CP2C6_RAT
ID CP2C6_RAT Reviewed; 490 AA.
AC P05178;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cytochrome P450 2C6;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIC6;
DE AltName: Full=Cytochrome P450 PB1;
DE AltName: Full=PTF2;
GN Name=Cyp2c6; Synonyms=Cyp2c-6;
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.
RC TISSUE=Liver;
RX PubMed=3335521; DOI=10.1016/s0021-9258(19)35409-2;
RA Kimura H., Yoshioka H., Sogawa K., Sakai Y., Fujii-Kuriyama Y.;
RT "Complementary DNA cloning of cytochrome P-450s related to P-450(M-1) from
RT the complementary DNA library of female rat livers. Predicted primary
RT structures for P-450f, PB-1, and PB-1-related protein with a bizarre
RT replacement block and their mode of transcriptional expression.";
RL J. Biol. Chem. 263:701-707(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-490.
RX PubMed=3015936; DOI=10.1016/s0021-9258(18)67437-x;
RA Gonzalez F.J., Kimura S., Song B.-J., Pastewka J., Gelboin H.V.,
RA Hardwick J.P.;
RT "Sequence of two related P-450 mRNAs transcriptionally increased during rat
RT development. An R.dre.1 sequence occupies the complete 3' untranslated
RT region of a liver mRNA.";
RL J. Biol. Chem. 261:10667-10672(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 132-267.
RX PubMed=3801454; DOI=10.1021/bi00372a028;
RA Friedberg T., Waxman D.J., Atchison M., Kumar A., Haaparanta T.,
RA Raphael C., Adesnik M.;
RT "Isolation and characterization of cDNA clones for cytochromes P-450
RT immunochemically related to rat hepatic P-450 form PB-1.";
RL Biochemistry 25:7975-7983(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX PubMed=3399405; DOI=10.1093/nar/16.13.6249;
RA Umeno M., Matsunaga E., Morris S., Gelboin H.V., Gonzalez F.J.;
RT "Sequence of the 5' end of the developmentally regulated rat P450 PB1
RT (P450IIC6) gene.";
RL Nucleic Acids Res. 16:6249-6249(1988).
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; K03501; AAA41066.1; -; mRNA.
DR EMBL; M13711; AAA41065.1; -; mRNA.
DR EMBL; X06712; CAA29899.1; -; Genomic_DNA.
DR PIR; S00955; A25954.
DR AlphaFoldDB; P05178; -.
DR SMR; P05178; -.
DR IntAct; P05178; 1.
DR STRING; 10116.ENSRNOP00000051625; -.
DR ChEMBL; CHEMBL1907986; -.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB00266; Dicoumarol.
DR PaxDb; P05178; -.
DR PRIDE; P05178; -.
DR RGD; 619934; Cyp2c6.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P05178; -.
DR PhylomeDB; P05178; -.
DR SABIO-RK; P05178; -.
DR PRO; PR:P05178; -.
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:0008405; F:arachidonic acid 11,12-epoxygenase activity; ISO:RGD.
DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; ISO:RGD.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0020037; F:heme binding; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; ISO:RGD.
DR GO; GO:0004497; F:monooxygenase activity; ISO:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; ISO: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; ISO:RGD.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISO:RGD.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0046483; P:heterocycle metabolic process; ISO:RGD.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:RGD.
DR GO; GO:0016098; P:monoterpenoid metabolic process; ISO:RGD.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW Microsome; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..490
FT /note="Cytochrome P450 2C6"
FT /id="PRO_0000051697"
FT BINDING 435
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 MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT CONFLICT 133
FT /note="N -> D (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="W -> S (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="D -> N (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 56003 MW; 42B3AAF53CFBAF8D CRC64;
MDLVMLLVLT LTCLILLSIW RQSSGRGKLP PGPIPLPIIG NIFQLNVKNI TQSLTSFSKV
YGPVFTLYFG TKPTVILHGY EAVKEALIDH GEEFAERGSF PVAEKINKDL GIVFSHGNRW
KEIRRFTLTT LRNLGMGKRN IEDRVQEEAR CLVEELRKTN GSPCDPTFIL GCAPCNVICS
IIFQNRFDYK DQDFLNLMEK LNENMKILSS PWTQFCSFFP VLIDYCPGSH TTLAKNVYHI
RNYLLKKIKE HQESLDVTNP RDFIDYYLIK WKQENHNPHS EFTLENLSIT VTDLFGAGTE
TTSTTLRYAL LLLLKCPEVT AKVQEEIDRV VGKHRSPCMQ DRSRMPYTDA HDHEVQRFID
LIPTNLPHAV TCDIKFRNYL IPKGTTIITS LSSVLHDSKE FPDPEIFDPG HFLDGNGKFK
KSDYFMPFSA GKRMCAGEGL ARMELFLFLT TILQNFKLKS VLHPKDIDTT PVFNGFASLP
PFYELCFIPL
