtKB:Q9WV07};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8-oxo-
CC         (5Z,9E,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37935,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57447, ChEBI:CHEBI:75326;
CC         EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9WV07};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37936;
CC         Evidence={ECO:0000250|UniProtKB:Q9WV07};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8-oxo-
CC         (5Z,9E,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37927,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:75322, ChEBI:CHEBI:75326;
CC         EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q9WV07};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37928;
CC         Evidence={ECO:0000250|UniProtKB:Q9WV07};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00726};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00726};
CC   -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
CC       biosynthesis. {ECO:0000250|UniProtKB:Q9BYJ1}.
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000250|UniProtKB:Q9BYJ1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=about water - Issue 153 of
CC       September 2013;
CC       URL="https://web.expasy.org/spotlight/back_issues/153/";
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DR   EMBL; AABR06064371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473948; EDM04845.1; -; Genomic_DNA.
DR   RefSeq; NP_001099263.1; NM_001105793.1.
DR   AlphaFoldDB; D3ZKX9; -.
DR   SMR; D3ZKX9; -.
DR   STRING; 10116.ENSRNOP00000010141; -.
DR   PhosphoSitePlus; D3ZKX9; -.
DR   PaxDb; 10116-ENSRNOP00000010141; -.
DR   Ensembl; ENSRNOT00000010141.8; ENSRNOP00000010141.4; ENSRNOG00000007454.8.
DR   Ensembl; ENSRNOT00055056381; ENSRNOP00055046487; ENSRNOG00055032634.
DR   Ensembl; ENSRNOT00060035249; ENSRNOP00060028978; ENSRNOG00060020365.
DR   Ensembl; ENSRNOT00065044734; ENSRNOP00065036630; ENSRNOG00065025961.
DR   GeneID; 287424; -.
DR   KEGG; rno:287424; -.
DR   UCSC; RGD:1306252; rat.
DR   AGR; RGD:1306252; -.
DR   CTD; 59344; -.
DR   RGD; 1306252; Aloxe3.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   GeneTree; ENSGT00940000156796; -.
DR   HOGENOM; CLU_004282_3_3_1; -.
DR   InParanoid; D3ZKX9; -.
DR   OMA; FWCHKTV; -.
DR   OrthoDB; 999249at2759; -.
DR   PhylomeDB; D3ZKX9; -.
DR   TreeFam; TF105320; -.
DR   Reactome; R-RNO-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR   UniPathway; UPA00222; -.
DR   UniPathway; UPA00881; -.
DR   PRO; PR:D3ZKX9; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Proteomes; UP000234681; Chromosome 10.
DR   Bgee; ENSRNOG00000007454; Expressed in esophagus and 11 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051120; F:hepoxilin A3 synthase activity; ISS:UniProtKB.
DR   GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106255; F:hydroperoxy icosatetraenoate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050486; F:intramolecular hydroxytransferase activity; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; ISS:UniProtKB.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0046513; P:ceramide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR   GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0043651; P:linoleic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR   GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR   GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR   GO; GO:0006665; P:sphingolipid metabolic process; ISS:UniProtKB.
DR   CDD; cd01753; PLAT_LOX; 1.
DR   Gene3D; 3.10.450.60; -; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR000907; LipOase.
DR   InterPro; IPR013819; LipOase_C.
DR   InterPro; IPR036226; LipOase_C_sf.
DR   InterPro; IPR020834; LipOase_CS.
DR   InterPro; IPR020833; LipOase_Fe_BS.
DR   InterPro; IPR001885; LipOase_mml.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR042062; PLAT_LOX_verte.
DR   PANTHER; PTHR11771:SF184; HYDROPEROXIDE ISOMERASE ALOXE3; 1.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PRINTS; PR00087; LIPOXYGENASE.
DR   PRINTS; PR00467; MAMLPOXGNASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   Genevisible; D3ZKX9; RN.
PE   1: Evidence at protein level;
KW   Cytoplasm; Dioxygenase; Fatty acid metabolism; Iron; Isomerase;
KW   Lipid metabolism; Lyase; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..711
FT                   /note="Hydroperoxide isomerase ALOXE3"
FT                   /id="PRO_0000423419"
FT   DOMAIN          2..119
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DOMAIN          119..711
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         408
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         413
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         588
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         592
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         711
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ   SEQUENCE   711 AA;  80440 MW;  41C3D9BBC6C4532B CRC64;
     MAVYRLCVTT GSYLKAGTLD NIYATLVGTC GESPKQKLDR VGRDFATGSV QKYKVRCASE
     LGEILLLRLH KERFAFFCKD PWYCSRICVT TPDGSVVHFP CYQWIDGYCT VELRPGTART
     ICQDALPLLL DHRKRELQAR QECYRWKIYA PGFPRMVDVS SFEEMESDKK FALTKTAPCA
     DQDDNSGNRY LPGFPMKVDI PSLLHMEPNI RYSATKTASL IFNALPASLG MKIRGLLDRK
     GSWKRLDDIR NIFWCHKTFT SEYVTEHWCE DSFFGYQYLN GVNPIMLHCL SSLPSKLPVT
     NDMVAPLLGP GTCLQTELER GHIFLADYWI LAEAPVHCLN GRQQYVTAPL CLLWLNPQGV
     LLPLAIQLSQ IPGPESPIFL PTDCELDWLL AKTWVRNSEF LVHENNTHFL CTHLLCEAFS
     MATLRQLPLC HPVYKLLLPH TRYTLQVNTI ARATLLNPDG LVDKVTSIGR RGLIYLMSTG
     LAHFTYTDFC LPDSLRARGV LTIPNYHYRD DGLKIWAAIE RFVSEIVSYY YPNDACVQQD
     SELQAWVGEI FAQAFLGRES SGFPSRLCTP GELVKYLTAI IFNCSAQHAA VNSGQHDFGA
     WMPNAPSSMR QPPPQTKGNT TMESYLETLP EVNTTCSNLL LFWLVSQEPK DQRPLGTYPD
     EHFTEEAPRQ SIAAFQKCLA QISKDIRARN ESLALPYAYL DPPLIENSVS I
//