ID CP1A1_DICLA Reviewed; 520 AA. AC P79716; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 22-JUL-2008, entry version 49. DE RecName: Full=Cytochrome P450 1A1; DE EC=1.14.14.1; DE AltName: Full=CYPIA1; GN Name=cyp1a1; OS Dicentrarchus labrax (European sea bass). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Percoidei; OC Moronidae; Dicentrarchus. OX NCBI_TaxID=13489; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=99138413; PubMed=9972466; RA Stien X., Amichot M., Berge J.-B., Lafaurie M.; RT "Molecular cloning of a CYP1A cDNA from the teleost fish Dicentrarchus RT labrax."; RL Comp. Biochem. Physiol. 121C:241-248(1998). 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. 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U78316; AAB36951.1; -; mRNA. DR HSSP; P00179; 1DT6. DR HOVERGEN; P79716; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050381; F:unspecific monooxygenase activity; IEA:EC. DR InterPro; IPR001128; Cyt_P450. 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 1 520 Cytochrome P450 1A1. FT /FTId=PRO_0000051635. FT METAL 464 464 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 520 AA; 58744 MW; 86761584B28E57FB CRC64; MVLMILPFIG SVSVSESLVA LTTVCLVYLI LKFFRTEIPE GLHRLPGPKP LPLIGNVLEV GNKPYLSLTA MSKRYGDVFR FRLGMRPSGC LSGSETVRKA LIKQGDEFAG RPDLYSFRFI NDGKSLAFST DKAGVWRALR KLAYSALRSF SSLEESTPRD SCVLEEHSAK EGEYLYSNML NAVMKVTGSF DPFRHIVVSV ANVICGMCFG RRYGHNDQEL LSLVNLSDPF GQVVGSGNPA DFIPVLQFLP STTMKNFMDI NARFNKFVQK IVSEHYTTYD KDNIRDITDS LIDHCEDRKL DENANVQMSD EKIVGIVNDL FGAGFDTIST ALSWSVMYLV AYPEIEERLY QELKENVGLD RTPLLCDRPN LPFLEAFILE IFRHSSFLPF TIPHCTSKDT SLNGYFIPKD TCVFINQWQI NHDPELWKDP SSFNPDRFLS ADGTELNKLE GEKVMVFGLG KRRCIGEVIA RNGVFLFLAI IVQKLHFKTL PGEPLDMTPE YGLTMKHKRC HLRATMRASE //