CP2C7_RAT
ID CP2C7_RAT Reviewed; 490 AA.
AC P05179; Q63706;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cytochrome P450 2C7;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIC7;
DE AltName: Full=Cytochrome P450F;
DE AltName: Full=PTF1;
GN Name=Cyp2c7; Synonyms=Cyp2c-7;
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 [MRNA].
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 [GENOMIC DNA] OF 1-66.
RC STRAIN=Sprague-Dawley;
RA Stroem A., Nilsson A.G., Zaphiropoulos P.G.;
RT "5' flanking sequence of the gene for rat cytochrome p-450f.";
RL Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-56, AND INDUCTION.
RX PubMed=2385231;
RA Westin S., Stroem A., Gustafsson J.-A., Zaphiropoulos P.G.;
RT "Growth hormone regulation of the cytochrome P-450IIC subfamily in the rat:
RT inductive, repressive, and transcriptional effects on P-450f (IIC7) and P-
RT 450PB1 (IIC6) gene expression.";
RL Mol. Pharmacol. 38:192-197(1990).
RN [4]
RP PROTEIN SEQUENCE OF 1-23.
RC TISSUE=Liver;
RX PubMed=3308889; DOI=10.1016/s0021-9258(18)47940-9;
RA Favreau L.V., Malchoff D.M., Mole J.E., Schenkman J.B.;
RT "Responses to insulin by two forms of rat hepatic microsomal cytochrome P-
RT 450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes.";
RL J. Biol. Chem. 262:14319-14326(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-490.
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 [6]
RP NUCLEOTIDE SEQUENCE OF 87-490.
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 [7]
RP METHYLATION AT ARG-144, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15047867; DOI=10.1091/mbc.e04-02-0101;
RA Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
RA Yates J.R. III, Howell K.E.;
RT "Organellar proteomics reveals Golgi arginine dimethylation.";
RL Mol. Biol. Cell 15:2907-2919(2004).
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: By growth hormone. P450 can be induced to high levels in
CC liver and other tissues by various foreign compounds, including drugs,
CC pesticides, and carcinogens. {ECO:0000269|PubMed:2385231}.
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; M18335; AAA41036.1; -; mRNA.
DR EMBL; X12595; CAA31108.1; -; Genomic_DNA.
DR EMBL; M31031; AAA41058.1; -; mRNA.
DR PIR; B28516; B28516.
DR RefSeq; NP_058854.1; NM_017158.2.
DR AlphaFoldDB; P05179; -.
DR SMR; P05179; -.
DR IntAct; P05179; 2.
DR STRING; 10116.ENSRNOP00000045029; -.
DR iPTMnet; P05179; -.
DR PhosphoSitePlus; P05179; -.
DR PaxDb; P05179; -.
DR PRIDE; P05179; -.
DR GeneID; 29298; -.
DR KEGG; rno:29298; -.
DR CTD; 29298; -.
DR RGD; 620379; Cyp2c7.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P05179; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P05179; -.
DR PRO; PR:P05179; -.
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; IDA: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:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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 Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Methylation; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Cytochrome P450 2C7"
FT /id="PRO_0000051698"
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 144
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:15047867"
FT CONFLICT 28
FT /note="K -> E (in Ref. 5; AAA41058)"
FT /evidence="ECO:0000305"
FT CONFLICT 57..65
FT /note="FSKTYGPVF -> VSIVGDPVI (in Ref. 2; CAA31108)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="L -> V (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="N -> I (in Ref. 5; AAA41058 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="N -> T (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="Q -> H (in Ref. 5; AAA41058)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..352
FT /note="MI -> HD (in Ref. 5; AAA41058)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..385
FT /note="KGT -> RRA (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 408..411
FT /note="DPGH -> VPWP (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="P -> A (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 56187 MW; 0FBACF3E9C6ABAA5 CRC64;
MDLVTFLVLT LSSLILLSLW RQSSRRRKLP PGPTPLPIIG NFLQIDVKNI SQSLTKFSKT
YGPVFTLYLG SQPTVILHGY EAIKEALIDN GEKFSGRGSY PMNENVTKGF GIVFSNGNRW
KEMRRFTIMN FRNLGIGKRN IEDRVQEEAQ CLVEELRKTK GSPCDPSLIL NCAPCNVICS
ITFQNHFDYK DKEMLTFMEK VNENLKIMSS PWMQVCNSFP SLIDYFPGTH HKIAKNINYM
KSYLLKKIEE HQESLDVTNP RDFVDYYLIK QKQANNIEQS EYSHENLTCS IMDLIGAGTE
TMSTTLRYAL LLLMKYPHVT AKVQEEIDRV IGRHRSPCMQ DRKHMPYTDA MIHEVQRFIN
FVPTNLPHAV TCDIKFRNYL IPKGTKVLTS LTSVLHDSKE FPNPEMFDPG HFLDENGNFK
KSDYFLPFSA GKRACVGEGL ARMQLFLFLT TILQNFNLKS LVHPKDIDTM PVLNGFASLP
PTYQLCFIPS
