ID A0A091D7P0_FUKDA Unreviewed; 236 AA.
AC A0A091D7P0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Arachidonate 15-lipoxygenase B {ECO:0000313|EMBL:KFO18856.1};
GN ORFNames=H920_19760 {ECO:0000313|EMBL:KFO18856.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO18856.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO18856.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO18856.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962,
CC ECO:0000256|RuleBase:RU003974};
CC -!- SIMILARITY: Belongs to the lipoxygenase family.
CC {ECO:0000256|RuleBase:RU003974}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR EMBL; KN125302; KFO18856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D7P0; -.
DR STRING; 885580.ENSFDAP00000015041; -.
DR Ensembl; ENSFDAT00000004629; ENSFDAP00000015041; ENSFDAG00000002662.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR OMA; ALREATX; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF161; POLYUNSATURATED FATTY ACID LIPOXYGENASE ALOX15B; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003974};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003974};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 2..150
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 178..236
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 236 AA; 25738 MW; 1F40A796C2E9256F CRC64;
MVKFRVRAST GEACGAGTWD KVSVTIVGTQ GESPPLPLGH LGKKFTAGCR GEEVEEAEKP
LSGTQTFPHP GEADFEVTLP EDVGPVLLLR VHKAPPALLR PLRTLAPGPR VLSLVPAGAA
EGPRGAPLRF PCYECLEGTG TLVLREGSAK VSWADHHPML ENQLQEGLQA KQKMYRDEKW
NWLLAKTWVH NAEFSVHEAL THLLHAHLLP EVFTMATLHQ LPHCCPLFKV TGSAYA
//