ID   CP19A_CALJA             Reviewed;         503 AA.
AC   Q95M61;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 99.
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   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Husen B., Einspanier A.;
RT   "Regulation of 17-beta-hydroxysteroid dehydrogenases type 1 and type 7
RT   during pregnancy in the marmoset monkey.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38191, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:16469, ChEBI:CHEBI:17347, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.14;
CC         Evidence={ECO:0000250|UniProtKB:P11511};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-4-ene-3,17-dione + 3 O2 + 3 reduced
CC         [NADPH--hemoprotein reductase] = estrone + formate + 4 H(+) + 4 H2O +
CC         3 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; AY034779; AAK58465.2; -; mRNA.
DR   RefSeq; NP_001254691.1; NM_001267762.1.
DR   AlphaFoldDB; Q95M61; -.
DR   SMR; Q95M61; -.
DR   STRING; 9483.ENSCJAP00000002075; -.
DR   GeneID; 100411557; -.
DR   KEGG; cjc:100411557; -.
DR   CTD; 1588; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   InParanoid; Q95M61; -.
DR   OrthoDB; 5385594at2759; -.
DR   Proteomes; UP000008225; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd20616; CYP19A1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24291:SF43; AROMATASE; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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..503
FT                   /note="Aromatase"
FT                   /id="PRO_0000051951"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         374
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
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   503 AA;  57794 MW;  775E8F1734412099 CRC64;
     MVLEMLNPMH YNITSMVPEA MPAATMPILL LTGLFLLVWN YEGTSSIPGP GYCMGIGPLI
     SHGRFLWMGI GNACNYYNRM YGEFMRVWIS GEETLIISKS SSMFHVMKHN HYSSRFGSKL
     GLQCIGMHEK GIIFNNNPDL WKTTRPLFMK ALSGPGLVRM VTVCAESLNT HLDRLEEVTN
     ESGFIDVLTL LRCVMLDTSN TLFLRIPLDE NAIVFKIQGY FDAWQALLIK PDIFFKISWL
     YKKYEKSVKD LKDAIEVLMA EKRRRISAEE KLEEHIDFAT ELILAEKRGD LTRENVNQCM
     LEMLIAAPDT MSVSLFFMLF LIAKHPNVEE AIMKEIQTVV GERDVKIDDI QKLKVVENFI
     YESMRYQPVV DLVMRKALED DVIDGYPVKK GTNIILNIGR MHRLEFFPKP NEFTLENFAK
     NVPYRYFQPF GFGPRSCAGK YIAMVMMKSI LVTLLRRFHV KTLGGECVES LQKTNDLALH
     PDHTKSMLEM IFTPRNSGWC LEH
//