CP19A_CHICK
ID CP19A_CHICK Reviewed; 507 AA.
AC P19098;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Aromatase;
DE EC=1.14.14.14 {ECO:0000250|UniProtKB:P11511};
DE AltName: Full=CYPXIX;
DE AltName: Full=Cytochrome P-450AROM;
DE AltName: Full=Cytochrome P450 19A1;
DE AltName: Full=Estrogen synthase;
GN Name=CYP19A1; Synonyms=AROM, CYP19;
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=Ovary;
RX PubMed=3182796; DOI=10.1016/s0021-9258(18)37601-4;
RA McPhaul M.J., Noble J.F., Simpson E.R., Mendelson C.R., Wilson J.D.;
RT "The expression of a functional cDNA encoding the chicken cytochrome P-
RT 450arom (aromatase) that catalyzes the formation of estrogen from
RT androgen.";
RL J. Biol. Chem. 263:16358-16363(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-47.
RC STRAIN=Leghorn; TISSUE=Liver;
RA Kudo T., Yamamoto H., Sato S., Sutou S.;
RT "Comparison of 5' upstream regions of chicken and quail aromatase genes.";
RL J. Reprod. Dev. 42:101-107(1996).
CC -!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19
CC androgens.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone
CC = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:38191, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC EC=1.14.14.14; Evidence={ECO:0000250|UniProtKB:P11511};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-4-ene-3,17-dione + 3 O2 + 3 reduced [NADPH--
CC hemoprotein reductase] = estrone + formate + 4 H(+) + 4 H2O + 3
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38195,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:16422, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.14;
CC Evidence={ECO:0000250|UniProtKB:P11511};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA48739.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J04047; AAA48738.1; -; mRNA.
DR EMBL; J04047; AAA48739.1; ALT_INIT; mRNA.
DR EMBL; D50335; BAA08871.1; -; Genomic_DNA.
DR PIR; A31916; A31916.
DR AlphaFoldDB; P19098; -.
DR SMR; P19098; -.
DR STRING; 9031.ENSGALP00000038215; -.
DR PaxDb; P19098; -.
DR VEuPathDB; HostDB:geneid_414854; -.
DR eggNOG; KOG0157; Eukaryota.
DR InParanoid; P19098; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; P19098; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008585; P:female gonad development; IEP:AgBase.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032355; P:response to estradiol; IBA:GO_Central.
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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..507
FT /note="Aromatase"
FT /id="PRO_0000051964"
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 507 AA; 58146 MW; DDDC1EF7AEC1577F CRC64;
MIPETLNPLN YFTSLVPDLM PVATVPIIIL ICFLFLIWNH EETSSIPGPG YCMGIGPLIS
HGRFLWMGVG NACNYYNKTY GEFVRVWISG EETFIISKSS SVFHVMKHWN YVSRFGSKLG
LQCIGMYENG IIFNNNPAHW KEIRPFFTKA LSGPGLVRMI AICVESTIVH LDKLEEVTTE
VGNVNVLNLM RRIMLDTSNK LFLGVPLDES AIVLKIQNYF DAWQALLLKP DIFFKISWLC
KKYEEAAKDL KGAMEILIEQ KRQKLSTVEK LDEHMDFASQ LIFAQNRGDL TAENVNQCVL
EMMIAAPDTL SVTLFIMLIL IADDPTVEEK MMREIETVMG DREVQSDDMP NLKIVENFIY
ESMRYQPVVD LIMRKALQDD VIDGYPVKKG TNIILNIGRM HKLEFFPKPN EFSLENFEKN
VPSRYFQPFG FGPRGCVGKF IAMVMMKAIL VTLLRRCRVQ TMKGRGLNNI QKNNDLSMHP
IERQPLLEMV FTQEAQTRIR VTKVDQH
