LOXE3_RAT
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 03-AUG-2022, entry version 66.
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;
CC Evidence={ECO:0000255|PROSITE-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 PaxDb; D3ZKX9; -.
DR PRIDE; D3ZKX9; -.
DR Ensembl; ENSRNOT00000010141; ENSRNOP00000010141; ENSRNOG00000007454.
DR GeneID; 287424; -.
DR KEGG; rno:287424; -.
DR UCSC; RGD:1306252; rat.
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; LCEAFSM; -.
DR OrthoDB; 385042at2759; -.
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 tissues.
DR Genevisible; D3ZKX9; RN.
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 transferase activity, transferring hydroxy groups; 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: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 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; PTHR11771; 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; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
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
