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 02-SEP-2026, entry version 171. 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 + 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 FunCoup; P05178; 59. DR IntAct; P05178; 1. DR STRING; 10116.ENSRNOP00000051625; -. DR BindingDB; P05178; -. DR ChEMBL; CHEMBL1907986; -. DR DrugBank; DB13746; Bioallethrin. DR DrugBank; DB00266; Dicoumarol. DR PaxDb; 10116-ENSRNOP00000051625; -. DR AGR; RGD:41261854; -. DR AGR; RGD:619934; -. 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:0052741; F:(R)-limonene 6-monooxygenase activity; ISO:RGD. DR GO; GO:0018675; F:(S)-limonene 6-monooxygenase activity; ISO:RGD. DR GO; GO:0018676; F:(S)-limonene 7-monooxygenase activity; ISO:RGD. DR GO; GO:0008404; F:arachidonate 14,15-epoxygenase activity; ISO:RGD. 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; IDA: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; ISO:RGD. DR GO; GO:0008395; F:steroid hydroxylase activity; ISO:RGD. DR GO; GO:0019369; P:arachidonate metabolic process; ISO:RGD. DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central. 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:0031667; P:response to nutrient levels; IEP:RGD. 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; IDA:RGD. DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD. DR CDD; cd20665; CYP2C-like; 1. DR FunFam; 1.10.630.10:FF:000299; Cytochrome P450 2C9; 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; IPR036396; Cyt_P450_sf. DR InterPro; IPR050182; Cytochrome_P450_fam2. DR PANTHER; PTHR24300:SF384; CYTOCHROME P450 2C29-RELATED; 1. DR PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 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 //