ID   LX15B_MOUSE             Reviewed;         677 AA.
AC   O35936;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 84.
DE   RecName: Full=Arachidonate 15-lipoxygenase type II;
DE            Short=15-LOX-2;
DE            EC=1.13.11.33;
DE   AltName: Full=8S-lipoxygenase;
DE            Short=8S-LOX;
GN   Name=Alox15b; Synonyms=Alox8;
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], AND CHARACTERIZATION.
RC   TISSUE=Epidermis;
RX   MEDLINE=97450967; PubMed=9305900; DOI=10.1074/jbc.272.39.24410;
RA   Jisaka M., Kim R.B., Boeglin W.E., Nanney L.B., Brash A.R.;
RT   "Molecular cloning and functional expression of a phorbol ester-
RT   inducible 8S-lipoxygenase from mouse skin.";
RL   J. Biol. Chem. 272:24410-24416(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=NMRI; TISSUE=Epidermis;
RX   MEDLINE=98186642; 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
RT   lipoxygenase from phorbol ester-treated mouse skin.";
RL   Biochim. Biophys. Acta 1391:7-12(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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,11Z,13E)-(15S)-
CC       15-hydroperoxyicosa-5,8,11,13-tetraenoate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in epidermis and brain. No
CC       expression found in heart, spleen, liver, skeletal muscle, kidney
CC       or testis.
CC   -!- INDUCTION: By phorbol ester.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC   -!- SIMILARITY: Contains 1 lipoxygenase domain.
CC   -!- SIMILARITY: Contains 1 PLAT domain.
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DR   EMBL; U93277; AAC53356.1; -; mRNA.
DR   EMBL; Y14696; CAA75003.1; -; mRNA.
DR   EMBL; AK028724; BAC26085.1; -; mRNA.
DR   EMBL; BC015253; AAH15253.1; -; mRNA.
DR   IPI; IPI00136170; -.
DR   RefSeq; NP_033791.1; -.
DR   UniGene; Mm.289672; -.
DR   HSSP; P12530; 1LOX.
DR   Ensembl; ENSMUSG00000020891; Mus musculus.
DR   GeneID; 11688; -.
DR   KEGG; mmu:11688; -.
DR   MGI; MGI:1098228; Alox8.
DR   HOGENOM; O35936; -.
DR   HOVERGEN; O35936; -.
DR   OMA; O35936; MPNLPPS.
DR   BRENDA; 1.13.11.33; 244.
DR   NextBio; 279335; -.
DR   ArrayExpress; O35936; -.
DR   Bgee; O35936; -.
DR   CleanEx; MM_ALOX8; -.
DR   GermOnline; ENSMUSG00000020891; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; ISS:UniProtKB.
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:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Cytoplasm; Dioxygenase; Iron; Leukotriene biosynthesis; Metal-binding;
KW   Oxidoreductase; Polymorphism.
FT   CHAIN         1    677       Arachidonate 15-lipoxygenase type II.
FT                                /FTId=PRO_0000220701.
FT   DOMAIN        2    125       PLAT.
FT   DOMAIN      126    677       Lipoxygenase.
FT   METAL       374    374       Iron; catalytic (By similarity).
FT   METAL       379    379       Iron; catalytic (By similarity).
FT   METAL       554    554       Iron; catalytic (By similarity).
FT   METAL       677    677       Iron; via carboxylate; catalytic (By
FT                                similarity).
FT   VARIANT      32     32       E -> G (in clone K12).
FT   VARIANT      38     38       L -> M (in clone G2).
FT   VARIANT      58     58       P -> R (in clone K12).
FT   VARIANT      76     76       V -> A (in clones G2, G5, G11 and K1).
FT   VARIANT     413    413       I -> V (in clone K7).
FT   VARIANT     536    536       R -> Q (in clones G2, G5 and G11).
SQ   SEQUENCE   677 AA;  76230 MW;  78DB1AC9C2F68399 CRC64;
     MAKCRVRVST GEACGAGTWD KVSVSIVGTH GESPLVPLDH LGKEFSAGAE EDFEVTLPQD
     VGTVLMLRVH KAPPEVSLPL MSFRSDAWFC RWFELEWLPG AALHFPCYQW LEGAGELVLR
     EGAAKVSWQD HHPTLQDQRQ KELESRQKMY SWKTYIEGWP RCLDHETVKD LDLNIKYSAM
     KNAKLFFKAH SAYTELKVKG LLDRTGLWRS LREMRRLFNF RKTPAAEYVF AHWQEDAFFA
     SQFLNGINPV LIRRCHSLPN NFPVTDEMVA PVLGPGTSLQ AELEKGSLFL VDHGILSGVH
     TNILNGKPQF SAAPMTLLHQ SSGSGPLLPI AIQLKQTPGP DNPIFLPSDD TWDWLLAKTW
     VRNSEFYIHE AVTHLLHAHL IPEVFALATL RQLPRCHPLF KLLIPHIRYT LHINTLAREL
     LVAPGKLIDK STGLGTGGFS DLIKRNMEQL NYSVLCLPED IRARGVEDIP GYYYRDDGMQ
     IWGAIKSFVS EIVSIYYPSD TSVQDDQELQ AWVREIFSEG FLGRESSGMP SLLDTREALV
     QYITMVIFTC SAKHAAVSSG QFDSCVWMPN LPPTMQLPPP TSKGQARPES FIATLPAVNS
     SSYHIIALWL LSAEPGDQRP LGHYPDEHFT EDAPRRSVAA FQRKLIQISK GIRERNRGLA
     LPYTYLDPPL IENSVSI
//