CP2C4_RABIT
ID CP2C4_RABIT Reviewed; 487 AA.
AC P11371;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytochrome P450 2C4;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIC4;
DE AltName: Full=Cytochrome P450 PBc4;
DE AltName: Full=P1-88;
DE AltName: Full=Progesterone 21-hydroxylase;
GN Name=CYP2C4;
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=3032948; DOI=10.1016/s0021-9258(18)45662-1;
RA Johnson E.F., Barnes H.J., Griffin K.J., Okino S., Tukey R.H.;
RT "Characterization of a second gene product related to rabbit cytochrome P-
RT 450 1.";
RL J. Biol. Chem. 262:5918-5923(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
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).
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 {ECO:0000250}.
CC Microsome membrane {ECO:0000250}.
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 -!- MISCELLANEOUS: This protein differs from other forms of cytochrome P450
CC in that it catalyzes the 21-hydroxylation of progesterone, resulting in
CC the formation of deoxycorticosterone.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; J02716; AAA31216.1; -; mRNA.
DR EMBL; M74200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A26731; A26731.
DR RefSeq; NP_001177360.1; NM_001190431.1.
DR AlphaFoldDB; P11371; -.
DR SMR; P11371; -.
DR STRING; 9986.ENSOCUP00000019521; -.
DR GeneID; 100349436; -.
DR KEGG; ocu:100349436; -.
DR CTD; 100349436; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P11371; -.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..487
FT /note="Cytochrome P450 2C4"
FT /id="PRO_0000051695"
FT BINDING 432
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"
SQ SEQUENCE 487 AA; 55387 MW; F0E7F55F7512F36A CRC64;
MDPVAGLVLG LCCLLLLSLW KQNSGRGKLP PGPTPFPIIG NILQIDVKDI SKSLTKFSER
YGPVFTVYLG MKPTVVLHGY KAVKEALVDL GEEFAGRGHF PIAEKVNKGL GIVFTNANTW
KEMRRFSLMT LRNFGMGKRS IEDRVQEEAR CLVEELRKTN ALPCDPTFIL GCAPCNVICS
VILHNRFDYK DEEFLKLMER LNENIRILSS PWLQVYNNFP ALLDYFPGIH KTLLKNADYT
KNFIMEKVKE HQKLLDVNNP RDFIDCFLIK MEKENNLEFT LGSLVIAVFD LFGAGTETTS
TTLRYSLLLL LKHPEVAARV QEEIERVIGR HRSPCMQDRS HMPYTDAVIH EIQRFIDLLP
TNLPHAVTRD VKFRNYFIPK GTDIITSLTS VLHDEKAFPN PKVFDPGHFL DESGNFKKSD
YFMPFSAGKR MCVGEGLARM ELFLFLTSIL QNFKLQSLVE PKDLDITAVV NGFVSVPPSY
QLCFIPI
