ID   CP2DG_CAVPO             Reviewed;         500 AA.
AC   Q64403; O54866;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Cytochrome P450 2D16;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIID16;
GN   Name=CYP2D16;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-38.
RC   STRAIN=13; TISSUE=Adrenal cortex;
RX   PubMed=7733969; DOI=10.1006/bbrc.1995.1617;
RA   Jiang Q., Voigt J.M., Colby H.D.;
RT   "Molecular cloning and sequencing of a guinea pig cytochrome P4502D
RT   (CYP2D16): high level expression in adrenal microsomes.";
RL   Biochem. Biophys. Res. Commun. 209:1149-1156(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hartley; TISSUE=Adrenal gland;
RA   Sun Y., Voigt J.M., Pierce J.C., Colby H.D.;
RT   "The gene sequence of a xenobiotic metabolism-related cytochrome P450
RT   isozyme (CYP2D16) in guinea pig adrenal gland.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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 at high levels in the inner zone of the
CC       adrenal cortex.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U21486; AAA68479.1; -; mRNA.
DR   EMBL; AF020345; AAB94568.1; -; Genomic_DNA.
DR   PIR; JC4153; JC4153.
DR   RefSeq; NP_001166507.1; NM_001173036.1.
DR   AlphaFoldDB; Q64403; -.
DR   SMR; Q64403; -.
DR   STRING; 10141.ENSCPOP00000016816; -.
DR   GeneID; 100169696; -.
DR   KEGG; ag:AAA68479; -.
DR   KEGG; cpoc:100169696; -.
DR   CTD; 100169696; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; Q64403; -.
DR   OrthoDB; 702827at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..500
FT                   /note="Cytochrome P450 2D16"
FT                   /id="PRO_0000051740"
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   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10634"
FT   CONFLICT        123
FT                   /note="I -> V (in Ref. 2; AAB94568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="Y -> N (in Ref. 2; AAB94568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="G -> R (in Ref. 2; AAB94568)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  55801 MW;  2429247E49BF6B24 CRC64;
     MGLLTGDALF SVAVAVAIFL LLVDLMHRRQ RWAARYPPGP VPVPGLGNLL QVDFENMAYS
     CDKLRHQFGD VFSLQFVWTP VVVVNGLLAV REALVNNSTD TSDRPTLPTN ALLGFGPKAQ
     GVIGAYYGPA WREQRRFSVS SLRNFGLGKK SLEQWVTEEA ACLCAAFTNH AGQPFCPKAL
     LNKAVCNVIS SLIYARRFDY DDPMVLRLLE FLEETLRENS SLKIQVLNSI PLLLRIPCVA
     AKVLSAQRSF IALNDKLLAE HNTGWAPDQP PRDLTDAFLT EMHKAQGNSE SSFNDENLRL
     LVSDLFGAGM VTTSVTLSWA LLLMILHPDV QRHVQEEIDE VIGQVRCPEM ADQAHMPFTN
     AVIHEVQRFA DIVPMGVPHM TSRDTEVQGF LIPKGTMLFT NLSSVLKDET VWEKPLHFHP
     GHFLDAEGRF VKREAFMPFS AGPRICLGEP LARMELFLFF TSLLQRFSFS VPEGQPRPSD
     RGAPYLVVLP SPYQLCAVLR