ID   CP191_CARAU             Reviewed;         510 AA.
AC   P79690; O57315;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Brain aromatase;
DE            EC=1.14.14.14 {ECO:0000250|UniProtKB:P11511};
DE   AltName: Full=CYPXIXA1;
DE   AltName: Full=Cytochrome P-450AROM;
DE   AltName: Full=Cytochrome P450 19 type 1;
DE   AltName: Full=Estrogen synthase;
GN   Name=cyp19a1; Synonyms=cyp19;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9685217; DOI=10.1016/s0303-7207(98)00015-x;
RA   Gelinas D.M., Pitoc G.A., Callard G.V.;
RT   "Isolation of a goldfish brain cytochrome P450 aromatase cDNA: mRNA
RT   expression during the seasonal cycle and after steroid treatment.";
RL   Mol. Cell. Endocrinol. 138:81-93(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Sudrajat A., Yoshiura Y., Gen K., Suetake H., Aida K.;
RT   "Two differing cDNAs encoding cytochrome P450arom (aromatase) exist in
RT   goldfish.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Brain specific.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U18974; AAB39408.1; -; mRNA.
DR   EMBL; AB009335; BAA23757.1; -; mRNA.
DR   AlphaFoldDB; P79690; -.
DR   SMR; P79690; -.
DR   PRIDE; P79690; -.
DR   Proteomes; UP000515129; Genome assembly.
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..510
FT                   /note="Brain aromatase"
FT                   /id="PRO_0000051968"
FT   BINDING         435
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"
FT   CONFLICT        14
FT                   /note="A -> T (in Ref. 2; BAA23757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495
FT                   /note="A -> S (in Ref. 2; BAA23757)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="E -> Q (in Ref. 2; BAA23757)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  58049 MW;  FAAE56AACF3AC646 CRC64;
     MEEVLKGTVN FAAAVQVTLM ALTGTLLLIL LHRIFTAKNW RNQSGVPGPG WLLGLGPIMS
     YSRFLWMGIG SACNYYNEKY GSIARVWISG EETFILSKSS AVYHVLKSNN YTGRFASKKG
     LQCIGMFEQG IIFNSNMALW KKVRTYFTKA LTGPGLQKSV DVCVSATNKQ LNVLQEFTDH
     SGHVDVLNLL RCIVVDVSNR LFLRIPLNEK DLLIKIHRYF STWQAVLIQP DVFFRLNFVY
     KKYHLAAKEL QDEMGKLVEQ KRQAINNMEK LDETDFATEL IFAQNHDELS VDDVRQCVLE
     MVIAAPDTLS ISLFFMLLLL KQNSVVEEQI VQEIQSQIGE RDVESADLQK LNVLERFIKE
     SLRFHPVVDF IMRRALEDDE IDGYRVAKGT NLILNIGRMH KSEFFQKPNE FNLENFENTV
     PSRYFQPFGC GPRACVGKHI AMVMTKAILV TLLSRFTVCP RHGCTVSTIK QTNNLSMQPV
     EEDPDSLAMR FIPRAQNICG DPHLGEKTEE