LX12B_MOUSE
ID LX12B_MOUSE Reviewed; 701 AA.
AC O70582;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Arachidonate 12-lipoxygenase, 12R-type {ECO:0000305};
DE Short=12R-LOX;
DE Short=12R-lipoxygenase;
DE EC=1.13.11.- {ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665};
DE AltName: Full=Epidermis-type lipoxygenase 12;
DE AltName: Full=Epidermis-type lipoxygenase 2;
DE Short=e-LOX 2;
GN Name=Alox12b {ECO:0000312|MGI:MGI:1274782}; Synonyms=Aloxe2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=NMRI; TISSUE=Epidermis;
RX PubMed=9518531; DOI=10.1016/s0005-2760(97)00214-2;
RA Krieg P., Kinzig A., Heidt M., Marks F., Fuerstenberger G.;
RT "cDNA cloning of a 8-lipoxygenase and a novel epidermis-type lipoxygenase
RT from phorbol ester-treated mouse skin.";
RL Biochim. Biophys. Acta 1391:7-12(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6 X SJL;
RX PubMed=9837935; DOI=10.1074/jbc.273.50.33540;
RA Sun D., McDonnell M., Chen X.-S., Lakkis M.M., Li H., Isaacs S.N.,
RA Elsea S.H., Patel P.I., Funk C.D.;
RT "Human 12(R)-lipoxygenase and the mouse ortholog. Molecular cloning,
RT expression, and gene chromosomal assignment.";
RL J. Biol. Chem. 273:33540-33547(1998).
RN [3]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10100631; DOI=10.1016/s0014-5793(99)00196-9;
RA Krieg P., Siebert M., Kinzig A., Bettenhausen R., Marks F.,
RA Fuerstenberger G.;
RT "Murine 12(R)-lipoxygenase: functional expression, genomic structure and
RT chromosomal localization.";
RL FEBS Lett. 446:142-148(1999).
RN [4]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=11256953; DOI=10.1042/0264-6021:3550097;
RA Siebert M., Krieg P., Lehmann W.D., Marks F., Fuerstenberger G.;
RT "Enzymic characterization of epidermis-derived 12-lipoxygenase
RT isoenzymes.";
RL Biochem. J. 355:97-104(2001).
RN [5]
RP FUNCTION IN ARACHIDONATE METABOLISM, CATALYTIC ACTIVITY, REACTION
RP MECHANISM, PATHWAY, AND MUTAGENESIS OF PHE-390; GLY-441; ALA-455 AND
RP VAL-631.
RX PubMed=16129665; DOI=10.1074/jbc.m508260200;
RA Meruvu S., Walther M., Ivanov I., Hammarstroem S., Fuerstenberger G.,
RA Krieg P., Reddanna P., Kuhn H.;
RT "Sequence determinants for the reaction specificity of murine (12R)-
RT lipoxygenase: targeted substrate modification and site-directed
RT mutagenesis.";
RL J. Biol. Chem. 280:36633-36641(2005).
RN [6]
RP FUNCTION IN SKIN BARRIER, AND DISRUPTION PHENOTYPE.
RX PubMed=17403930; DOI=10.1083/jcb.200612116;
RA Epp N., Fuerstenberger G., Mueller K., de Juanes S., Leitges M.,
RA Hausser I., Thieme F., Liebisch G., Schmitz G., Krieg P.;
RT "12R-lipoxygenase deficiency disrupts epidermal barrier function.";
RL J. Cell Biol. 177:173-182(2007).
RN [7]
RP FUNCTION IN SKIN BARRIER, AND PATHWAY.
RX PubMed=17429434; DOI=10.1038/sj.jid.5700825;
RA Moran J.L., Qiu H., Turbe-Doan A., Yun Y., Boeglin W.E., Brash A.R.,
RA Beier D.R.;
RT "A mouse mutation in the 12R-lipoxygenase, Alox12b, disrupts formation of
RT the epidermal permeability barrier.";
RL J. Invest. Dermatol. 127:1893-1897(2007).
RN [8]
RP FUNCTION IN SKIN BARRIER, AND DISRUPTION PHENOTYPE.
RX PubMed=21558561; DOI=10.1074/jbc.m111.251496;
RA Zheng Y., Yin H., Boeglin W.E., Elias P.M., Crumrine D., Beier D.R.,
RA Brash A.R.;
RT "Lipoxygenases mediate the effect of essential fatty acid in skin barrier
RT formation: a proposed role in releasing omega-hydroxyceramide for
RT construction of the corneocyte lipid envelope.";
RL J. Biol. Chem. 286:24046-24056(2011).
