CP2DE_BOVIN
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 03-AUG-2022, entry version 134.
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; Q01361; -.
DR PeptideAtlas; Q01361; -.
DR PRIDE; Q01361; -.
DR Ensembl; ENSBTAT00000037679; ENSBTAP00000037503; ENSBTAG00000026502.
DR GeneID; 282211; -.
DR KEGG; bta:282211; -.
DR CTD; 282211; -.
DR VEuPathDB; HostDB:ENSBTAG00000026502; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000153331; -.
DR InParanoid; Q01361; -.
DR OMA; ETYRPIQ; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000026502; Expressed in liver and 103 other 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:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01686; EP450ICYP2D.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 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
