ID CP1A1_LIZAU Reviewed; 521 AA. AC O42231; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 54. DE RecName: Full=Cytochrome P450 1A1; DE EC=1.14.14.1; DE AltName: Full=CYPIA1; GN Name=cyp1a1; OS Liza aurata (Golden grey mullet). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Mugilomorpha; Mugilidae; OC Liza. OX NCBI_TaxID=48191; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Cousinou M., Lopez-Barea J., Dorado G.; RL Submitted (SEP-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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF022433; AAB70307.1; -; mRNA. DR HSSP; P00179; 1DT6. DR HOVERGEN; O42231; -. DR BRENDA; 1.14.14.1; 292698. 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_0000051638. FT METAL 463 463 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 521 AA; 59064 MW; CD23195E40228DBE CRC64; MALMILPFIG ALSVSESLVA LVTVCLVYLI IKSFQANIPE GLSRLPGPKP LPIIGNVLEV GSRPYLSLTE MSKRYGNVFQ IQIGMRPVVV LSGNETVRQA LIKQGDEFAG RPDLYSFRFI SEGKSLAFST DQAGVWRARR KLAYSALRSF STLEGTTPEY SCVLEEHISK EAEYLIKQLD TVMKADGSFD PFRYIVVSVA NVICGMCFGR RYDHHDRELL SLVNLSDEFG QVVGSGNPAD FIPILQYLPN KTMKKFVNIN DRFISFVQKI VSEHYATFNK DNIRDITDSL IDHCEDRKLD ENANVQMSDE KVVGIVNDLF GAGLDTISTA LSWSVMYLVA YPEIQERLYQ ELKENVGLDR TPVLSDRNNL PLLEAFILEI FRHSSFLPFT IPHCTTKDTS LNGYYIPKDT CVFINQWQIN HDPELWKEPS SFNPDRFLSA DGTEVNKVDG EKVMVFGLGK RRCIGEVIAR NEVYMFLAIL IQKLHFYNLP GEPLDMTPEY GLTMKHKRCH LRATVRVRSD H //