ID   CP2DA_RAT               Reviewed;         504 AA.
AC   P12939;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Cytochrome P450 2D10;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIID10;
DE   AltName: Full=Cytochrome P450-CMF1B;
DE   AltName: Full=Cytochrome P450-DB5;
DE   AltName: Full=Debrisoquine 4-hydroxylase;
GN   Name=Cyp2d10; Synonyms=Cyp2d-10, Cyp2d5;
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2771656; DOI=10.1093/nar/17.15.6407;
RA   Ishida N., Inuzuka C., Tawaragi Y., Sugita O., Nakazato H., Noguchi T.,
RA   Sassa S., Kappas A.;
RT   "Cytochrome P450CMF cDNA: nucleotide sequence of P450CMF1b.";
RL   Nucleic Acids Res. 17:6407-6407(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=2107330; DOI=10.1007/bf02099942;
RA   Matsunaga E., Umeno M., Gonzalez F.J.;
RT   "The rat P450 IID subfamily: complete sequences of four closely linked
RT   genes and evidence that gene conversions maintained sequence homogeneity at
RT   the heme-binding region of the cytochrome P450 active site.";
RL   J. Mol. Evol. 30:155-169(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-504.
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   [5]
RP   GLYCOSYLATION AT SER-382.
RX   PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA   Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT   "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT   mitochondria by combination of mass spectrometry and immunological
RT   methods.";
RL   PLoS ONE 8:E76399-E76399(2013).
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; J02869; AAA41003.1; -; mRNA.
DR   EMBL; M25143; AAA41034.1; -; mRNA.
DR   EMBL; X52030; CAA36272.1; -; Genomic_DNA.
DR   EMBL; M22329; AAA41045.1; -; mRNA.
DR   PIR; S09611; O4RTD5.
DR   RefSeq; NP_775426.1; NM_173304.2.
DR   AlphaFoldDB; P12939; -.
DR   SMR; P12939; -.
DR   IntAct; P12939; 1.
DR   STRING; 10116.ENSRNOP00000040266; -.
DR   GlyGen; P12939; 1 site.
DR   iPTMnet; P12939; -.
DR   PhosphoSitePlus; P12939; -.
DR   PaxDb; P12939; -.
DR   PRIDE; P12939; -.
DR   GeneID; 286963; -.
DR   KEGG; rno:286963; -.
DR   UCSC; RGD:628630; rat.
DR   CTD; 286963; -.
DR   RGD; 628630; Cyp2d5.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P12939; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; P12939; -.
DR   PRO; PR:P12939; -.
DR   Proteomes; UP000002494; Unplaced.
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:0004497; F:monooxygenase activity; TAS: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: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   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Heme; Iron; Membrane; Metal-binding;
KW   Microsome; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..504
FT                   /note="Cytochrome P450 2D10"
FT                   /id="PRO_0000051736"
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   CARBOHYD        382
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000269|PubMed:24098488"
SQ   SEQUENCE   504 AA;  57076 MW;  F308EE06F2605DFE CRC64;
     MELLNGTGLW PMAIFTVIFI LLVDLMHRHQ RWTSRYPPGP VPWPVLGNLL QVDPSNMPYS
     MYKLQHRYGD VFSLQMGWKP MVIVNRLKAV QEVLVTHGED TADRPPVPIF KCLGVKPRSQ
     GVVFASYGPE WREQRRFSVS TLRTFGMGKK SLEEWVTKEA GHLCDAFTAQ NGRSINPKAM
     LNKALCNVIA SLIFARRFEY EDPYLIRMLT LVEESLIEVS GFIPEVLNTF PALLRIPGLA
     DKVFQGQKTF MAFLDNLLAE NRTTWDPAQP PRNLTDAFLA EVEKAKGNPE SSFNDENLRM
     VVVDLFTAGM VTTATTLTWA LLLMILYPDV QRRVQQEIDE VIGQVRCPEM TDQAHMPYTN
     AVIHEVQRFG DIAPLNLPRI TSCDIEVQDF VIPKGTTLII NLSSVLKDET VWEKPLRFHP
     EHFLDAQGNF VKHEAFMPFS AGRRACLGEP LARMELFLFF TCLLQHFSFS VPAGQPRPST
     LGNFAISVAP LPYQLCAAVR EQGH