ID   CP2H2_CHICK             Reviewed;         491 AA.
AC   P20678;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   13-SEP-2023, entry version 138.
DE   RecName: Full=Cytochrome P450 2H2;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIH2;
DE   AltName: Full=Cytochrome P450 PCHP7;
GN   Name=CYP2H2;
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=2470563; DOI=10.1089/dna.1.1989.8.179;
RA   Hansen A.J., May B.K.;
RT   "Sequence of a chicken phenobarbital-inducible cytochrome P450 cDNA:
RT   regulation of two P450 mRNAs transcribed from different genes.";
RL   DNA 8:179-191(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-25.
RX   PubMed=1527070; DOI=10.1016/s0021-9258(18)41804-2;
RA   Nakai K., Ward A.M., Gannon M., Rifkind A.B.;
RT   "Beta-naphthoflavone induction of a cytochrome P-450 arachidonic acid
RT   epoxygenase in chick embryo liver distinct from the aryl hydrocarbon
RT   hydroxylase and from phenobarbital-induced arachidonate epoxygenase.";
RL   J. Biol. Chem. 267:19503-19512(1992).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-21.
RX   PubMed=2375760; DOI=10.1042/bj2690085;
RA   Sinclair J.F., Wood S., Lambrecht L., Gorman N., Mende-Mueller L.,
RA   Smith L., Hunt J., Sinclair P.;
RT   "Isolation of four forms of acetone-induced cytochrome P-450 in chicken
RT   liver by HPLC and their enzymic characterization.";
RL   Biochem. J. 269:85-91(1990).
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 phenobarbital.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M25469; AAA48743.1; -; mRNA.
DR   PIR; A31418; A31418.
DR   RefSeq; NP_001001757.1; NM_001001757.1.
DR   AlphaFoldDB; P20678; -.
DR   SMR; P20678; -.
DR   STRING; 9031.ENSGALP00000009294; -.
DR   GeneID; 414841; -.
DR   KEGG; gga:414841; -.
DR   CTD; 414841; -.
DR   VEuPathDB; HostDB:geneid_414841; -.
DR   InParanoid; P20678; -.
DR   PRO; PR:P20678; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20665; CYP2C-like; 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; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24300:SF356; CYTOCHROME P450 2E1; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..491
FT                   /note="Cytochrome P450 2H2"
FT                   /id="PRO_0000051767"
FT   BINDING         436
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"
SQ   SEQUENCE   491 AA;  56485 MW;  63F906362FDC8722 CRC64;
     MDFLGLPTIL LLVCISCFLI AAWRSTSQRG KEPPGPTPIP IIGNVFQLNP WDLMESFKEL
     SKKYGPIFTI HLGPKKVVVL YGYDVVKEAL IDNGEAFSGR GNLPLFEKVF KGTGIVTSNG
     ESWRQMRRFA LTTLRDFGMG KKSIEERIQE EARFLVERIR NTHEKPFNPT VFLMHAVSNI
     ICSTVFGDRF DYEDKKFLDL IEMLDENERY QNRIQTQLYN FFPTILDYLP GPHKTLIKSI
     ETVDDFITEI IRAHQESFDA SCPRDFIDAF INKMQQEKEN SYFTVESLTR TTLDLFLAGT
     GTTSTTLRYG LLILLKHPEI EEKMHKEIDR VVGRDRSPCM ADRSQLPYTD AVIHEIQRFI
     DFLPVNLPRA VIKDTKLRDY FIPKDTMIFP LLSPILQDCK EFPNPEKFDP GHFLNANGTF
     RKSNYFMPFS AGKRICAGEG LARMELFLFL TSILQNFSLK PVKDRKDIDI SPIVTSAANI
     PRPYEVSFIP R
//