ID CP1A2_CAVPO Reviewed; 515 AA.
AC Q64391; Q64404;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-APR-2013, entry version 91.
DE RecName: Full=Cytochrome P450 1A2;
DE EC=1.14.14.1;
DE AltName: Full=CYPIA2;
GN Name=CYP1A2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC Hystricognathi; Caviidae; Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Liver;
RX PubMed=9434738; DOI=10.1006/abbi.1997.0409;
RA Mori T., Itoh S., Ohgiya S., Ishizaki K., Kamataki T.;
RT "Regulation of CYP1A and CYP3A mRNAs by ascorbic acid in guinea
RT pigs.";
RL Arch. Biochem. Biophys. 348:268-277(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Liver;
RA Black V.H.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC monooxygenases. In liver microsomes, this enzyme is involved in an
CC NADPH-dependent electron transport pathway. It oxidizes a variety
CC of structurally unrelated compounds, including steroids, fatty
CC acids, and xenobiotics. Most active in catalyzing 2-hydroxylation
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC oxidized flavoprotein + H(2)O.
CC -!- COFACTOR: Heme group (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR EMBL; D50457; BAA09048.1; -; mRNA.
DR EMBL; U23501; AAB70866.1; -; mRNA.
DR RefSeq; NP_001166165.1; NM_001172694.1.
DR ProteinModelPortal; Q64391; -.
DR SMR; Q64391; 34-514.
DR STRING; 10141.ENSCPOP00000017610; -.
DR Ensembl; ENSCPOT00000001250; ENSCPOP00000017610; ENSCPOG00000001235.
DR GeneID; 100135513; -.
DR CTD; 1544; -.
DR eggNOG; COG2124; -.
DR GeneTree; ENSGT00680000099714; -.
DR HOGENOM; HOG000036991; -.
DR HOVERGEN; HBG106944; -.
DR InParanoid; Q64391; -.
DR OrthoDB; EOG4WSW9D; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IEA:EC.
DR GO; GO:0034875; F:caffeine oxidase activity; IEA:Compara.
DR GO; GO:0032451; F:demethylase activity; IEA:Compara.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:Compara.
DR GO; GO:0045333; P:cellular respiration; IEA:Compara.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Compara.
DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEA:Compara.
DR GO; GO:0042738; P:exogenous drug catabolic process; IEA:Compara.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Compara.
DR GO; GO:0030324; P:lung development; IEA:Compara.
DR GO; GO:0032787; P:monocarboxylic acid metabolic process; IEA:Compara.
DR GO; GO:0016098; P:monoterpenoid metabolic process; IEA:Compara.
DR GO; GO:0071615; P:oxidative deethylation; IEA:Compara.
DR GO; GO:0070989; P:oxidative demethylation; IEA:Compara.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IEA:Compara.
DR GO; GO:0009791; P:post-embryonic development; IEA:Compara.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Compara.
DR GO; GO:0006706; P:steroid catabolic process; IEA:Compara.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:Compara.
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; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01683; EP450ICYP1A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome_P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Complete proteome; Endoplasmic reticulum; Heme; Iron;
KW Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 515 Cytochrome P450 1A2.
FT /FTId=PRO_0000051650.
FT METAL 458 458 Iron (heme axial ligand) (By similarity).
FT BINDING 226 226 Substrate (By similarity).
FT MOD_RES 289 289 N6-acetyllysine (By similarity).
FT CONFLICT 149 149 V -> L (in Ref. 2; AAB70866).
SQ SEQUENCE 515 AA; 58423 MW; E5EDF0B9D33151A8 CRC64;
MPLSWLLPFS AMELLLTATI FYLVLWVVKA FRLQVPKGLK SPPGPWGWPL IGHVLTLGKN
PHLALTRLSA RYGDVLQIRI GSTPVVVLSG LDTIRQALVR QSDDFKGRPD LYSSTFISDG
QSMIFNPDSG PVWAARRRLA QSALQSFSVA SDPASVSSCY LEEHVSREAE HLVTKLLDLM
AGPGCFEPSS QIVGSVANVI GAMCFGKNFP QTSEEMLQIV NTSKEFTEFA SSGNPVDFFP
ILRYLPNPML QQFKDFNKRF LQFLQKTVQE HYQDFDKNHV QDIASALFKH SEESPHVNGD
LIPRKKIVNL VNDIFGAGFD TVTTAISWSL LYLVTKPEIQ KKIHKELDAV IGRDRKPRLA
DRPQLPYMEA FILEVFRYSS FLPFTIPHCT TRDTILNGFY IPKDRCVFIN QWQVNHDPKQ
WEDPFEFRPE RFLLANNTAV DKTLSDKILL FGLGKRRCIG ETLGRWEVFL FLAILLQQLE
FSVPPGVKVD LTPVYGLTMK PPHCQHVQAR PRFSK
//
