CP2D1_RAT
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 03-AUG-2022, entry version 168.
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 + 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; 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_153313.1.
DR AlphaFoldDB; P10633; -.
DR SMR; P10633; -.
DR IntAct; P10633; 1.
DR STRING; 10116.ENSRNOP00000041174; -.
DR BindingDB; P10633; -.
DR ChEMBL; CHEMBL2475; -.
DR iPTMnet; P10633; -.
DR PhosphoSitePlus; P10633; -.
DR PaxDb; P10633; -.
DR PRIDE; P10633; -.
DR GeneID; 266684; -.
DR KEGG; rno:266684; -.
DR UCSC; RGD:708427; rat.
DR CTD; 266684; -.
DR RGD; 708427; Cyp2d1.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P10633; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P10633; -.
DR TreeFam; TF352043; -.
DR SABIO-RK; P10633; -.
DR PRO; PR:P10633; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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: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; 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:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
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..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
