ID   CP1A5_CHICK             Reviewed;         528 AA.
AC   P79761;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Cytochrome P450 1A5;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA5;
DE   AltName: Full=Cytochrome P450 TCDDAA;
GN   Name=CYP1A5;
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].
RC   TISSUE=Liver;
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}.
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DR   EMBL; X99454; CAA67816.1; -; mRNA.
DR   RefSeq; NP_990477.1; NM_205146.2.
DR   AlphaFoldDB; P79761; -.
DR   SMR; P79761; -.
DR   STRING; 9031.ENSGALP00000002016; -.
DR   PaxDb; 9031-ENSGALP00000002016; -.
DR   GeneID; 396051; -.
DR   KEGG; gga:396051; -.
DR   CTD; 1544; -.
DR   VEuPathDB; HostDB:geneid_396051; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P79761; -.
DR   OrthoDB; 2900138at2759; -.
DR   PhylomeDB; P79761; -.
DR   SABIO-RK; P79761; -.
DR   PRO; PR:P79761; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
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:0008392; F:arachidonic acid epoxygenase activity; IDA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0019825; F:oxygen binding; IDA:AgBase.
DR   GO; GO:1990748; P:cellular detoxification; IDA:AgBase.
DR   GO; GO:0036146; P:cellular response to mycotoxin; IEP:AgBase.
DR   GO; GO:0046677; P:response to antibiotic; IMP:AgBase.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IMP:AgBase.
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; Reference proteome.
FT   CHAIN           1..528
FT                   /note="Cytochrome P450 1A5"
FT                   /id="PRO_0000051659"
FT   BINDING         467
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   528 AA;  60071 MW;  5D73AAA637CEB957 CRC64;
     MGPEEVMVQA SSPGLISATE VLVAAATFCL LLLLTQTRRQ HAPKGLRSPP GPRGLPMLGS
     VLELRKDPHL VLTRLSRKYG DVMEVTIGSR PVVVLSGLET IKQALVRQAE DFMGRPDLYS
     FRHITDGQSL TFSTDTGEMW KARRKLAQNA LKNFSIAASP TASSSCLLEE HVSTEASYLV
     TKFLQLMEEK QSFDPYRYMV VSVANVICAI CFGKRYDHDD QELLSVVNVV DEFVDVTAAG
     NPADFIPLLR YLPSRNMDSF LDFNKRFMKL LQTAVEEHYQ TFDKNNIRDV TDSLIEQCVE
     KKAEANGATQ IPNEKIINLV NDIFGAGFDT VTTALSWSLM YLVTYPHMQK KIQAELDQTI
     GRERRPRLSD RGMLPYTEAF ILEMFRHSSF MPFTIPHSTT RDTVLNGYYI PKDRCVFINQ
     WQVNHDEKLW KDPQAFNPER FLNAEGTEVN KVDAEKVMTF GLGKRRCIGE NIGKWEVFLF
     LSTLLQQLEF SIQDGKKADM TPIYGLSMKH KRCEHFQVKK RFSMKSSN
//