CP2CK_MACFA
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 03-AUG-2022, entry version 116.
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.XP_005566064.1; -.
DR GeneID; 102117212; -.
DR CTD; 1558; -.
DR eggNOG; KOG0156; Eukaryota.
DR OrthoDB; 702827at2759; -.
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 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..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