ID A0A341ASR6_NEOAA Unreviewed; 663 AA. AC A0A341ASR6; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 05-FEB-2025, entry version 27. DE SubName: Full=LOW QUALITY PROTEIN: arachidonate 15-lipoxygenase {ECO:0000313|RefSeq:XP_024592292.1}; GN Name=ALOX15 {ECO:0000313|RefSeq:XP_024592292.1}; OS Neophocaena asiaeorientalis asiaeorientalis (Yangtze finless porpoise) OS (Neophocaena phocaenoides subsp. asiaeorientalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti; OC Phocoenidae; Neophocaena. OX NCBI_TaxID=1706337 {ECO:0000313|Proteomes:UP000252040, ECO:0000313|RefSeq:XP_024592292.1}; RN [1] {ECO:0000313|RefSeq:XP_024592292.1} RP IDENTIFICATION. RC TISSUE=Meat {ECO:0000313|RefSeq:XP_024592292.1}; RG RefSeq; RL Submitted (OCT-2024) to UniProtKB. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000256|PIRSR:PIRSR601885-1}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR601885-1}; CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_024592292.1; XM_024736524.1. DR STRING; 1706337.A0A341ASR6; -. DR KEGG; nasi:112394032; -. DR InParanoid; A0A341ASR6; -. DR Proteomes; UP000252040; Unplaced. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004052; F:arachidonate 12(S)-lipoxygenase activity; IEA:UniProtKB-ARBA. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0019369; P:arachidonate metabolic process; IEA:UniProtKB-ARBA. DR GO; GO:0034440; P:lipid oxidation; IEA:InterPro. DR GO; GO:0019372; P:lipoxygenase pathway; IEA:UniProtKB-ARBA. DR CDD; cd01753; PLAT_LOX; 1. DR FunFam; 3.10.450.60:FF:000004; Arachidonate 12-lipoxygenase, 12S-type; 1. DR FunFam; 1.20.245.10:FF:000001; Arachidonate 5-lipoxygenase a; 1. DR FunFam; 2.60.60.20:FF:000002; Arachidonate 5-lipoxygenase a; 1. DR Gene3D; 3.10.450.60; -; 1. DR Gene3D; 1.20.245.10; Lipoxygenase-1, Domain 5; 1. 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; IPR001885; LipOase_mml. DR InterPro; IPR001024; PLAT/LH2_dom. DR InterPro; IPR036392; PLAT/LH2_dom_sf. DR InterPro; IPR042062; PLAT_LOX_verte. DR PANTHER; PTHR11771; LIPOXYGENASE; 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 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 Calcium {ECO:0000256|PIRSR:PIRSR601885-2}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601885-1}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR601885-1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003974}; KW Reference proteome {ECO:0000313|Proteomes:UP000252040}. FT DOMAIN 2..115 FT /note="PLAT" FT /evidence="ECO:0000259|PROSITE:PS50095" FT DOMAIN 115..663 FT /note="Lipoxygenase" FT /evidence="ECO:0000259|PROSITE:PS51393" FT BINDING 17 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2" FT BINDING 74 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2" FT BINDING 75 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2" FT BINDING 361 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1" FT BINDING 366 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1" FT BINDING 663 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1" FT SITE 100 FT /note="Essential for stabilizing binding to COTL1" FT /evidence="ECO:0000256|PIRSR:PIRSR601885-3" SQ SEQUENCE 663 AA; 75005 MW; C5A301355200191C CRC64; MGLYRVRASS GSSLCAGSNN KVQLWLVGQH GEVALGWRVR PMRGKEAEFE VDVSEYLGPL LFVKLSKWHL LQDDAWFCNW ISVQGPGASG DQFRFPCYRW LEGKGILSLP EGTGRTVVDD PQGLFKKHRE EEPEERRKLY WWGNWKDELI LNMAGATICD LPTDERFLED KRIDFEASLV KGLADLAIKD SSNILTSWNS LDDFNRIFWC GQSKLAERVR DSWKEDALFG YQFLNGSNPM LLRCSNHLPA RLEFPPGMEE LQAQLEKELQ GGTLFEADVS LLDGIKANVI LCSQQYLAAP LVMLKLQPDG KLLPMVIQLQ LPCKGSLPPL LFLPMDPPMA WLLAKCWVRS SDFQLHELQS HLLRGHLVAE VIAVATVRCL PSIHPMFKLL ILHIRYTTEI NLRARTGLVA DLGIFDQVVS TGGGGHVDLF KRAGAFLTYS SFCXPDDLAE RGLLGVKSPF YVQDALRLWE IISHYVEGIV SLHYKTDKSV KEDLELQAWC XEITEIGLLG AQDRGFPIAL QSKDQLCHFX TTCIFTCTGQ YSSNHLDQLD WYAWVPNAPC TMRLPLPTTK DVTLETAMAT LPNFHQASLQ MSITWQLGRR QSIMVALDQH EEEYFSGPEP KAALKKFREE LAALEKGIEI WNAKLDLPYE YLWPSLVENS VAI //