CC -!- FUNCTION: Catalyzes the regio and stereo-specific incorporation of a
CC single molecule of dioxygen into free and esterified polyunsaturated
CC fatty acids generating lipid hydroperoxides that can be further reduced
CC to the corresponding hydroxy species (PubMed:16129665). Does not
CC convert arachidonic acid to (12R)-hydroperoxyeicosatetraenoic
CC acid/(12R)-HPETE (PubMed:10100631, PubMed:11256953). In the skin, acts
CC upstream of ALOXE3 on the lineolate moiety of esterified omega-
CC hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone
CC derivative, a crucial step in the conjugation of omega-hydroxyceramide
CC to membrane proteins. Therefore plays a crucial role in the synthesis
CC of corneocytes lipid envelope and the establishment of the skin barrier
CC to water loss (PubMed:17403930, PubMed:17429434, PubMed:21558561). May
CC also play a role in the regulation of the expression of airway mucins
CC (By similarity). {ECO:0000250|UniProtKB:O75342,
CC ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953,
CC ECO:0000269|PubMed:16129665, ECO:0000269|PubMed:17403930,
CC ECO:0000269|PubMed:17429434, ECO:0000269|PubMed:21558561}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl
CC (5Z,8Z,10E,12R,14Z)-hydroperoxyiecosatetraenoate;
CC Xref=Rhea:RHEA:41311, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033,
CC ChEBI:CHEBI:78034; Evidence={ECO:0000269|PubMed:10100631,
CC ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41312;
CC Evidence={ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-
CC methyl-8-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate;
CC Xref=Rhea:RHEA:43480, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033,
CC ChEBI:CHEBI:83344; Evidence={ECO:0000269|PubMed:10100631};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43481;
CC Evidence={ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12R)-hydroperoxy-
CC (5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:41336,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:75230;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41337;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-[omega-(9Z,12Z)-octadecadienoyloxy]acyl-beta-D-glucosyl-
CC (1<->1)-octadecasphing-4E-enine + O2 = N-[omega-(9R)-hydroperoxy-
CC (10E,12Z)-octadecadienoyloxy]acyl-beta-D-glucosyl-(1<->1)-
CC octadecasphing-4E-enine; Xref=Rhea:RHEA:40495, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:134621, ChEBI:CHEBI:134624;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40496;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acyl (9Z,12Z)-octadecadienoate octadecasphin-4E-enine + O2 =
CC N-acyl (9R)-hydroperoxy-(10E,12Z)-octadecadienoate octadecasphing-4E-
CC enine; Xref=Rhea:RHEA:41239, ChEBI:CHEBI:15379, ChEBI:CHEBI:77888,
CC ChEBI:CHEBI:77889; Evidence={ECO:0000250|UniProtKB:O75342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41240;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-octadecatrienoate + O2 = 10-hydroperoxy-
CC (6Z,8E,12Z)-octadecatrienoate; Xref=Rhea:RHEA:43476,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32391, ChEBI:CHEBI:83342;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43477;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = 14-
CC hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate;
CC Xref=Rhea:RHEA:43472, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:83336; Evidence={ECO:0000250|UniProtKB:O75342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43473;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = (8Z,10E,14Z)-12-
CC hydroperoxyeicosatrienoate; Xref=Rhea:RHEA:43468, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:71589, ChEBI:CHEBI:83334;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43469;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 =
CC (5Z,7Z,8Z,10E,14Z,17Z)-12-hydroperoxyeicosapentaenoate;
CC Xref=Rhea:RHEA:41344, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:78078; Evidence={ECO:0000250|UniProtKB:O75342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41345;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z)-octadecatrienoate + O2 = 10R-hydroperoxy-
CC (6Z,8E,12Z)-octadecatrienoate; Xref=Rhea:RHEA:41340,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32391, ChEBI:CHEBI:78070;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41341;
CC Evidence={ECO:0000250|UniProtKB:O75342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-
CC methyl-(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:61868, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033,
CC ChEBI:CHEBI:78180; Evidence={ECO:0000269|PubMed:11256953,
