ID   CP2CG_RABIT             Reviewed;         487 AA.
AC   P15123;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Cytochrome P450 2C16;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC16;
GN   Name=CYP2C16;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2326187; DOI=10.1093/nar/18.6.1429;
RA   Hassett C., Omiecinski C.J.;
RT   "Sequence and gene expression of rabbit cytochrome P450 IIC16: comparison
RT   to highly related family members.";
RL   Nucleic Acids Res. 18:1429-1434(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 414-487.
RX   PubMed=3426576; DOI=10.1016/0006-291x(87)90370-6;
RA   Hassett C., Omiecinski C.J.;
RT   "Use of a conserved consensus oligomer in the identification of cytochrome
RT   P-450 mRNAs.";
RL   Biochem. Biophys. Res. Commun. 149:326-333(1987).
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   -!- TISSUE SPECIFICITY: Expressed constitutively in liver, lung, testes,
CC       and kidney.
CC   -!- INDUCTION: By phenobarbital in each tissue with the exception of the
CC       kidney.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M29661; AAA31227.1; -; mRNA.
DR   EMBL; M29968; AAA31226.1; -; mRNA.
DR   EMBL; M18376; AAA31215.1; -; mRNA.
DR   PIR; S12765; O4RBC6.
DR   RefSeq; NP_001164593.1; NM_001171122.1.
DR   AlphaFoldDB; P15123; -.
DR   SMR; P15123; -.
DR   PRIDE; P15123; -.
DR   GeneID; 100328938; -.
DR   KEGG; ocu:100328938; -.
DR   CTD; 100328938; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_22_3_1; -.
DR   InParanoid; P15123; -.
DR   OrthoDB; 702827at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..487
FT                   /note="Cytochrome P450 2C16"
FT                   /id="PRO_0000051706"
FT   BINDING         432
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"
SQ   SEQUENCE   487 AA;  55542 MW;  F282245DA3CB90A2 CRC64;
     MDPVVVLVLG LCCLLLLSHW KQNSGRGKLP PGPTPFPIIG NILQIDAKDI SKSLTKFSER
     YGPVFTVYLG MKPAVVLHGY QAVKEALVDL GEEFAGRGSF PMLDKVSKGL GIVFTNGKRW
     KEIRRFSLMT LRNFGMGKRS IEDRVQEEAR CLVEELRKTN ASPCDPTFIL GCAPCNVICS
     IIFHNRFDYK DEEFLKLLEK FNENVRILSS PWLQVCNNFP ALIDYLPGSH KTLLKNSDYV
     KNFIMEKVKE HQKFLDVNNP RDFIDCFLIK MEQENHLEFT LESLVTTVFD LFGAGTETTS
     TTLRYSLLLL LKHPEVADKV QEEIERVIGR HRSPCMQDRS RMPYTDAVIH EIQRFIDLVP
     NNLPHTVTRD IKFRNYFIPK GTDIMTSLTS VLHDEKAFPN PKVFDPGHFL DESGNFKKSD
     YFMPFSAGKR ICVGEALARM ELFLFLTSIL QNFKLQSLVE PKDLDITAVL NGFVSVPPSF
     QLCFIPV