ID   CP2M1_ONCMY             Reviewed;         499 AA.
AC   Q92088;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cytochrome P450 2M1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIM1;
DE   AltName: Full=LMC1;
DE   AltName: Full=Lauric acid omega-6-hydroxylase;
GN   Name=cyp2m1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Shasta; TISSUE=Liver;
RX   PubMed=9587416; DOI=10.1006/abbi.1998.0607;
RA   Yang Y.-H., Wang J.-L., Miranda C.L., Buhler D.R.;
RT   "CYP2M1: cloning, sequencing, and expression of a new cytochrome P450 from
RT   rainbow trout liver with fatty acid (omega-6)-hydroxylation activity.";
RL   Arch. Biochem. Biophys. 352:271-280(1998).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=2403346; DOI=10.1016/0006-291x(90)91179-v;
RA   Miranda C.L., Wang J.L., Henderson M.C., Williams D.E., Buhler D.R.;
RT   "Regiospecificity in the hydroxylation of lauric acid by rainbow trout
RT   hepatic cytochrome P450 isozymes.";
RL   Biochem. Biophys. Res. Commun. 171:537-542(1990).
CC   -!- FUNCTION: Has (omega-6)-hydroxylation activity toward lauric acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Microsome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: In kidney and in liver from juvenile and sexually
CC       mature trout from both sexes.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U16657; AAA62499.1; -; mRNA.
DR   AlphaFoldDB; Q92088; -.
DR   SMR; Q92088; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IMP:AgBase.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0048252; P:lauric acid metabolic process; IDA:AgBase.
DR   GO; GO:0002933; P:lipid hydroxylation; IDA:AgBase.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..499
FT                   /note="Cytochrome P450 2M1"
FT                   /id="PRO_0000051777"
FT   BINDING         441
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   499 AA;  56773 MW;  2D5C106C192ECBA2 CRC64;
     MDVLHILQTN FVSIIIGFVV IILLWMNRGK QSNSRLPPGP APIPLLGNLL RMDVKAPYKL
     YMELSKKYGS VFTVWLGSKP VVVISGYQAI KDAFVTQGEE FSGRANYPVI MTVSKGYGVL
     VSSGKRSKDL RRFSLMTLKT FGMGRRSIEE RVQEEAKMLV KAFGEYRDSV VNPKELLCNC
     VGNVICSIVF GHRFENDDPM FQLIQKAVDA YFNVLSSPIG AMYNMFPRIV WCFPGNHHEM
     FAIVNKAKVY IQEQAEIRLK TLNISEPQDF IEAFLVKMLE EKDDPNTEFN NGNMVMTAWS
     LFAAGTETTS STLRQSFLMM IKYPHIQESV QKEIDEVIGS RVPTVDDRVK MPYTDAVIHE
     VQRYMDLSPT SVPHKVMRDT EFYNYHIPEG TMVLPLLSSV LVDPKLFKNP DEFDPENFLD
     ENGVFKKNDG FFAFGVGKRA CPGEALARVE LFLFFTSVLQ RFTFTGTKPP EEINIEPACS
     SFGRLPRSYD CYIKLRTEK