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Database: UniProt
Entry: H2MRV6_ORYLA
LinkDB: H2MRV6_ORYLA
Original site: H2MRV6_ORYLA 
ID   H2MRV6_ORYLA            Unreviewed;       486 AA.
AC   H2MRV6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Lipoxygenase domain-containing protein {ECO:0000259|PROSITE:PS51393};
GN   Name=LOC110014609 {ECO:0000313|Ensembl:ENSORLP00000021490.2};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000021490.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000021490.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000021490.2,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000021490.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000021490.2};
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   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC       {ECO:0000256|RuleBase:RU003974}.
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DR   AlphaFoldDB; H2MRV6; -.
DR   Ensembl; ENSORLT00000021491.2; ENSORLP00000021490.2; ENSORLG00000030647.1.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   GeneTree; ENSGT00940000155191; -.
DR   HOGENOM; CLU_004282_3_1_1; -.
DR   TreeFam; TF105320; -.
DR   Proteomes; UP000001038; Chromosome 9.
DR   Bgee; ENSORLG00000030647; Expressed in pharyngeal gill and 2 other cell types or tissues.
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; 3.10.450.60; -; 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   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   PANTHER; PTHR11771:SF161; POLYUNSATURATED FATTY ACID LIPOXYGENASE ALOX15B; 1.
DR   Pfam; PF00305; Lipoxygenase; 2.
DR   PRINTS; PR00087; LIPOXYGENASE.
DR   PRINTS; PR00467; MAMLPOXGNASE.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601885-1};
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:UP000001038}.
FT   DOMAIN          1..486
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   BINDING         202
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   BINDING         207
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   BINDING         363
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   BINDING         486
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
SQ   SEQUENCE   486 AA;  56563 MW;  4D964F418580A663 CRC64;
     LLRWAVYKEG IPLCMEADTL KSLPPDDRYP YTRELEFNFT AVDGFWRTPF KNRFVLSDYA
     MKHWREDAFF GYQFLNGVNP MMIQRCKTLP SKFPVPLDMN FSKSQLTLRT EMMKGNIFLC
     DYNILDGVET NTINGRKQFL AAPLVLLHKN EDDEMMPIAI QLKQEPGEDN PIFFPTDSEY
     DWLLAKTYVK SADSNLHELN YHLLRTHLLA EVFAVSLQRN LPRVHPVYKL LIRHTRYTLQ
     INVLARNSEL QKISSAFVGH LNYRSLCIPD DIIDRGLEDV PNFYYRDDGL KLWNIMFVHG
     ILSFYYKTDC MVQNDAELQN WIQEIFENGF LRCNETGIPQ KFTTVAELVK FVTMVMFTCS
     AQHAAVNTGQ YDLYGWMPNG PSTMQEPPPT HKGKADEASF LSTLPDVQTT VHILATVWLL
     SMQSSDARYL HDFVEEHFTE DFPKYKVTTF QRDLIKLSED IKDRNENLKL PYTFLDPKLV
     ENSVAI
//
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