ID   F1MP67_BOVIN            Unreviewed;       490 AA.
AC   F1MP67;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Cytochrome P450 {ECO:0000256|RuleBase:RU368047};
DE            EC=1.14.14.- {ECO:0000256|RuleBase:RU368047};
GN   Name=CYP2C281 {ECO:0000313|Ensembl:ENSBTAP00000034278.4,
GN   ECO:0000313|VGNC:VGNC:110248};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000034278.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000034278.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000034278.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000034278.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000034278.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       In liver microsomes, this enzyme is involved in an NADPH-dependent
CC       electron transport pathway. It oxidizes a variety of structurally
CC       unrelated compounds, including steroids, fatty acids, and xenobiotics.
CC       {ECO:0000256|RuleBase:RU368047}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|RuleBase:RU368047};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU368047}. Microsome membrane
CC       {ECO:0000256|RuleBase:RU368047}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   RefSeq; XP_001252335.1; XM_001252334.4.
DR   RefSeq; XP_002698445.1; XM_002698399.4.
DR   AlphaFoldDB; F1MP67; -.
DR   SMR; F1MP67; -.
DR   STRING; 9913.ENSBTAP00000034278; -.
DR   PaxDb; 9913-ENSBTAP00000034278; -.
DR   Ensembl; ENSBTAT00000034383.5; ENSBTAP00000034278.4; ENSBTAG00000049496.1.
DR   GeneID; 785540; -.
DR   KEGG; bta:785540; -.
DR   CTD; 785540; -.
DR   VEuPathDB; HostDB:ENSBTAG00000049496; -.
DR   VGNC; VGNC:110248; CYP2C281.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000162654; -.
DR   HOGENOM; CLU_001570_22_3_1; -.
DR   InParanoid; F1MP67; -.
DR   OMA; SYELCFI; -.
DR   OrthoDB; 2900138at2759; -.
DR   TreeFam; TF352043; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000049496; Expressed in liver and 10 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20665; CYP2C-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24300:SF200; CYTOCHROME P450 2C70; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01686; EP450ICYP2D.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..490
FT                   /note="Cytochrome P450"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003269549"
SQ   SEQUENCE   490 AA;  55854 MW;  0E29811D722DA468 CRC64;
     MDLSVVLVIC LSILIFLFLW NQRHAKGTLP PGPTPLPIVG NILQINIKNV SKSISKLAED
     YGPVFTLYFG MKPTVVLHGY EAVKQVLIDQ SEEFSGRGSL PVADNINQGL GIIFSNGEIW
     KQTRRFSLMV LRNMGMGKRT IEHRIQEEAL CLVEALKKTN GCPCDPTFLL TYAPCNVICS
     IIFRNRFEYS DESFLTLAKY IHENATIFST PWIELYNAFP SLLHYLPGSH NTLFKNMTEQ
     RKFILEKIKE HQESLDLNNP QDFIDYFLIK MEKEKHNKQS EFTMDNLITT VWDVFTAGIE
     TTSISLKYGL LLLLKHPEVT AKVQEEINRV VGRNRSPCMQ DRSRMPYTDA VIHEIQRYID
     IVPNNLPHAA AQDIKFREYL IPKGTTILTS LTSVLHDGKE FPNPEQFDPG HFLDKSGNFK
     KSDYFMVFSA GKRVCIGEGL ARMELFLLLV SILQKFTLKP LVDPKNIDTT PLLKGVGSIP
     HFYEVCFIPV
//