ID   CP2CK_MACFA             Reviewed;         490 AA.
AC   P33262;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   24-JAN-2024, entry version 121.
DE   RecName: Full=Cytochrome P450 2C20;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC20;
DE   AltName: Full=Cytochrome P450-MK1;
DE   AltName: Full=Cytochrome P450-MKMP13;
GN   Name=CYP2C20;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1282830; DOI=10.1016/0167-4781(92)90113-e;
RA   Komori M., Kikuchi O., Sakuma T., Funaki J., Kitada M., Kamataki T.;
RT   "Molecular cloning of monkey liver cytochrome P-450 cDNAs: similarity of
RT   the primary sequences to human cytochromes P-450.";
RL   Biochim. Biophys. Acta 1171:141-146(1992).
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 3-methylcholanthrene (3MC).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; S53046; AAB24950.1; -; mRNA.
DR   PIR; S28166; S28166.
DR   RefSeq; NP_001270692.1; NM_001283763.1.
DR   AlphaFoldDB; P33262; -.
DR   SMR; P33262; -.
DR   STRING; 9541.ENSMFAP00000035864; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   OrthoDB; 2900138at2759; -.
DR   Proteomes; UP000233100; 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   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:SF317; CYTOCHROME P450 2C8; 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 2C20"
FT                   /id="PRO_0000051709"
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;  55638 MW;  7CEC7078C2F25990 CRC64;
     MDPFVVLVLC LSFVLLFSLW RQSSGRRKLP PGPTPLPIIG NILQIDVKDI CKSFSNFSKV
     YGPVFTVYFG MNPVVVLHGY ETVKEALIDN AEEFSGRGIL PISERITNGL GIISSNGKRW
     KETRRFSLTT LRNFGMGKRS IEDRVQEEAR CLVEELRKTK ASPCDPTFIL GCAPCNVICS
     VVFQKRFDYK DENFLTLIKR FTVNFRILTS PWIQVCNNFP LLIDCFPGTH NKLLKNVALT
     KSYIREKVKE HQATLDVNNP RDFIDCFLIK MEQEKDNQQS EFTIENLVGT VADLFVAGTE
     TTSTTLRYGL LLLLKHPEVT AKVQEEIDHV IGRHRSPCMQ DRSHMPYTDA VIHEIQRYID
     LVPTGVPHAV TTDIKFRNYL IPKGTIIITL LTSVLHDDKE FPNPKIFDPG HFLDENGNFK
     KSDYFMPFSA GKRICAGEGL ARMELFLFLT TILQNFNLKS VADLKNLNTT SATRGIISLP
     PSYQICFIPV
//