CC ECO:0000269|PubMed:16129665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61869;
CC Evidence={ECO:0000305|PubMed:16129665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-(9Z,12Z)-octadecadienoate + O2 = 1-O-methyl-(9R)-
CC hydroperoxy-(10E,12Z)-octadecadienoate; Xref=Rhea:RHEA:61872,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:69080, ChEBI:CHEBI:145036;
CC Evidence={ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61873;
CC Evidence={ECO:0000305|PubMed:16129665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 =
CC 1-O-methyl-8-hydroperoxy-20-hydroxy-(5Z,9E,11Z,14Z)-
CC eicosatetraenoate; Xref=Rhea:RHEA:61876, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:145032, ChEBI:CHEBI:145033;
CC Evidence={ECO:0000269|PubMed:16129665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61877;
CC Evidence={ECO:0000305|PubMed:16129665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 =
CC 1-O-methyl-12-hydroperoxy-20-hydroxy-(5Z,8Z,10E,14Z)-
CC eicosatetraenoate; Xref=Rhea:RHEA:61880, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:145032, ChEBI:CHEBI:145034;
CC Evidence={ECO:0000269|PubMed:16129665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61881;
CC Evidence={ECO:0000305|PubMed:16129665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 =
CC 1-O-methyl-9-hydroperoxy-20-hydroxy-(5Z,7E,11Z,14Z)-
CC eicosatetraenoate; Xref=Rhea:RHEA:61884, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:145032, ChEBI:CHEBI:145035;
CC Evidence={ECO:0000269|PubMed:16129665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61885;
CC Evidence={ECO:0000305|PubMed:16129665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-(9Z,12Z)-octadecadienoate + O2 = 1-O-methyl-(13S)-
CC hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:41756,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:69080, ChEBI:CHEBI:78040;
CC Evidence={ECO:0000269|PubMed:16129665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41757;
CC Evidence={ECO:0000305|PubMed:16129665};
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 -!- ACTIVITY REGULATION: Increased by calcium.
CC {ECO:0000269|PubMed:11256953}.
CC -!- PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid
CC biosynthesis.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
CC -!- TISSUE SPECIFICITY: Expressed in skin epidermis and other stratified
CC epithelia including tongue and forestomach. Low levels of expression
CC are found in trachea, brain and lung. Not expressed in intestine,
CC liver, kidney, adipose tissue, muscle or hematopoietic cells.
CC {ECO:0000269|PubMed:9518531}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression begins at day 15.5.
CC {ECO:0000269|PubMed:9837935}.
CC -!- DISRUPTION PHENOTYPE: Mice die within 3 to 5 hours after birth due to
CC defective skin barrier function loosing around 30% of body weight
CC within 3 hours. Dehydration through the skin is increased 8 folds. The
CC outside-in barrier acquisition is also affected, the skin remaining
CC permeable at 18.5 dpc while it is impermeable in wild-type mice. The
CC stratum corneum is more tightly packed while other layers are
CC unaffected. Processing of filaggrin/FG is aberrant and the skin
CC displays structural abnormalities. The cornified envelope is more
CC fragile and the ceramide composition of the epidermis is altered.
CC {ECO:0000269|PubMed:17403930, ECO:0000269|PubMed:21558561}.
CC -!- MISCELLANEOUS: Mummy, a recessive ethylnitrosurea-induced mutant has a
CC nonsense mutation in the catalytic domain of Lox12b, resulting in
CC truncation of the protein by 68 amino acids. The affected mice are born
CC with red, shiny skin that desiccates and appears scaly. They probably
CC die of dehydration like mice with targeted disruption of the gene
CC (PubMed:17429434). {ECO:0000305|PubMed:17429434}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; Y14334; CAA74714.1; -; mRNA.
DR EMBL; AF059251; AAC79681.1; -; mRNA.
DR CCDS; CCDS24885.1; -.
DR RefSeq; NP_033789.1; NM_009659.2.
DR AlphaFoldDB; O70582; -.
DR SMR; O70582; -.
DR STRING; 10090.ENSMUSP00000035250; -.
DR SwissLipids; SLP:000000658; -.
DR SwissLipids; SLP:000000941; -.
DR SwissLipids; SLP:000000942; -.
DR PhosphoSitePlus; O70582; -.
DR PaxDb; O70582; -.
DR PRIDE; O70582; -.
DR ProteomicsDB; 292149; -.
DR Antibodypedia; 12404; 102 antibodies from 19 providers.
DR DNASU; 11686; -.
DR Ensembl; ENSMUST00000036424; ENSMUSP00000035250; ENSMUSG00000032807.
DR GeneID; 11686; -.
DR KEGG; mmu:11686; -.
DR UCSC; uc007jpk.1; mouse.
DR CTD; 242; -.
DR MGI; MGI:1274782; Alox12b.
DR VEuPathDB; HostDB:ENSMUSG00000032807; -.
