ID   CP2A8_MESAU             Reviewed;         494 AA.
AC   P24454;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Cytochrome P450 2A8;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIA8;
DE   AltName: Full=Cytochrome P450-AFB;
DE   AltName: Full=Cytochrome P450-MC1;
GN   Name=CYP2A8;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2275554; DOI=10.1016/0003-9861(90)90664-k;
RA   Lai T.S., Chiang J.Y.L.;
RT   "Cloning and characterization of two major 3-methylcholanthrene inducible
RT   hamster liver cytochrome P450s.";
RL   Arch. Biochem. Biophys. 283:429-439(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2502109; DOI=10.1016/0006-291x(89)91991-8;
RA   Fukuhara M., Nagata K., Mizokami K., Yamazoe Y., Takanaka A., Kato R.;
RT   "Complete cDNA sequence of a major 3-methylcholanthrene-inducible
RT   cytochrome P-450 isozyme (P-450AFB) of Syrian hamsters with high activity
RT   toward aflatoxin B1.";
RL   Biochem. Biophys. Res. Commun. 162:265-272(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-15.
RC   TISSUE=Liver;
RX   PubMed=2391346; DOI=10.1093/oxfordjournals.jbchem.a123133;
RA   Koga N., Ariyoshi N., Nakashima H., Yoshimura H.;
RT   "Purification and characterization of two forms of 2,3,4,7,8-
RT   pentachlorodibenzofuran-inducible cytochrome P-450 in hamster liver.";
RL   J. Biochem. 107:826-833(1990).
CC   -!- FUNCTION: Highly active in 7-ethoxycoumarin O-deethylation, and
CC       benzphetamine N-demethylation; moderately active in testosterone 7-
CC       alpha-hydroxylation, ethylmorphine N-demethylation, p-nitroanisole O-
CC       demethylation; and only slightly active in benzopyrene 3-hydroxylation,
CC       7-ethoxyresorufin O-deethylation, testosterone 2-alpha-hydroxylation
CC       and testosterone 17-oxidation. Competent in the metabolic activation of
CC       aflatoxin B1.
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   -!- TISSUE SPECIFICITY: Liver.
CC   -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M63788; AAA37068.1; -; mRNA.
DR   EMBL; M27906; AAA37084.1; -; mRNA.
DR   PIR; A33293; A33293.
DR   RefSeq; NP_001268512.1; NM_001281583.1.
DR   AlphaFoldDB; P24454; -.
DR   SMR; P24454; -.
DR   STRING; 10036.ENSMAUP00000001731; -.
DR   GeneID; 101825889; -.
DR   KEGG; ag:AAA37068; -.
DR   KEGG; maua:101825889; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   OrthoDB; 2900138at2759; -.
DR   Proteomes; UP000189706; 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; cd20668; CYP2A; 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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   PANTHER; PTHR24300:SF103; CYTOCHROME P450-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01684; EP450ICYP2A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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; Microsome; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..494
FT                   /note="Cytochrome P450 2A8"
FT                   /id="PRO_0000051671"
FT   BINDING         439
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"
FT   CONFLICT        417
FT                   /note="S -> L (in Ref. 2; AAA37084)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  57387 MW;  16816672AA4B112B CRC64;
     MLVSGMLLVV VLTCLSVMII MSVWRQRRLL RKMPPGPTPL PFIGNFLELD TEKFYDCLSK
     MRERYGPVFT IHLGPRPAVM LWGYDAVKEA LIDQAEELSD RGEQAFFDWF FKGYGVVFSS
     GERAKQLRRF SIATLRDFGF GKRGIEERTI EETSFLIQAL RDTNGATIDP TFYMSRTVSN
     VISSIVFGNR FEYDDKEFLS LLGMIMRSFQ FMSTSTGQLF EMFYSVMKHL PGCQHQAYKE
     MQGLEDFIAR KVEENQRTLD PNSPRDFIDS FLIRMQEEKK NPRTQFHMRN LLMTTLNLFF
     AGTETVSTTT RYGFLLLMKY PHIAAKMHEE IDQVIGRNRQ PKYEDHLKMP YTEAVIYEIQ
     RFVDVVPLGL PRSTTKDIKF RDFLIPKGTD VFPVLSSVLK DPKFFSNPND FNPQHFSDDK
     GQFKKSNAFM PFSVGKRYCF GESLAKMELF IFFTTIMQNF CFKSPQAPQD IDVTPQYFSF
     AAIPPKFTMS FLPR
//