CP192_CARAU
ID CP192_CARAU Reviewed; 518 AA.
AC O73686; O57316;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Ovarian aromatase;
DE EC=1.14.14.14 {ECO:0000250|UniProtKB:P11511};
DE AltName: Full=CYPXIXA2;
DE AltName: Full=Cytochrome P-450AROM;
DE AltName: Full=Cytochrome P450 19 type 2;
DE AltName: Full=Estrogen synthase;
GN Name=cyp19a2;
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=Ovary;
RX PubMed=9529008; DOI=10.1210/endo.139.4.5899;
RA Tchoudakova A., Callard G.V.;
RT "Identification of multiple CYP19 genes encoding different cytochrome P450
RT aromatase isozymes in brain and ovary.";
RL Endocrinology 139:2179-2189(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
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: Ovarian specific.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF020704; AAC14013.1; -; mRNA.
DR EMBL; AB009336; BAA23758.1; -; mRNA.
DR AlphaFoldDB; O73686; -.
DR SMR; O73686; -.
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 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; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..518
FT /note="Ovarian aromatase"
FT /id="PRO_0000051969"
FT BINDING 457
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 85
FT /note="F -> L (in Ref. 2; BAA23758)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="S -> T (in Ref. 2; BAA23758)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="R -> G (in Ref. 2; BAA23758)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="A -> G (in Ref. 2; BAA23758)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="F -> L (in Ref. 2; BAA23758)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="K -> E (in Ref. 2; BAA23758)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="R -> K (in Ref. 2; BAA23758)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="M -> I (in Ref. 2; BAA23758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 58612 MW; 004A9333D8952DEB CRC64;
MAGELLQPCG MKQVHLGEAV LELLMQGAHN SSYGAQDNVC GAMATLLLLL LCLLLAIRHH
WTEKDHVPGP CFLLGLGPLL SYCRFIWSGI GTASNYYNSK YGDIVRVWIN GEETLILSRS
SAVYHVLRKS LYTSRFGSKL GLQCIGMHEQ GIIFNSNVAL WKKVRSFYAK ALTGPGLQRT
LEICITSTNT HLDNLSHLMD ARGQVDILNL LRCIVVDISN RLFLGVPLNE HDLLQKIHKY
FDTWQTVLIK PDVYFRLAWW LHRKHKRDAQ ELQDAIAALI EQKRVQLTRA EKFDQLDFTA
ELIFAQSHGE LSTENVRQCV LEMIIAAPDT LSISLFFMLL LLKQNPDVEL KILQEMNAVL
AGRSLQHSHL SGFHILESFI NESLRFHPVV DFTMRRALDD DVIEGYKVKR GTNIILNVGR
MHRSEFFPKP NEFSLDNFQK NVPSRFFQPF GSGPRSCVGK HMAMVMMKSI LVTLLSRFSV
CPVKGCTVDS IPQTNDLSQQ PVEEPSSLSV QLILRNAL
