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   16-JUN-2009, entry version 55.
DE   RecName: Full=Cytochrome P450 19 type 2;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPXIXA2;
DE   AltName: Full=Ovarian aromatase;
DE   AltName: Full=Estrogen synthetase;
DE   AltName: Full=P-450AROM;
GN   Name=cyp19a2;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   MEDLINE=98187857; PubMed=9529008; DOI=10.1210/en.139.4.2179;
RA   Tchoudakova A., Callard G.V.;
RT   "Identification of multiple CYP19 genes encoding different cytochrome
RT   P450 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
CC       C19 androgens.
CC   -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC       oxidized flavoprotein + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Ovarian specific.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AF020704; AAC14013.1; -; mRNA.
DR   EMBL; AB009336; BAA23758.1; -; mRNA.
DR   HOVERGEN; O73686; -.
DR   BRENDA; 1.14.14.1; 141457.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN         1    518       Cytochrome P450 19 type 2.
FT                                /FTId=PRO_0000051969.
FT   METAL       457    457       Iron (heme axial ligand) (By similarity).
FT   CONFLICT     85     85       F -> L (in Ref. 2; BAA23758).
FT   CONFLICT    166    166       S -> T (in Ref. 2; BAA23758).
FT   CONFLICT    263    263       R -> G (in Ref. 2; BAA23758).
FT   CONFLICT    300    300       A -> G (in Ref. 2; BAA23758).
FT   CONFLICT    373    373       F -> L (in Ref. 2; BAA23758).
FT   CONFLICT    407    407       K -> E (in Ref. 2; BAA23758).
FT   CONFLICT    410    410       R -> K (in Ref. 2; BAA23758).
FT   CONFLICT    462    462       M -> I (in Ref. 2; BAA23758).
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
//