ID   CP2D1_RAT               Reviewed;         504 AA.
AC   P10633; O35105; Q6AZ78;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 184.
DE   RecName: Full=Cytochrome P450 2D1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIID1;
DE   AltName: Full=Cytochrome P450-CMF1A;
DE   AltName: Full=Cytochrome P450-DB1;
DE   AltName: Full=Cytochrome P450-UT-7;
DE   AltName: Full=Debrisoquine 4-hydroxylase;
GN   Name=Cyp2d1; Synonyms=Cyp2d-1, Cyp2d9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3582092; DOI=10.1089/dna.1987.6.149;
RA   Gonzalez F.J., Matsunaga T., Nagata K., Meyer U.A., Nebert D.W.,
RA   Pastewka J., Kozak C.A., Gillette J., Gelboin H.V., Hardwick J.P.;
RT   "Debrisoquine 4-hydroxylase: characterization of a new P450 gene subfamily,
RT   regulation, chromosomal mapping, and molecular analysis of the DA rat
RT   polymorphism.";
RL   DNA 6:149-161(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2819073; DOI=10.1021/bi00444a030;
RA   Matsunaga E., Zanger U.M., Hardwick J.P., Gelboin H.V., Meyer U.A.,
RA   Gonzalez F.J.;
RT   "The CYP2D gene subfamily: analysis of the molecular basis of the
RT   debrisoquine 4-hydroxylase deficiency in DA rats.";
RL   Biochemistry 28:7349-7355(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3190674; DOI=10.1016/s0006-291x(88)80896-9;
RA   Ishida N., Tawaragi Y., Inuzuka C., Sugita O., Kubota I., Nakazato H.,
RA   Noguchi T., Sassa S.;
RT   "Four species of cDNAs for cytochrome P450 isozymes immunorelated to P450C-
RT   M/F encode for members of P450IID subfamily, increasing the number of
RT   members within the subfamily.";
RL   Biochem. Biophys. Res. Commun. 156:681-688(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=9434752; DOI=10.1006/abbi.1997.0402;
RA   Wan J., Imaoka S., Chow T., Hiroi T., Yabusaki Y., Funae Y.;
RT   "Expression of four rat CYP2D isoforms in Saccharomyces cerevisiae and
RT   their catalytic specificity.";
RL   Arch. Biochem. Biophys. 348:383-390(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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 + reduced [NADPH--hemoprotein reductase] +
CC         O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O +
CC         H(+); 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; M16654; AAA41054.1; -; mRNA.
DR   EMBL; J02867; AAA41001.1; -; mRNA.
DR   EMBL; M22328; AAA41043.1; -; mRNA.
DR   EMBL; AB008422; BAA23122.1; -; mRNA.
DR   EMBL; BC078696; AAH78696.1; -; mRNA.
DR   PIR; A26822; A26822.
DR   RefSeq; NP_695225.1; NM_153313.2.
DR   AlphaFoldDB; P10633; -.
DR   SMR; P10633; -.
DR   FunCoup; P10633; 51.
DR   IntAct; P10633; 1.
DR   BindingDB; P10633; -.
DR   ChEMBL; CHEMBL2475; -.
DR   iPTMnet; P10633; -.
DR   PhosphoSitePlus; P10633; -.
DR   GeneID; 266684; -.
DR   KEGG; rno:266684; -.
DR   UCSC; RGD:708427; rat.
DR   AGR; RGD:708427; -.
DR   CTD; 266684; -.
DR   RGD; 708427; Cyp2d1.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P10633; -.
DR   OrthoDB; 47901at9989; -.
DR   PhylomeDB; P10633; -.
DR   SABIO-RK; P10633; -.
DR   PRO; PR:P10633; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0070330; F:aromatase activity; ISO:RGD.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
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; ISO:RGD.
DR   GO; GO:0019369; P:arachidonate metabolic process; IBA:GO_Central.
DR   GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR   GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
DR   CDD; cd20663; CYP2D; 1.
DR   FunFam; 1.10.630.10:FF:000004; cytochrome P450 2D15 isoform X1; 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   InterPro; IPR050182; Cytochrome_P450_fam2.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   PANTHER; PTHR24300:SF119; CYTOCHROME P450-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..504
FT                   /note="Cytochrome P450 2D1"
FT                   /id="PRO_0000051728"
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   CONFLICT        123..124
FT                   /note="IL -> VF (in Ref. 3; AAA41043)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="Q -> R (in Ref. 3; AAA41043)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="F -> I (in Ref. 3; AAA41043, 4; BAA23122 and 5;
FT                   AAH78696)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   504 AA;  57175 MW;  2F9AD87B4EF327DC CRC64;
     MELLNGTGLW SMAIFTVIFI LLVDLMHRRH RWTSRYPPGP VPWPVLGNLL QVDLSNMPYS
     LYKLQHRYGD VFSLQKGWKP MVIVNRLKAV QEVLVTHGED TADRPPVPIF KCLGVKPRSQ
     GVILASYGPE WREQRRFSVS TLRTFGMGKK SLEEWVTKEA GHLCDAFTAQ AGQSINPKAM
     LNKALCNVIA SLIFARRFEY EDPYLIRMVK LVEESLTEVS GFIPEVLNTF PALLRIPGLA
     DKVFQGQKTF MALLDNLLAE NRTTWDPAQP PRNLTDAFLA EVEKAKGNPE SSFNDENLRM
     VVVDLFTAGM VTTATTLTWA LLLMILYPDV QRRVQQEIDE VIGQVRCPEM TDQAHMPYTN
     AVIHEVQRFG DIAPLNLPRF TSCDIEVQDF VIPKGTTLII NLSSVLKDET VWEKPHRFHP
     EHFLDAQGNF VKHEAFMPFS AGRRACLGEP LARMELFLFF TCLLQRFSFS VPVGQPRPST
     HGFFAFPVAP LPYQLCAVVR EQGL
//