ID LOX12_RABIT Reviewed; 663 AA. AC O19043; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 61. DE RecName: Full=Arachidonate 12-lipoxygenase, 12S-type; DE Short=12-LOX; DE EC=1.13.11.31; GN Name=ALOX12; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX MEDLINE=98263260; PubMed=9600854; DOI=10.1006/jmbi.1998.1737; RA Berger M., Schwarz K., Thiele H., Reimann I., Huth A., Borngraeber S., RA Kuehn H., Thiele B.-J.; RT "Simultaneous expression of leukocyte-type 12-lipoxygenase and RT reticulocyte-type 15-lipoxygenase in rabbits."; RL J. Mol. Biol. 278:935-948(1998). CC -!- FUNCTION: Oxygenase and 14,15-leukotriene A4 synthase activity. 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. CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. 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; Z97654; CAB10746.1; -; mRNA. DR RefSeq; NP_001139620.1; -. DR HSSP; P12530; 1LOX. DR SMR; O19043; 2-663. DR GeneID; 100271999; -. DR HOVERGEN; O19043; -. DR BRENDA; 1.13.11.31; 255. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004052; F:arachidonate 12-lipoxygenase activity; IEA:EC. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. 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 INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 663 Arachidonate 12-lipoxygenase, 12S-type. FT /FTId=PRO_0000220685. FT DOMAIN 2 115 PLAT. FT DOMAIN 116 663 Lipoxygenase. FT METAL 361 361 Iron; catalytic (By similarity). FT METAL 366 366 Iron; catalytic (By similarity). FT METAL 541 541 Iron; catalytic (By similarity). FT METAL 663 663 Iron; via carboxylate; catalytic (By FT similarity). SQ SEQUENCE 663 AA; 75234 MW; 19670402E5C22A8B CRC64; MGVYRVCVST GASIYAGSKN KVELWLVGQH GEVELGSCLR PSRNKEEEFK VNVSKYLGSL LFVKLRKKHF LKEDAWFCNW ISVQALGAAE DKYWFPCYRW VVGDGVQSLP VGTGCTTVGD PQGLFQKHRE QELEERRKLY QWGSWKEGLI LNVAGSKLTD LPVDERFLED KKIDFEASLA WGLAELALKN SLNILAPWKT LDDFNRIFWC GRSKLARRVR DSWQEDSLFG YQFLNGANPM LLRRSVQLPA RLVFPPGMEE LQAQLEKELK AGTLFEADFA LLDNIKANVI LYCQQYLAAP LVMLKLQPDG KLMPMVIQLH LPKIGSSPPP LFLPTDPPMV WLLAKCWVRS SDLQVHELNS HLLRGHLMAE VFTVATMRCL PSIHPVFKLI VPHLRYTLEI NVRARNGLVS DFGIFDQIMS TGGGGHVQLL QQAGAFLTYR SFCPPDDLAD RGLLGVESSF YAQDALRLWE IISRYVQGIM GLYYKTDEAV RDDLELQSWC REITEIGLQG AQKQGFPTSL QSVAQACHFV TMCIFTCTGQ HSSIHLGQLD WFTWVPNAPC TMRLPPPTTK DATLETVMAT LPNLHQSSLQ MSIVWQLGRD QPIMVPLGQH QEEYFSGPEP RAVLEKFREE LAIMDKEIEV RNEKLDIPYE YLRPSIVENS VAI //