CP19A_ORYLA
ID CP19A_ORYLA Reviewed; 518 AA.
AC Q92087; O13271; O13279; Q9PRF4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Orange-red; TISSUE=Ovarian follicle;
RX PubMed=7592531; DOI=10.1093/oxfordjournals.jbchem.a124768;
RA Tanaka M., Fukada S., Matsuyama M., Nagahama Y.;
RT "Structure and promoter analysis of the cytochrome P-450 aromatase gene of
RT the teleost fish, medaka (Oryzias latipes).";
RL J. Biochem. 117:719-725(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovarian follicle;
RX PubMed=8916038;
RX DOI=10.1002/(sici)1098-2795(199611)45:3<285::aid-mrd4>3.0.co;2-o;
RA Fukada S., Tanaka M., Matsuyama M., Kobayashi D., Nagahama Y.;
RT "Isolation, characterization, and expression of cDNAs encoding the medaka
RT (Oryzias latipes) ovarian follicle cytochrome P-450 aromatase.";
RL Mol. Reprod. Dev. 45:285-290(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 418-496.
RC STRAIN=Da, and HNI;
RX PubMed=10613850; DOI=10.1101/gr.9.12.1277;
RA Ohtsuka M., Makino S., Yoda K., Wada H., Naruse K., Mitani H., Shima A.,
RA Ozato K., Kimura M., Inoko H.;
RT "Construction of a linkage map of the Medaka (Oryzias latipes) and mapping
RT of the Da mutant locus defective in dorsoventral patterning.";
RL Genome Res. 9:1277-1287(1999).
CC -!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19
CC androgens. {ECO:0000250}.
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; D82968; BAA11656.1; -; mRNA.
DR EMBL; D82969; BAA11657.1; -; Genomic_DNA.
DR EMBL; AB030454; BAA85121.1; -; Genomic_DNA.
DR EMBL; AB030455; BAA85122.1; -; Genomic_DNA.
DR RefSeq; NP_001265808.1; NM_001278879.1.
DR AlphaFoldDB; Q92087; -.
DR SMR; Q92087; -.
DR STRING; 8090.ENSORLP00000003688; -.
DR Ensembl; ENSORLT00000003689; ENSORLP00000003688; ENSORLG00000002949.
DR Ensembl; ENSORLT00020029605; ENSORLP00020034671; ENSORLG00020021280.
DR GeneID; 101174651; -.
DR KEGG; ola:101174651; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00840000129915; -.
DR InParanoid; Q92087; -.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000001038; Chromosome 3.
DR Proteomes; UP000265180; Chromosome 3.
DR Proteomes; UP000265200; Unplaced.
DR Bgee; ENSORLG00000002949; Expressed in ovary and 1 other tissue.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008585; P:female gonad development; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032355; P:response to estradiol; IBA:GO_Central.
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..518
FT /note="Aromatase"
FT /id="PRO_0000051972"
FT BINDING 446
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 518 AA; 58941 MW; 39EFE4C412D2382A CRC64;
MDLIPACDRT MSSSCLVAEL VSIAPNTTVG LPSGIPMATR SLILLVCLLL MVWSHSEKKT
IPGPSFCLGL GPLMSYLRFI WTGIGTASNY YNNKYGDIVR VWINGEETLI LSRASAVHHV
LKNRKYTSRF GSKQGLSCIG MNEKGIIFNN NVALWKKIRT YFTKALTGPN LQQTVEVCVT
STQTHLDNLS SLSYVDVLGF LRCTVVDISN RLFLGVPVDE KELLQKIHKY FDTWQTVLIK
PDIYFKFSWI HQRHKTAAQE LQDAIESLVE RKRKEMEQAE KLDNINFTAE LIFAQGHGEL
SAENVRQCVL EMVIAAPDTL SISLFFMLLL LKQNPHVELQ LLQEIDTIVG DSQLQNQDLQ
KLQVLESFIN ECLRFHPVVD FTMRRALFDD IIDGHRVQKG TNIILNTGRM HRTEFFHKAN
EFSLENFQKN TPRRYFQPFG SGPRACVGRH IAMVMMKSIL VTLLSQYSVC PHEGLTLDCL
PQTNNLSQQP VEHHQEADHL SMTFLPRQRG IWESPSPF
