ID LX12E_MOUSE Reviewed; 662 AA. AC P55249; Q91YW6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 25-NOV-2008, entry version 74. DE RecName: Full=Arachidonate 12-lipoxygenase, epidermal-type; DE Short=12-LOX; DE EC=1.13.11.31; GN Name=Alox12e; Synonyms=Alox12-ps2, Aloxe; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X 129/Sv; TISSUE=Epidermis; RX MEDLINE=96394429; PubMed=8798535; DOI=10.1074/jbc.271.38.23338; RA Funk C.D., Keeney D.S., Oliw E.H., Boeglin W.E., Brash A.R.; RT "Functional expression and cellular localization of a mouse epidermal RT lipoxygenase."; RL J. Biol. Chem. 271:23338-23344(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/Sv; TISSUE=Epidermis; RX MEDLINE=96085100; PubMed=7492614; DOI=10.1016/0005-2760(95)00158-9; RA van Dijk K.W., Steketee K., Havekes L., Frants R., Hofker M.; RT "Genomic and cDNA cloning of a novel mouse lipoxygenase gene."; RL Biochim. Biophys. Acta 1259:4-8(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NMRI; TISSUE=Skin; RX MEDLINE=97188602; PubMed=9037187; DOI=10.1016/S0014-5793(96)01517-7; RA Kinzig A., Fuerstenberger G., Mueller F., Vogel S., Mueller-Decker K., RA Mincheva A., Lichter P., Marks F., Krieg P.; RT "Murine epidermal lipoxygenase (Aloxe) encodes a 12-lipoxygenase RT isoform."; RL FEBS Lett. 402:162-166(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-260; LEU-453 RP AND SER-617. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)- CC 12-hydroperoxyicosa-5,8,10,14-tetraenoate. CC -!- COFACTOR: Binds 1 iron ion per subunit. CC -!- PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- TISSUE SPECIFICITY: Epidermal. CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. CC -!- CAUTION: Was originally thought to be an arachidonate 8- CC lipoxygenase and was called LOX8. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U39200; AAC52869.1; -; mRNA. DR EMBL; U24181; AAC52324.1; -; Genomic_DNA. DR EMBL; X99252; CAA67625.1; -; mRNA. DR EMBL; BC013751; AAH13751.1; -; mRNA. DR EMBL; BC051047; AAH51047.1; -; mRNA. DR RefSeq; NP_663717.1; -. DR UniGene; Mm.274093; -. DR HSSP; P12530; 1LOX. DR Ensembl; ENSMUSG00000018907; Mus musculus. DR GeneID; 11685; -. DR KEGG; mmu:11685; -. DR MGI; MGI:1274790; Alox12e. DR HOGENOM; P55249; -. DR HOVERGEN; P55249; -. DR NextBio; 279323; -. DR ArrayExpress; P55249; -. DR CleanEx; MM_ALOX12E; -. DR GermOnline; ENSMUSG00000018907; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IEA:EC. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016165; F:lipoxygenase activity; IEA:InterPro. DR GO; GO:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR001024; LipOase_LH2. DR InterPro; IPR001885; LipOase_mml. DR Gene3D; G3DSA:2.60.60.20; Lipase_LipOase; 1. DR PANTHER; PTHR11771; LipOase; 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 PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Dioxygenase; Iron; Leukotriene biosynthesis; Metal-binding; KW Oxidoreductase. FT CHAIN 1 662 Arachidonate 12-lipoxygenase, epidermal- FT type. FT /FTId=PRO_0000220688. FT DOMAIN 2 114 PLAT. FT DOMAIN 115 662 Lipoxygenase. FT METAL 360 360 Iron; catalytic (By similarity). FT METAL 365 365 Iron; catalytic (By similarity). FT METAL 540 540 Iron; catalytic (By similarity). FT METAL 662 662 Iron; via carboxylate; catalytic (By FT similarity). FT VARIANT 260 260 V -> L (in strain:FVB/N). FT VARIANT 453 453 V -> L (in strain:FVB/N). FT VARIANT 617 617 P -> S (in strain:FVB/N). FT CONFLICT 619 619 P -> A (in Ref. 2; AAC52324). SQ SEQUENCE 662 AA; 75456 MW; D67768415EE988F7 CRC64; MVKYKILVAT GDSVFAGSAN LVHLWLVGEH GEADLGKQLR PLLGRKTELE VDVPLHLGRL LAVKLRKQKG LLDSDWFCKS ITVQGPGTQG EAFFPCYSWV QGKETICLTE GTALKVTDDT QNLFRKYREQ ELENRRNVYR WGSWKEGLIL PIAGSTERDL PRNQRFMKDK DLDFSLSLVK ELKNFAIKGT LDFVSRVQKL EDYQKVFPHT KTALPERVRG SWKEDALFGY QFLNGANPML LRRSMRLPAR LVLPPGMEDV QTQLEKELKA GSLFEVDFSL LDGVKPNIII FKQQYVTAPL VMLKLQPDGR LLPMVIQLQP PRHGCPPPLL FLPSDPPMAW LLAKIWVRSS DFQLHQLQSH LLRGHLMAEV ISVATMRSLP SLHPIYKLLA PHFRYTMEIN TLARNNLVSE WGIFDLVVST GSGGHVDILQ RATSCLTYRS FCPPDDLADR GLVGVKSSLY AQDALRLWEI ISRYVERMVE LFYRSDTDVK EDPELQVWCR EVTEVGLLGA QDRGFPLSLE SRAELCRFVA MCIFTCTGQH ASTHLGQLDW YAWIPNGPCT MRKPPPISKD VTERDIVDSL PCLQQARMQI TVTKFLGRRQ PVMVALGQHK EEYFSGPRPR DVLKQFQEEL AIMDKEIEVR NASLDLPYEY LRPSLVENSV TI //