DR eggNOG; ENOG502SJSP; Eukaryota.
DR GeneTree; ENSGT00940000162032; -.
DR HOGENOM; CLU_004282_3_3_1; -.
DR InParanoid; O70582; -.
DR OMA; RCRNPNR; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; O70582; -.
DR TreeFam; TF105320; -.
DR BRENDA; 1.13.11.31; 3474.
DR Reactome; R-MMU-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
DR UniPathway; UPA00222; -.
DR UniPathway; UPA00881; -.
DR BioGRID-ORCS; 11686; 2 hits in 75 CRISPR screens.
DR PRO; PR:O70582; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O70582; protein.
DR Bgee; ENSMUSG00000032807; Expressed in esophagus and 40 other tissues.
DR ExpressionAtlas; O70582; baseline and differential.
DR Genevisible; O70582; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0106237; F:arachidonate 12(R)-lipoxygenase activity; IEA:RHEA.
DR GO; GO:0004052; F:arachidonate 12(S)-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0047677; F:arachidonate 8(R)-lipoxygenase activity; IMP:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; IDA:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; ISO:MGI.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0070257; P:positive regulation of mucus secretion; ISS:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; 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; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..701
FT /note="Arachidonate 12-lipoxygenase, 12R-type"
FT /id="PRO_0000220690"
FT DOMAIN 2..119
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 120..701
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 398
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 403
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 578
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 582
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 701
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT VARIANT 9
FT /note="A -> V (in strain: C57BL/6 X SJL)"
FT VARIANT 351
FT /note="M -> V (in strain: C57BL/6 X SJL)"
FT VARIANT 361
FT /note="T -> I (in strain: C57BL/6 X SJL)"
FT MUTAGEN 390
FT /note="F->A: Reduced enzymatic activity and altered
FT stereoselectivity of the oxygenation reaction."
FT /evidence="ECO:0000269|PubMed:16129665"
FT MUTAGEN 390
FT /note="F->W: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16129665"
FT MUTAGEN 441
FT /note="G->A: Reduced enzymatic activity and changed
FT stereoselectivity of the oxygenation reaction."
FT /evidence="ECO:0000269|PubMed:16129665"
FT MUTAGEN 441
FT /note="G->V: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16129665"
FT MUTAGEN 455
FT /note="A->I,W: Reduced enzymatic activity and altered
FT stereoselectivity of the oxygenation reaction."
FT /evidence="ECO:0000269|PubMed:16129665"
FT MUTAGEN 631
FT /note="V->A,G: Increased enzymatic activity and changed
FT stereoselectivity of the oxygenation reaction to produce
FT (11R)-HPETE preferentially instead of (12R)-HPETE."
FT /evidence="ECO:0000269|PubMed:16129665"
SQ SEQUENCE 701 AA; 80578 MW; FAE3A3B8D2AA142E CRC64;
MATYKVKVAT GTDFFSGTLD SISLTIVGTQ GESHKQRLNH FGRDFATGAV DDYTVQCQQD
LGELIIIRLH KEPHSFLAKD PWYCNYVQIC APDCRVYHFP AYQWMDGYET LALREATGKI
TADDTLPILL EHRQEEIRAK KDFYHWRVFV PGLPNYVDIP SYHPPPRRCR NPNRPEWDGY
IPGFPILINI KATRFLNSNL RFSFVKTASF FYRLGPMALA FKLRGLVDRK RSWKRLKDIK
NIFPATKSVV SEYVAEHWTE DSFFGYQYLN GINPGLIRRC TQIPDKFPVT DEMVAPFLGE
GTCLQAELER GNIYLADYRI LDGIPTVELN GQQQHHCAPM CLLHFGPDGN MMPIAIQLSQ
TPGPDCPIFL PNDSEWDWLL AKTWVRYAEF YSHEAVAHLL ESHLIGEAFC LALLRNLPMC
HPLYKLLIPH TRYNVQINSI GRALLLNKGG LSARAMSLGL EGFAQVMVRG LSELTYKSLC
IPNDFVERGV QDLPGYYFRD DSLAVWYAME RYVTEIITYY YPNDAAVEGD PELQCWVQEI
FKECLLGRES SGFPTCLRTI PELIEYVTMV MYTCSARHAA VNSGQLEYTS WMPNFPSSMR
NPPMQTKGLT TLQTYMDTLP DVKTTCIVLL VLWTLCREPD DRRPLGHFPD IHFVEEGPRR
SIEAFRQNLN QISHNIRQRN KCLTLPYYYL DPVLIENSIS I
