ID   CP2DE_BOVIN             Reviewed;         500 AA.
AC   Q01361; Q29454;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Cytochrome P450 2D14;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIID14;
GN   Name=CYP2D14;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1396678; DOI=10.1111/j.1432-1033.1992.tb17242.x;
RA   Tsuneoka Y., Matsuo Y., Higuchi R., Ichikawa Y.;
RT   "Characterization of the cytochrome P-450IID subfamily in bovine liver.
RT   Nucleotide sequences and microheterogeneity.";
RL   Eur. J. Biochem. 208:739-746(1992).
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   -!- 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; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: P450 can be induced to high levels in liver and other
CC       tissues by various foreign compounds, including drugs, pesticides, and
CC       carcinogens.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X68013; CAA48149.1; -; mRNA.
DR   EMBL; X68481; CAA48501.1; -; mRNA.
DR   PIR; S37284; S37284.
DR   RefSeq; NP_776954.1; NM_174529.2.
DR   AlphaFoldDB; Q01361; -.
DR   SMR; Q01361; -.
DR   STRING; 9913.ENSBTAP00000037503; -.
DR   PaxDb; 9913-ENSBTAP00000000869; -.
DR   PeptideAtlas; Q01361; -.
DR   Ensembl; ENSBTAT00000037679.5; ENSBTAP00000037503.5; ENSBTAG00000026502.5.
DR   GeneID; 282211; -.
DR   KEGG; bta:282211; -.
DR   CTD; 282211; -.
DR   VEuPathDB; HostDB:ENSBTAG00000026502; -.
DR   VGNC; VGNC:111838; CYP2D6.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000153331; -.
DR   InParanoid; Q01361; -.
DR   OMA; RYGHVWK; -.
DR   OrthoDB; 2900138at2759; -.
DR   Reactome; R-BTA-211935; Fatty acids.
DR   Reactome; R-BTA-211958; Miscellaneous substrates.
DR   Reactome; R-BTA-211981; Xenobiotics.
DR   Reactome; R-BTA-211999; CYP2E1 reactions.
DR   Reactome; R-BTA-9027307; Biosynthesis of maresin-like SPMs.
DR   Reactome; R-BTA-9749641; Aspirin ADME.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000026502; Expressed in liver and 103 other cell types or tissues.
DR   ExpressionAtlas; Q01361; baseline.
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:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20663; CYP2D; 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:SF1; CYTOCHROME P450 2D6-RELATED; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Cytochrome P450 2D14"
FT                   /id="PRO_0000051738"
FT   BINDING         446
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"
FT   CONFLICT        112
FT                   /note="H -> R (in Ref. 1; CAA48149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="R -> A (in Ref. 1; CAA48501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="L -> S (in Ref. 1; CAA48501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="D -> G (in Ref. 1; CAA48149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="F -> P (in Ref. 1; CAA48501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="K -> R (in Ref. 1; CAA48149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="E -> G (in Ref. 1; CAA48149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="R -> A (in Ref. 1; CAA48149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413
FT                   /note="E -> Q (in Ref. 1; CAA48149)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  56083 MW;  D356E8736A04C92A CRC64;
     MGLLSGDTLG PLAVALLIFL LLLDLMHRRS RWAPRYPPGP TPLPVLGNLL QVDFEDPRPS
     FNQLRRRFGN VFSLQQVWTP VVVLNGLAAV REALVYRSQD TADRPPPAVY EHLGYGPRAE
     GVILARYGDA WREQRRFSLT TLRNFGLGKK SLEQWVTEEA SCLCAAFADQ AGRPFSPMDL
     LNKAVSNVIA SLTFGCRFEY NDPRIIKLLD LTEDGLKEEF NLVRKVVEAV PVLLSIPGLA
     ARVFPAQKAF MALIDELIAE QKMTRDPTQP PRHLTDAFLD EVKEAKGNPE SSFNDENLRL
     VVADLFSAGM VTTSTTLAWA LLLMILHPDV QRRVQQEIDE VIGQVRRPEM GDQALMPFTV
     AVVHEVQRFA DIVPLGLPHM TSRDIEVQGF HIPKGTTLIT NLSSVLKDET VWEKPFRFHP
     EHFLDAQGRF VKQEAFIPFS AGRRACLGEP LARMELFLFF TSLLQHFSFS VPAGQPRPSE
     HGVFAFLVTP APYQLCAVPR
//