ID   CP19A_HORSE             Reviewed;         503 AA.
AC   O46512; O46513;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=Cytochrome P450 19A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPXIX;
DE   AltName: Full=Aromatase;
DE   AltName: Full=Estrogen synthetase;
DE   AltName: Full=P-450AROM;
DE   AltName: Full=P450 17-alpha;
GN   Name=CYP19A1; Synonyms=CYP19;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (CLONE A1 AND CLONE A17).
RC   TISSUE=Follicular cell;
RX   MEDLINE=99392955; PubMed=10465286; DOI=10.1210/en.140.9.4133;
RA   Boerboom D., Kerban A., Sirois J.;
RT   "Dual regulation of promoter II- and promoter 1f-derived cytochrome
RT   P450 aromatase transcripts in equine granulosa cells during human
RT   chorionic gonadotropin-induced ovulation: a novel model for the study
RT   of aromatase promoter switching.";
RL   Endocrinology 140:4133-4141(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=22478897; PubMed=12591609; DOI=10.1016/S0167-4781(02)00621-8;
RA   Seralini G.E., Tomilin A., Auvray P., Nativelle-Serpentini C.,
RA   Sourdaine P., Moslemi S.;
RT   "Molecular characterization and expression of equine testicular
RT   cytochrome P450 aromatase.";
RL   Biochim. Biophys. Acta 1625:229-238(2003).
CC   -!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from
CC       C19 androgens. Final rate-limiting step.
CC   -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC       oxidized flavoprotein + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in placenta. Highly expressed in
CC       follicles (0 hour:hCG), followed by a drop (12-24 hour:hCG) and by
CC       an increase (30-39 hour:hCG). Highly expressed in corpora lutea.
CC       Also expressed in granulosa cell layer. Not expressed in theca
CC       interna.
CC   -!- DOMAIN: Contains a I helix thought to serve as the substrate-
CC       binding pocket.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC   -!- CAUTION: Clone A1 form may be a splice variant or an artifact.
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DR   EMBL; AF031520; AAC04698.1; -; mRNA.
DR   EMBL; AF031521; AAC04699.1; -; mRNA.
DR   EMBL; AJ012610; CAB38442.1; -; mRNA.
DR   RefSeq; NP_001075274.1; -.
DR   UniGene; Eca.11648; -.
DR   Ensembl; ENSECAG00000020474; Equus caballus.
DR   GeneID; 100009712; -.
DR   KEGG; ecb:100009712; -.
DR   HOVERGEN; O46512; -.
DR   OMA; O46512; TRENVNQ.
DR   BRENDA; 1.14.14.1; 1464.
DR   GO; GO:0005789; C:endoplasmic reticulum 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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    503       Cytochrome P450 19A1.
FT                                /FTId=PRO_0000051954.
FT   REGION      294    324       Substrate-binding pocket (Potential).
FT   METAL       437    437       Iron (heme axial ligand) (By similarity).
FT   MOD_RES     162    162       Phosphothreonine (By similarity).
FT   CONFLICT    342    347       ERDLKN -> RNLSNK (in Ref. 1; clone A1).
FT   CONFLICT    348    503       Missing (in Ref. 1; clone A1).
SQ   SEQUENCE   503 AA;  57825 MW;  878E2CB040B5AECE CRC64;
     MILEMLNPMH YNLTSMVPEV MPVATLPILL LTGFLFFVWN HEETSSIPGP GYCMGIGPLI
     SHLRFLWMGL GSACNYYNKM YGEFVRVWIS GEETLVISKS SSTFHIMKHD HYSSRFGSTF
     GLQYMGMHEN GVIFNNNPAV WKALRPFFVK ALSGPSLARM VTVCVESVNN HLDRLDEVTN
     ALGHVNVLTL MRRTMLDASN TLFLRIPLDE KNIVLKIQGY FDAWQALLIK PNIFFKISWL
     SRKHQKSIKE LRDAVGILAE EKRHRIFTAE KLEDHVDFAT DLILAEKRGE LTKENVNQCI
     LEMMIAAPDT LSVTVFFMLC LIAQHPKVEE ALMKEIQTVL GERDLKNDDM QKLKVMENFI
     NESMRYQPVV DIVMRKALED DVIDGYPVKK GTNIILNIGR MHKLEFFPKP NEFTLENFEK
     NVPYRYFQPF GFGPRSCAGK FIAMVMMKVM LVSLLRRFHV KTLQGNCLEN MQKTNDLALH
     PDESRSLPAM IFTPRNSEKC LEH
//