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 25-MAY-2022, entry version 96. DE RecName: Full=Cytochrome P450 1A1; DE EC=1.14.14.1; DE AltName: Full=CYPIA1; GN Name=cyp1a1; OS Dicentrarchus labrax (European seabass) (Morone labrax). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Moronidae; Dicentrarchus. OX NCBI_TaxID=13489; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=9972466; DOI=10.1016/s0742-8413(98)10045-2; 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 monooxygenases. CC In liver microsomes, this enzyme is involved in an NADPH-dependent CC electron transport pathway. It oxidizes a variety of structurally CC unrelated compounds, including steroids, fatty acids, and xenobiotics. CC -!- CATALYTIC ACTIVITY: CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:142491; EC=1.14.14.1; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane; Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. 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 AlphaFoldDB; P79716; -. DR SMR; P79716; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 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 InterPro; IPR036396; Cyt_P450_sf. 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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; KW Monooxygenase; Oxidoreductase. FT CHAIN 1..520 FT /note="Cytochrome P450 1A1" FT /id="PRO_0000051635" FT METAL 464 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000250" FT BINDING 230 FT /note="Substrate" FT /evidence="ECO:0000250" 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 //