ID   CP1A1_SPAAU             Reviewed;         521 AA.
AC   O42457; O42458;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1;
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Percoidei;
OC   Sparidae; Sparus.
OX   NCBI_TaxID=8175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Cousinou M., Lopez-Barea J., Dorado G.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 175-521.
RC   TISSUE=Liver;
RA   Tom M.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC       monooxygenases. They oxidize a variety of structurally unrelated
CC       compounds, including steroids, fatty acids, and xenobiotics.
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; AF011223; AAB64297.1; -; mRNA.
DR   EMBL; AF005719; AAB62887.1; -; mRNA.
DR   HSSP; P00179; 1DT6.
DR   HOVERGEN; O42457; -.
DR   BRENDA; 1.14.14.1; 191612.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   PANTHER; PTHR19383:SF63; Cyt_P450_E_grp-I_CYP1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01683; EP450ICYP1A.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN         1    521       Cytochrome P450 1A1.
FT                                /FTId=PRO_0000051647.
FT   METAL       463    463       Iron (heme axial ligand) (By similarity).
FT   CONFLICT    175    177       LVK -> GTR (in Ref. 2).
FT   CONFLICT    209    209       G -> A (in Ref. 2; AAB62887).
FT   CONFLICT    212    212       Y -> S (in Ref. 2; AAB62887).
SQ   SEQUENCE   521 AA;  59122 MW;  8FE00D86460B303B CRC64;
     MVLMILPFVG PVSVSESLVA IITMCLVYMI LKFFRTEIPE GLCQLPGPKP LPIIGNVLEV
     GRNPYLSLTA MSKRYGDVFQ IQIGMRPVVV LSGSETVRQA LIKQGDDFAG RPDLYSFRFI
     NDGKSLAFST DQAGVWRARR KLAYSALRSF STLEGTTPEY SCALEEHVSK EAEYLVKQLN
     TVMETDGSFD PFRHIVVSVA NVICGMCFGR RYDHNNQELL NLVNLSDEFG QVVASGNPAD
     FIPILQYLPS TSMKKFVSIN DRFNAFVQKI VSEHYTTFDK DNIRDITDSL IDHCEDRKLD
     ENSNVQMSDE KVVGIVNDLF GAGFDTISTA LSWSVMYLVA YPEIQERLYQ EMKESVGLDR
     TPCLSDKPKL PFLEAFILEI FRHSSFLPFT IPHCSSKDTS LNGYFIPKDT CVFINQWQIN
     HDPELWKDPS SFNPDRFLNT DGTELNKLEG EKMMVFGLGK RRCIGEVIAR NEVFLFLAIL
     VQNLRFHAKP GEPLDMTPEY GLTMKHKRCH LRAAMRSRNE E
//