ID   CP19A_RABIT             Reviewed;         503 AA.
AC   Q29605;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=CYP19;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=HY; TISSUE=Ovary;
RX   PubMed=8949389;
RA   Delarue B., Mittre H., Feral C., Benhaim A., Leymarie P.;
RT   "Rapid sequencing of rabbit aromatase cDNA using RACE PCR.";
RL   C. R. Acad. Sci. III, Sci. Vie 319:663-670(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}.
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DR   EMBL; Z70301; CAA94314.1; -; mRNA.
DR   EMBL; Z68271; CAA92574.1; -; mRNA.
DR   RefSeq; NP_001164392.1; NM_001170921.2.
DR   AlphaFoldDB; Q29605; -.
DR   SMR; Q29605; -.
DR   STRING; 9986.ENSOCUP00000010591; -.
DR   PRIDE; Q29605; -.
DR   GeneID; 100328545; -.
DR   KEGG; ocu:100328545; -.
DR   CTD; 1588; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   InParanoid; Q29605; -.
DR   OrthoDB; 1247045at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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..503
FT                   /note="Aromatase"
FT                   /id="PRO_0000051961"
FT   BINDING         437
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   503 AA;  57402 MW;  DE4AD796D635AF3D CRC64;
     MVLEMLNPMH FNITTMVPAA MPAATMPILL LTCLLLLIWN YEGTSSIPGP GYCMGIGPLI
     SYARFLWMGI GSACNYYNKM YGEFIRVWIC GEETLIISKS SSMFHVMKHS HYVSRFGSKP
     GLQCIGMHEN GIIFNNNPAL WKVVRPFFMK ALTGPGLVQM VAICVGSIGR HLDKLEEVTT
     RSGCVDVLTL MRRIMLDTSN TLFLGIPMDE SAIVVKIQGY FDAWQALLLK PNIFFKISWL
     YKKYEKSVKD LKDAIDILVE KKRRRISTAE KLEDHMDFAT NLIFAEKRGD LTRENVNQCV
     LEMLIAAPDT MSVSVFFMLF LIAKHPSVEE AIMEEIQTVV GERDIRIDDI QKLKVVENFI
     YESMRYQPVV DLVMRKALED DVIDGYPVKK GTNIILNIGR MHRLEFFPKP NEFTLENFAK
     NVPYRYFQPF GFGPRGCAGK YIAMVMMKVI LVTLLRRFQV KALQGRSVEN IQKKNDLSLH
     PDETSDLLEM IFTPRNSDTC LGQ