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Database: UniProt
Entry: W5N833_LEPOC
LinkDB: W5N833_LEPOC
Original site: W5N833_LEPOC 
ID   W5N833_LEPOC            Unreviewed;       606 AA.
AC   W5N833;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Si:dkey-17e16.9 {ECO:0000313|Ensembl:ENSLOCP00000016792.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016792.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000016792.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR   EMBL; AHAT01030453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5N833; -.
DR   Ensembl; ENSLOCT00000016822.1; ENSLOCP00000016792.1; ENSLOCG00000013611.1.
DR   GeneTree; ENSGT00940000156796; -.
DR   Proteomes; UP000018468; Linkage group LG2.
DR   Bgee; ENSLOCG00000013611; Expressed in testis and 8 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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: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; IPR001885; LipOase_mml.
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   Pfam; PF01477; PLAT; 1.
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; PS51393; LIPOXYGENASE_3; 2.
DR   PROSITE; PS50095; PLAT; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR601885-2};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {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   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   DOMAIN          35..152
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          152..358
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   DOMAIN          359..606
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   BINDING         50
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         113
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         114
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         483
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   SITE            137
FT                   /note="Essential for stabilizing binding to COTL1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-3"
SQ   SEQUENCE   606 AA;  69056 MW;  34C60B9F6AAEF497 CRC64;
     MMTSRAQSGA NWVQGSCWPP ALWWGWMNCS SSRMETYKVT VTTGDMVHSG TFDRVFITLV
     GSEDRSERTV LSTEGQDLSS GMVMELAVSA PDLLGDLLFV RLDKEQCFFL PDDDWFCSKV
     EVTTPSGETV LFPCYRWVSD KWAVELREGK AKKVFEDQHP ILIQQRTGEL ELCHNLYRWA
     VFREGLPKMV GIDDPALLPH DARFSFTKAM DLLVRSKTAL DELKLRSLAD RKKPWTKWED
     IKRIFWFNKT MVSGYVQKHW EEDWFLGYQC LNGCNPVVVQ RCCQLPPNFP VPSCLVNPFL
     EAGSTLEKEL LKGNIYLCDY KVLDGITPNL INNRLQYMVA PLCLLYKKTS DQLVPIAIQH
     TAIGGIGLIE ILERAVQSLT YSSLCLPEDI SARGVESVPN YYYRDDGLCL WNSINRFVKG
     MVKVYYPDDN AVVKDTELQS WIKEIFTEGF QERPESEIPQ SFTSLEEVTK FVNMVVFTVS
     AQHAAVNSGL FDFSSWMPNS PSSLQWPPPI TKGSTTMSDI LKALPDINTT VRLMATTWLL
     SKQPSDFVAL GQYPWEHFIE DAPCRLILEL QEDLAALSQK IKERNAQLEL PYTYLLPELI
     ENSIAL
//
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