ID   CP2H1_CHICK             Reviewed;         491 AA.
AC   P05180;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Cytochrome P450 2H1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIH1;
DE   AltName: Full=Cytochrome P450 PB15;
DE   AltName: Full=Cytochrome P450 PCHP3;
GN   Name=CYP2H1;
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], AND INDUCTION.
RX   PubMed=2424910; DOI=10.1016/s0021-9258(18)67676-8;
RA   Hobbs A.A., Mattschoss L.A., May B.K., Williams K.E., Elliott W.H.;
RT   "The cDNA and protein sequence of a phenobarbital-induced chicken
RT   cytochrome P-450.";
RL   J. Biol. Chem. 261:9444-9449(1986).
RN   [2]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=11572089; DOI=10.1007/s004410100414;
RA   Zhu Y., Wang M., Lin H., Li Z., Luo J.;
RT   "Identification of estrogen-responsive genes in chick liver.";
RL   Cell Tissue Res. 305:357-363(2001).
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   -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:11572089}.
CC   -!- INDUCTION: By phenobarbital (PubMed:2424910). Significantly increased
CC       expression by estrogen. Rapidly up-regulated within 0.5 hour after
CC       extrogen exposure with a peak at 1-4 hours. Expression is significantly
CC       decreased below control level after 30 hours (PubMed:11572089).
CC       {ECO:0000269|PubMed:11572089, ECO:0000269|PubMed:2424910}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M13454; AAA48742.1; -; mRNA.
DR   PIR; A24814; A24814.
DR   RefSeq; NP_001001616.1; NM_001001616.1.
DR   AlphaFoldDB; P05180; -.
DR   SMR; P05180; -.
DR   STRING; 9031.ENSGALP00000039271; -.
DR   PaxDb; 9031-ENSGALP00000039271; -.
DR   GeneID; 414746; -.
DR   KEGG; gga:414746; -.
DR   VEuPathDB; HostDB:geneid_414746; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P05180; -.
DR   OrthoDB; 2900138at2759; -.
DR   PhylomeDB; P05180; -.
DR   PRO; PR:P05180; -.
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:0009410; P:response to xenobiotic stimulus; IDA:AgBase.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..491
FT                   /note="Cytochrome P450 2H1"
FT                   /id="PRO_0000051766"
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;  56261 MW;  E2345F98AE99CA2F CRC64;
     MDFLGLPTIL LLVCISCLLI AAWRSTSQRG KEPPGPTPIP IIGNVFQLNP WDLMGSFKEL
     SKKYGPIFTI HLGPKKIVVL YGYDIVKEAL IDNGEAFSGR GILPLIEKLF KGTGIVTSNG
     ETWRQLRRFA LTTLRDFGMG KKGIEERIQE EAHFLVERIR KTHEEPFNPG KFLIHAVANI
     ICSIVFGDRF DYEDKKFLDL IEMLEENNKY QNRIQTLLYN FFPTILDSLP GPHKTLIKNT
     ETVDDFIKEI VIAHQESFDA SCPRDFIDAF INKMEQEKEN SYFTVESLTR TTLDLFLAGT
     GTTSTTLRYG LLILLKHPEI EEKMHKEIDR VVGRDRSPCM ADRSQLPYTD AVIHEIQRFI
     DFLPLNVPHA VIKDTKLRDY FIPKDTMIFP LLSPILQDCK EFPNPEKFDP GHFLNANGTF
     RRSDYFMPFS AGKRICAGEG LARMEIFLFL TSILQNFSLK PVKDRKDIDI SPIITSLANM
     PRPYEVSFIP R
//