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Cytochrome P450 2D4 (EC 1.14.14.1) (CYPIID18) (CYPIID4) (Cytochrome P450 2D-29) (Cytochrome P450 2D-35) (Cytochrome P450 2D18) (Cytochrome P450-CMF3) (Cytochrome P450-DB4) (Debrisoquine 4-hydroxylase)

 CP2D4_RAT               Reviewed;         500 AA.
Q64680; O35107; P13108; Q566D3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 133.
RecName: Full=Cytochrome P450 2D4;
EC=1.14.14.1;
AltName: Full=CYPIID18;
AltName: Full=CYPIID4;
AltName: Full=Cytochrome P450 2D-29;
AltName: Full=Cytochrome P450 2D-35;
AltName: Full=Cytochrome P450 2D18;
AltName: Full=Cytochrome P450-CMF3;
AltName: Full=Cytochrome P450-DB4;
AltName: Full=Debrisoquine 4-hydroxylase;
Name=Cyp2d4; Synonyms=Cyp2d-18, Cyp2d-4, Cyp2d18;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=2107330; DOI=10.1007/BF02099942;
Matsunaga E., Umeno M., Gonzalez F.J.;
"The rat P450 IID subfamily: complete sequences of four closely linked
genes and evidence that gene conversions maintained sequence
homogeneity at the heme-binding region of the cytochrome P450 active
site.";
J. Mol. Evol. 30:155-169(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=7733922; DOI=10.1006/bbrc.1995.1534;
Kawashima H., Strobel H.W.;
"cDNA cloning of a novel rat brain cytochrome P450 belonging to the
CYP2D subfamily.";
Biochem. Biophys. Res. Commun. 209:535-540(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9434752; DOI=10.1006/abbi.1997.0402;
Wan J., Imaoka S., Chow T., Hiroi T., Yabusaki Y., Funae Y.;
"Expression of four rat CYP2D isoforms in Saccharomyces cerevisiae and
their catalytic specificity.";
Arch. Biochem. Biophys. 348:383-390(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 177-500.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=3190674; DOI=10.1016/S0006-291X(88)80896-9;
Ishida N., Tawaragi Y., Inuzuka C., Sugita O., Kubota I., Nakazato H.,
Noguchi T., Sassa S.;
"Four species of cDNAs for cytochrome P450 isozymes immunorelated to
P450C-M/F encode for members of P450IID subfamily, increasing the
number of members within the subfamily.";
Biochem. Biophys. Res. Commun. 156:681-688(1988).
-!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
monooxygenases. In liver microsomes, this enzyme is involved in an
NADPH-dependent electron transport pathway. It oxidizes a variety
of structurally unrelated compounds, including steroids, fatty
acids, and xenobiotics.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
-!- TISSUE SPECIFICITY: Brain.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X52029; CAA36271.1; -; Genomic_DNA.
EMBL; U48220; AAC52883.1; -; mRNA.
EMBL; U48219; AAC52882.1; -; mRNA.
EMBL; AB008425; BAA23125.1; -; mRNA.
EMBL; BC093609; AAH93609.1; -; mRNA.
EMBL; M22331; AAA41052.1; -; mRNA.
RefSeq; NP_612524.1; NM_138515.2.
UniGene; Rn.26060; -.
ProteinModelPortal; Q64680; -.
SMR; Q64680; -.
STRING; 10116.ENSRNOP00000011880; -.
ChEMBL; CHEMBL2304403; -.
PaxDb; Q64680; -.
PRIDE; Q64680; -.
Ensembl; ENSRNOT00000011880; ENSRNOP00000011880; ENSRNOG00000032261.
GeneID; 171522; -.
KEGG; rno:171522; -.
UCSC; RGD:620640; rat.
CTD; 171522; -.
RGD; 620640; Cyp2d4.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00900000140799; -.
HOVERGEN; HBG015789; -.
InParanoid; Q64680; -.
KO; K07414; -.
OMA; AFNADDY; -.
OrthoDB; EOG091G0BT8; -.
PhylomeDB; Q64680; -.
TreeFam; TF352043; -.
Reactome; R-RNO-211935; Fatty acids.
Reactome; R-RNO-211958; Miscellaneous substrates.
Reactome; R-RNO-211981; Xenobiotics.
Reactome; R-RNO-211999; CYP2E1 reactions.
Reactome; R-RNO-9027307; Biosynthesis of maresin-like SPMs.
PRO; PR:Q64680; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000032261; -.
Genevisible; Q64680; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0008391; F:arachidonic acid monooxygenase activity; IDA:RGD.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
GO; GO:0004509; F:steroid 21-monooxygenase activity; IMP:RGD.
GO; GO:0019369; P:arachidonic acid metabolic process; IDA:RGD.
GO; GO:0042416; P:dopamine biosynthetic process; IDA:RGD.
GO; GO:0042417; P:dopamine metabolic process; IDA:RGD.
GO; GO:0017144; P:drug metabolic process; IDA:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0006587; P:serotonin biosynthetic process from tryptophan; IDA:RGD.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR01686; EP450ICYP2D.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
2: Evidence at transcript level;
Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane;
Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
Reference proteome.
CHAIN 1 500 Cytochrome P450 2D4.
/FTId=PRO_0000051742.
METAL 446 446 Iron (heme axial ligand). {ECO:0000250}.
CONFLICT 327 327 R -> H (in Ref. 1; CAA36271, 3; BAA23125
and 5; AAA41052). {ECO:0000305}.
CONFLICT 400 400 I -> T (in Ref. 1; CAA36271, 3; BAA23125
and 5; AAA41052). {ECO:0000305}.
CONFLICT 473 473 A -> T (in Ref. 1; CAA36271 and 5;
AAA41052). {ECO:0000305}.
CONFLICT 480 480 N -> D (in Ref. 1; CAA36271 and 5;
AAA41052). {ECO:0000305}.
CONFLICT 483 483 V -> I (in Ref. 1; CAA36271 and 5;
AAA41052). {ECO:0000305}.
SEQUENCE 500 AA; 56684 MW; 9848A8BE5ABA09C5 CRC64;
MRMPTGSELW PIAIFTIIFL LLVDLMHRRQ RWTSRYPPGP VPWPVLGNLL QIDFQNMPAG
FQKLRCRFGD LFSLQLAFES VVVLNGLPAL REALVKYSED TADRPPLHFN DQSGFGPRSQ
GVVLARYGPA WRQQRRFSVS TFRHFGLGKK SLEQWVTEEA RCLCAAFADH SGFPFSPNTL
LDKAVCNVIA SLLFACRFEY NDPRFIRLLD LLKDTLEEES GFLPMLLNVF PMLLHIPGLL
GKVFSGKKAF VAMLDELLTE HKVTWDPAQP PRDLTDAFLA EVEKAKGNPE SSFNDENLRV
VVADLFMAGM VTTSTTLTWA LLFMILRPDV QCRVQQEIDE VIGQVRRPEM ADQARMPFTN
AVIHEVQRFA DILPLGVPHK TSRDIEVQGF LIPKGTTLII NLSSVLKDET VWEKPLRFHP
EHFLDAQGNF VKHEAFMPFS AGRRACLGEP LARMELFLFF TCLLQRFSFS VPAGQPRPSN
YGVFGALTTP RPYQLCASPR


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