ID   CP1A4_CHICK             Reviewed;         530 AA.
AC   P79760;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Cytochrome P450 1A4;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA4;
DE   AltName: Full=Cytochrome P450 TCDDAHH;
GN   Name=CYP1A4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8955152; DOI=10.1074/jbc.271.51.33054;
RA   Gilday D.J., Gannon M., Yutzey K., Bader D., Rifkind A.B.;
RT   "Molecular cloning and expression of two novel avian cytochrome P450 1A
RT   enzymes induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin.";
RL   J. Biol. Chem. 271:33054-33059(1996).
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   -!- INDUCTION: By 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).
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; X99453; CAA67815.1; -; mRNA.
DR   RefSeq; NP_990478.1; NM_205147.1.
DR   AlphaFoldDB; P79760; -.
DR   SMR; P79760; -.
DR   STRING; 9031.ENSGALP00000039219; -.
DR   PaxDb; P79760; -.
DR   PRIDE; P79760; -.
DR   GeneID; 396052; -.
DR   KEGG; gga:396052; -.
DR   CTD; 1543; -.
DR   VEuPathDB; HostDB:geneid_396052; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P79760; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; P79760; -.
DR   SABIO-RK; P79760; -.
DR   PRO; PR:P79760; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
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   GO; GO:0004497; F:monooxygenase activity; IDA:GO_Central.
DR   GO; GO:0019825; F:oxygen binding; IDA:AgBase.
DR   GO; GO:0046677; P:response to antibiotic; IMP:AgBase.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IMP:AgBase.
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; Reference proteome.
FT   CHAIN           1..530
FT                   /note="Cytochrome P450 1A4"
FT                   /id="PRO_0000051658"
FT   BINDING         469
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   530 AA;  59361 MW;  40736B4CA5936F2E CRC64;
     MAAGPQAAME QASSPGLISA TEVLVAAATF CLLLLLTQTR RQHAPKGLRS PPGPRGLPML
     GNVLELRKDP HLVLTRLSRK YGDVMEVTIG SRPVVVLSGL ETIKQALVRQ AEDFMGRPDL
     PSWQYVSNGH SLAFSYECGD AWKARRKLAQ NALKTFSIAA SPTASSSCLL EEHVSTEASY
     LVTKFLQLME EKQSFNPNSY LMVSVANVIC AICFGKRYDH DDQELLSVVN MNTEFGDVAA
     AGNPADFIPL LRYLPNRAMA AFKDVNARFS AFVQKIVQNH YSTFDKEHIR DVTDSLIGHC
     QEKRTGEDVR VQPSDESIIS IVNDLFGAGF DTVTTALSWC MMYAALYPHI QKKIQAELDQ
     TIGRERRPRL SDRGMLPYTE AFILEAFRHS SLLPFTIPHC TTKDTVLNGY YIPKDTCVFI
     NQWQANHDEK IWKDPPSFKP ERFLNAAGTE LSRTEADKVL IFGLGKRRCI GESIGRWEVF
     LFLTTILQQL EISLAPGQRV DITPQYGLTM KYKQCECFQM KKRFPSKGSA