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Database: UniProt
Entry: Q64391
LinkDB: Q64391
Original site: Q64391 
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   05-OCT-2016, entry version 112.
DE   RecName: Full=Cytochrome P450 1A2;
DE            EC=1.14.14.1 {ECO:0000250|UniProtKB:P05177};
DE   AltName: Full=CYPIA2;
DE   AltName: Full=Cholesterol 25-hydroxylase {ECO:0000250|UniProtKB:P05177};
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       {ECO:0000250|UniProtKB:P05177}.
CC   -!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
CC       O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
CC       {ECO:0000250|UniProtKB:P05177}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane
CC       {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
DR   EMBL; D50457; BAA09048.1; -; mRNA.
DR   EMBL; U23501; AAB70866.1; -; mRNA.
DR   RefSeq; NP_001166165.1; NM_001172694.1.
DR   ProteinModelPortal; Q64391; -.
DR   STRING; 10141.ENSCPOP00000017610; -.
DR   GeneID; 100135513; -.
DR   CTD; 1544; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   eggNOG; COG2124; LUCA.
DR   HOGENOM; HOG000036991; -.
DR   HOVERGEN; HBG106944; -.
DR   InParanoid; Q64391; -.
DR   OrthoDB; EOG091G0BT8; -.
DR   TreeFam; TF105095; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
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; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Endoplasmic reticulum; Glycoprotein; Heme; Iron;
KW   Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Steroid metabolism;
KW   Sterol metabolism.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P56592}.
FT   CHAIN         2    515       Cytochrome P450 1A2.
FT                                /FTId=PRO_0000051650.
FT   METAL       458    458       Iron (heme axial ligand). {ECO:0000250}.
FT   BINDING     226    226       Substrate. {ECO:0000250}.
FT   CARBOHYD     69     69       O-linked (GlcNAc). {ECO:0000250}.
FT   CONFLICT    149    149       V -> L (in Ref. 2; AAB70866).
FT                                {ECO:0000305}.
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
//
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