ID   CP2CC_RAT               Reviewed;         490 AA.
AC   P11510;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   08-NOV-2023, entry version 145.
DE   RecName: Full=Cytochrome P450 2C12, female-specific;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC12;
DE   AltName: Full=Cytochrome P450 15-beta;
DE   AltName: Full=Cytochrome P450-UT-1;
DE   AltName: Full=Cytochrome P450-UT-I;
DE   AltName: Full=Cytochrome P450I;
GN   Name=Cyp2c12; Synonyms=Cyp2c-12, Cyp2c40;
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].
RX   PubMed=2837761; DOI=10.1073/pnas.85.12.4214;
RA   Zaphiropoulos P.G., Mode A., Stroem A., Moeller C., Fernandez C.,
RA   Gustafsson J.-A.;
RT   "cDNA cloning, sequence, and regulation of a major female-specific and
RT   growth hormone-inducible rat liver cytochrome P-450 active in 15 beta-
RT   hydroxylation of steroid sulfates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:4214-4217(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3164963;
RA   Zaphiropoulos P.G., Mode A., Stroem A., Husman B., Andersson G.,
RA   Gustafsson J.-A.;
RT   "Sequence and regulation of two growth-hormone-controlled, sex-specific
RT   isozymes of cytochrome P-450 in rat liver, P-450(15)beta and P-
RT   450(16)alpha.";
RL   Acta Med. Scand. Suppl. 723:161-167(1988).
CC   -!- FUNCTION: This P450 is active in 15-beta-hydroxylation of steroid
CC       sulfates.
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.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; J03786; AAA41005.1; -; mRNA.
DR   PIR; A32140; A32140.
DR   RefSeq; NP_113760.1; NM_031572.1.
DR   AlphaFoldDB; P11510; -.
DR   SMR; P11510; -.
DR   IntAct; P11510; 1.
DR   STRING; 10116.ENSRNOP00000015802; -.
DR   DrugBank; DB15093; Somapacitan.
DR   PaxDb; 10116-ENSRNOP00000015802; -.
DR   GeneID; 25011; -.
DR   KEGG; rno:25011; -.
DR   AGR; RGD:2470; -.
DR   CTD; 25011; -.
DR   RGD; 2470; Cyp2c12.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P11510; -.
DR   OrthoDB; 2900138at2759; -.
DR   PhylomeDB; P11510; -.
DR   PRO; PR:P11510; -.
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; IBA:GO_Central.
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:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20665; CYP2C-like; 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   PANTHER; PTHR24300:SF140; CYTOCHROME P450 2C40-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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..490
FT                   /note="Cytochrome P450 2C12, female-specific"
FT                   /id="PRO_0000051702"
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;  55919 MW;  C2B637DA69F62C82 CRC64;
     MDPFVVLVLS LSFLLLLYLW RPSPGRGKLP PGPTPLPIFG NFLQIDMKDI RQSISNFSKT
     YGPVFTLYFG SQPTVVLHGY EAVKEALIDY GEEFSGRGRM PVFEKATKGL GISFSRGNVW
     RATRHFTVNT LRSLGMGKRT IEIKVQEEAE WLVMELKKTK GSPCDPKFII GCAPCNVICS
     IIFQNRFDYK DKDFLSLIEN VNEYIKIVST PAFQVFNAFP ILLDYCPGNH KTHSKHFAAI
     KSYLLKKIKE HEESLDVSNP RDFIDYFLIQ RCQENGNQQM NYTQEHLAIL VTNLFIGGTE
     TSSLTLRFAL LLLMKYPHIT DKVQEEIGQV IGRHRSPCML DRIHMPYTNA MIHEVQRYID
     LAPNGLLHEV TCDTKFRDYF IPKGTAVLTS LTSVLHARKE FPNPEMFDPG HFLDENGNFK
     KSDYFMPFSA GKRKCVGEGL ASMELFLFLT TILQNFKLKS LSDPKDIDIN SIRSEFSSIP
     PTFQLCFIPV
//