ID   CP2C1_RABIT             Reviewed;         490 AA.
AC   P00180; Q00172;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Cytochrome P450 2C1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC1;
DE   AltName: Full=Cytochrome P-450 IIC1;
DE   AltName: Full=Cytochrome P450 PBc1;
GN   Name=CYP2C1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=2317269; DOI=10.1089/dna.1990.9.37;
RA   Zhao J., Chan G., Govind S., Bell P., Kemper B.W.;
RT   "Structure of 5' regions and expression of phenobarbital-inducible rabbit
RT   cytochrome P450IIC genes.";
RL   DNA Cell Biol. 9:37-48(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-490.
RX   PubMed=6546520; DOI=10.1021/bi00297a005;
RA   Leighton J.K., Debrunner-Vossbrinck B.A., Kemper B.;
RT   "Isolation and sequence analysis of three cloned cDNAs for rabbit liver
RT   proteins that are related to rabbit cytochrome P-450 (form 2), the major
RT   phenobarbital-inducible form.";
RL   Biochemistry 23:204-210(1984).
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   -!- INTERACTION:
CC       P00180; O15503: INSIG1; Xeno; NbExp=2; IntAct=EBI-6251821, EBI-6252425;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By phenobarbital.
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; M74199; AAA31436.1; -; Genomic_DNA.
DR   EMBL; K01522; AAA31211.1; -; mRNA.
DR   PIR; A00181; O4RBP1.
DR   AlphaFoldDB; P00180; -.
DR   SMR; P00180; -.
DR   IntAct; P00180; 2.
DR   STRING; 9986.ENSOCUP00000019969; -.
DR   PRIDE; P00180; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P00180; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..490
FT                   /note="Cytochrome P450 2C1"
FT                   /id="PRO_0000051692"
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                   /evidence="ECO:0000250"
SQ   SEQUENCE   490 AA;  55615 MW;  2054D538A83E7D17 CRC64;
     MDPVVVLGLC LSCLLLLSLW KQSYGGGKLP PGPTPFPILG NILQIGIQDI SKSFTKLSEV
     YGPVFTVYLG MKPTVVIHGY DAVKEALVDL GEEFSGRIVF PLTAKINKGY GIVFSNGKRW
     KETRRFSLMT LRDFGMGKRS IEDRVQEEAR CLVEELRKTN GSPCNPTFIL GAAPCNVICS
     VIFQNRFDYT DQDFLSLMGK LNENFKILNS PWVQMCNNFP ILIDYLPGSH NKILRNNIYI
     RNYVLEKIKE HQETLDINNP RDFIDCFLIK MEQEKDNQQS EFTIENLMTT LSDVFGAGTE
     TTSTTLRYGL LLLMKHPEVI AKVQEEIERV IGRHRSPCMQ DRSRMPYTDA TVHEIQRYIN
     LIPNNVPRAT TCNVKFRSYL IPKGTAVITS LTSMLYNDKE FPNPDRFDPG HFLDASGKFR
     KSDYFMPFST GKRVCVGEVL ARMELFLFLT AILQNFTPKP LVDPKDIDTT PLVSGLGRVP
     PLYQLSFIPA