Sequence of LOX15_PIG

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
arachidonate 15-lipoxygenase
P16469
Sus scrofa
663
75004
Reaction
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Sequences with same EC No.
Sequence
show sequence in fasta format
  0 MGLYRVRVST GSSFYAGSQN QVQLWLVGQH GEAALGWCLR PARGKETEFS VDVSEYLGPL
 60 LFVKLRKRHL LQDDAWFCNW ISVQGPGANG DEFRFPCYRW VEGDRILSLP EGTARTVVDD
120 PQGLFKKHRE EELAERRKLY RWGNWKDGLI LNIASTGIHD LPVDERFLED KRIDFEASLA
180 KGLADLAVKD SLNVLMSWNS LDSFNRIFWC GQSKLAERVR DSWKEDALFG YQFLNGTNPM
240 LLRHSVELPA RLKFPPGMEE LQAQLEKELQ GGTLFEADFS LLDGIKANVI LCSQQYLAVP
300 LVMLKLQPDG KLLPMVIQLQ LPHEGSPLPP LFLPTDPPMV WLLAKCWVRS SDFQLHELHS
360 HLLRGHLMAE VIAVATMRCL PSIHPIFKLL IPHFRYTMEI NVRARNGLVS DLGIFDQVVS
420 TGGGGHVELL RRAAALLTYS SFCPPDDLAD RGLLGVESSF YAQDALRLWE VISRYVEGIV
480 SLHYKTDESV KEDLELQAWC REFTEIGLLG AQDRGFPVSL QSKEQLCHFV TMCIFTCTGQ
540 HSSNHLGQLD WYSWVPNAPC TMRLPPPTTK DATLETVMAT LPNFHQASLQ MSITWQLGRC
600 QPTMVALGQH EEEYFSGPGP KAVLTKFREE LAALDKDIEV RNAKLALPYE YLRPSRVENS
660 VAI
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
303539
Yoshimoto T.,Suzuki H.,Yamamoto S.,Takai T.,Yokoyama C.,Tanabe T.
Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes.
Proc. Natl. Acad. Sci. U.S.A.
87
2142-2146
1990
303540
Arakawa T.,Oshima T.,Kishimoto K.,Yoshimoto T.,Yamamoto S.
Molecular structure and function of the porcine arachidonate 12-lipoxygenase gene.
J. Biol. Chem.
267
12188-12191
1992
303542
Suzuki H.,Kishimoto K.,Yoshimoto T.,Yamamoto S.,Kanai F.,Ebina Y.,Miyatake A.,Tanabe T.
Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase.
Biochim. Biophys. Acta
1210
308-316
1994
303543
Xu S.,Mueser T.C.,Marnett L.J.,Funk M.O. Jr.
Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis.
Structure
20
1490-1497
2012