ID CP1A1_CHACA Reviewed; 521 AA. AC Q92039; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Cytochrome P450 1A1; DE EC=1.14.14.1; DE AltName: Full=CYPIA1; GN Name=cyp1a1; Synonyms=cyp1a; OS Chaetodon capistratus (Four-eye butterflyfish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Chaetodontiformes; Chaetodontidae; Chaetodon. OX NCBI_TaxID=37949; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Vrolijk N.H., Lin C., Chen T.T.; RT "Characterization and expression of a CYP1A gene from the tropical teleost, RT Chaetodon capistratus."; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. CC They oxidize a variety of structurally unrelated compounds, including CC 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; U19855; AAA62123.1; -; mRNA. DR AlphaFoldDB; Q92039; -. DR SMR; Q92039; -. 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 CDD; cd20676; CYP1A; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24289:SF18; CYTOCHROME P450 1A2; 1. DR PANTHER; PTHR24289; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01683; EP450ICYP1A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 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..521 FT /note="Cytochrome P450 1A1" FT /id="PRO_0000051634" FT BINDING 229 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 463 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" SQ SEQUENCE 521 AA; 58653 MW; 45FFA98CC37BE919 CRC64; MALMILPFIG SVSVSESLVA LTAVCLVYLI LKFFRTEIPA GLRQLPGPKP LPIIGNVLEV GSKPHLSLTA MSKRYGDVFQ IQIGMRPVVV LSGSETVRQA LIKQGDEFSG RPDLYSFTFI NDGKSLAFST DQAGVCGACR KLAYSALRSF STLDGTTPEY SCMLEEHICK EGECLINQLN TVMKADGSFD PFRHIVVSVA NVICGMCFGR RYDHNDQDLL RLVNLSDEFG QVAGSGNPAD FINILRFLPS TTMKKFMTIN ADFNTFVKKI VGEHYATFDK NNIRDITDSL IDHCEDRKLD ENCNVQMSDE KIVGIVNDLF GAGFDTVSTA LSWSVMYLVA YPDIQERLFQ EIKDNVGLDR TPLLSDRSKV PYLEAFILEL FRHSSFLPFT IPHCSAKDTS LNGYFIPKDT CVFINQWQIN RDPELWKDPS SFNPDRFLSC NGTEVNKQEG EKVMVFGMGK RRCIGEVIAR NEVYRGLAIL IQRLQFHEMP GELLDMTPEY GLTMKHKRCH LRATMRARNE Q //