ID   CP2C2_RABIT             Reviewed;         490 AA.
AC   P00181; Q28683;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Cytochrome P450 2C2;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC2;
DE   AltName: Full=Cytochrome P450 PBc2;
DE   AltName: Full=Cytochrome P450 PHP2;
DE   AltName: Full=Laurate omega-1 hydroxylase;
GN   Name=CYP2C2;
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 [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2831965; DOI=10.1021/bi00401a014;
RA   Imai Y., Komori M., Sato R.;
RT   "Comparison of primary structures deduced from cDNA nucleotide sequences
RT   for various forms of liver microsomal cytochrome P-450 from phenobarbital-
RT   treated rabbits.";
RL   Biochemistry 27:80-88(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 12-490.
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX   PubMed=3780371; DOI=10.1089/dna.1986.5.371;
RA   Govind S., Bell P.A.;
RT   "Structure of genes in the cytochrome P-450PBc subfamily: conservation of
RT   intron locations in the phenobarbital-inducible family.";
RL   DNA 5:371-382(1986).
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       In the epoxidation of arachidonic acid it generates only 14,15- and
CC       11,12-cis-epoxyeicosatrienoic acids.
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       P00181; O15503: INSIG1; Xeno; NbExp=3; IntAct=EBI-4320576, EBI-6252425;
CC       P00181; O00264: PGRMC1; Xeno; NbExp=6; IntAct=EBI-4320576, EBI-1045534;
CC       P00181; P16435: POR; Xeno; NbExp=4; IntAct=EBI-4320576, EBI-726554;
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}.
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DR   EMBL; M19137; AAA31217.1; -; mRNA.
DR   EMBL; K01521; AAA31210.1; -; mRNA.
DR   EMBL; M14955; AAA31208.1; -; Genomic_DNA.
DR   PIR; A27718; O4RBP2.
DR   RefSeq; NP_001164584.1; NM_001171113.1.
DR   AlphaFoldDB; P00181; -.
DR   SMR; P00181; -.
DR   BioGRID; 1173522; 4.
DR   IntAct; P00181; 27.
DR   STRING; 9986.ENSOCUP00000013127; -.
DR   GeneID; 100328924; -.
DR   KEGG; ocu:100328924; -.
DR   CTD; 100328924; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P00181; -.
DR   OrthoDB; 702827at2759; -.
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 2C2"
FT                   /id="PRO_0000051693"
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   CONFLICT        17
FT                   /note="P -> L (in Ref. 2; AAA31210 and 3; AAA31208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471
FT                   /note="P -> L (in Ref. 2; AAA31210)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   490 AA;  55776 MW;  C105A6C6F3687E23 CRC64;
     MDLVVVLGLC LSCLLLPSLW KQSHGGGKLP PGPTPFPILG NVLQLDFKDL SKSLTNLSKV
     YGPVFTVYLG MKPTVVVHGY EAVKEALVDL GHELSGRSRF LVTAKLNKGF GVIFSNGKRW
     TETRRFSLMT LRNFGMGKRS IEERVQEEAH CLVEELRKTN ASPCDPTFIL GAAPCNVICS
     VIFQNRFDYT DQDFLSLMGK FNENFKILNS PWVQFCNCFP ILFDYFPGSH RKAVKNIFYV
     KNYITEQIKE HQKSLDINNP RDFIDCFLIK MEQEKCNQQS EFTIENLLTT VSDVFMAGTE
     TTSTTLRYGL LLLMKHPEVI AKVQEEIERV IGRHRSPCMQ DRSRMPYTDA TVHEIQRYIN
     LIPNNVPHTT ICNLKFRNYL IPKGTDVLTS LSSVLHDDKE FPNPDRFDPG HFLDASGNFR
     KSDYFMPFST GKRVCVGEAL ARMELFLFLT AILQNFTPKP LVNPNNVDEN PFSSGIVRVP
     PLYRVSFIPV