ID   LOX5_MESAU              Reviewed;         673 AA.
AC   P51399;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=Arachidonate 5-lipoxygenase;
DE            Short=5-lipoxygenase;
DE            Short=5-LO;
DE            EC=1.13.11.34;
GN   Name=ALOX5;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Syrian;
RX   MEDLINE=97109716; PubMed=8951996; DOI=10.1016/S0952-3278(96)90008-3;
RA   Kitzler J.W., Eling T.E.;
RT   "Cloning, sequencing and expression of a 5-lipoxygenase from Syrian
RT   hamster embryo fibroblasts.";
RL   Prostaglandins Leukot. Essent. Fatty Acids 55:269-277(1996).
CC   -!- CATALYTIC ACTIVITY: Arachidonate + O(2) = leukotriene A(4) +
CC       H(2)O.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity).
CC   -!- PATHWAY: Lipid metabolism; leukotriene A4 biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein (By similarity). Note=Calcium binding promotes binding to
CC       membranes (By similarity).
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; U43333; AAA85257.1; -; mRNA.
DR   HSSP; P12530; 1LOX.
DR   HOVERGEN; P51399; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004051; F:arachidonate 5-lipoxygenase activity; IEA:EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
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   Calcium; Cytoplasm; Dioxygenase; Iron; Leukotriene biosynthesis;
KW   Membrane; Metal-binding; Oxidoreductase; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    673       Arachidonate 5-lipoxygenase.
FT                                /FTId=PRO_0000220694.
FT   DOMAIN        2    117       PLAT.
FT   DOMAIN      118    673       Lipoxygenase.
FT   METAL        17     17       Calcium 1; via carbonyl oxygen;
FT                                structural (By similarity).
FT   METAL        18     18       Calcium 2; via carbonyl oxygen;
FT                                structural (By similarity).
FT   METAL        19     19       Calcium 2; structural (By similarity).
FT   METAL        44     44       Calcium 2; structural (By similarity).
FT   METAL        45     45       Calcium 2; via carbonyl oxygen;
FT                                structural (By similarity).
FT   METAL        47     47       Calcium 2; structural (By similarity).
FT   METAL        79     79       Calcium 1; via carbonyl oxygen;
FT                                structural (By similarity).
FT   METAL        80     80       Calcium 1; via carbonyl oxygen;
FT                                structural (By similarity).
FT   METAL       367    367       Iron; catalytic (By similarity).
FT   METAL       372    372       Iron; catalytic (By similarity).
FT   METAL       550    550       Iron; catalytic (By similarity).
FT   METAL       554    554       Iron; catalytic (By similarity).
FT   METAL       673    673       Iron; via carboxylate; catalytic (By
FT                                similarity).
FT   MOD_RES     271    271       Phosphoserine (By similarity).
FT   MOD_RES     523    523       Phosphoserine (By similarity).
SQ   SEQUENCE   673 AA;  77873 MW;  A7AF63B11CDC7972 CRC64;
     MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA VDSYDVTVDE
     ELGEIQLVRI EKRKYWLHDD WYLKYITLKT PTDYIEFPCY RWITGEGEIV LRDGRAKLAR
     DDQIHILKQH RRKELEARQK QYRWMEWNPG FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN
     YSKAMENLFI NRFMHMFQSS WNDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC
     NPVLIKRCRE LPQKLPVTTE MVECSLERHL SLEQEVQEGN IFIVDYELLD GIDANKTDPC
     THQFLAAPIC LLYKNLANKI VPIAIQLNQA PGEKNPIFLP SDAKYDWLLA KIWVRSSDFH
     VHQTITHLLC THLVSEVFGI AMYRQLPAVH PIFKLLVAHV RFTIAINTKA REQLICEYGL
     FDKANATGGG GHVQMVQRAV QDLTYSSLCF PEAIKARGMD STEDIPYYFY RDDGLLVWEA
     IQSFTSEVVS IYYEDDQVVM EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT
     VVIFTASAQH AAVNFGQYDW CSWIPNAPPT MRAPPATAKG VVTIEQIVAT LPDRGRSCWH
     LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMTRFRKN LEAIVNVIAE RNKNKKLPYY
     YLSPDRIPNS VAI
//