ID   CP1A1_LIMLI             Reviewed;         521 AA.
AC   O42430;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1;
OS   Limanda limanda (Dab).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Pleuronectidae; Pleuronectinae; Limanda.
OX   NCBI_TaxID=27771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=21315588; PubMed=11423384; DOI=10.1016/S1532-0456(01)00188-0;
RA   Craft J.A., Robertson F.E., McPhail M.E., Brown E., Stagg R.M.;
RT   "Measurement of cytochrome P4501A induction in dab (Limanda limanda)
RT   and other teleosts with species-specific cDNA probes: isolation and
RT   characterisation of dab cDNA and its use in expression studies with
RT   beta-naphthoflavone-treated fish.";
RL   Comp. Biochem. Physiol. 129C:115-127(2001).
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; AJ001724; CAA04953.1; -; mRNA.
DR   HSSP; P00179; 1DT6.
DR   HOVERGEN; O42430; -.
DR   BRENDA; 1.14.14.1; 289164.
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_0000051637.
FT   METAL       463    463       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   521 AA;  59063 MW;  11DE326C8A7FBDF9 CRC64;
     MMLMMLPFIG SVSVSESLVA MTTVCLVYLI LKFFQTEIPE GLRRLPGPKP LPIIGNVLEM
     GSRPYLSLTA MSKRYGNVFQ IQIGMRPVVV LSGSETVRQA LIKQGDDFAG RPDLYSFRFI
     NEGKSLAFST DKAGIWRARR KLAYSALRSF ATLEGTTPEY SCVLEEHVCK EGEYLIKQLN
     TAMTADGSFD PFRHIVVSVA NVICGMCFGR RYDHDDQELV GLVTLSDEFG RVVGSGNPAD
     FIPILQYLPS ATMKNFLRIN GRFTEFVQKI VTEHYTTFDK DNIRDITDSL IDHCEDRKLD
     ENSNVQMSDE KIVGIVNDLF GAGFDTVSTA LSWSVMYLVA HPEIQERLYQ EIEDKVGLDR
     MPLLSDKPNL PFLEAFILEI LRHSSFLPFT IPHCTTKDTS LNGYFIPKDT CVFINQWQIN
     HDPEMWKDPS SFNPDRFLSA DGSEVNKLDG EKVMAFGMGK RRCIGEVIAR NEVYLFLAIL
     IQKLHFLPIP GEKLDMTPEY GLTMKHKRCH LKATMRARNE H
//