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 [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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//
