CP19A_TAEGU
ID CP19A_TAEGU Reviewed; 509 AA.
AC Q92112;
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 Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7968362; DOI=10.1016/0169-328x(94)90136-8;
RA Shen P., Campagnoni C.W., Kampf K., Schlinger B.A., Arnold A.P.,
RA Campagnoni A.T.;
RT "Isolation and characterization of a zebra finch aromatase cDNA: in situ
RT hybridization reveals high aromatase expression in brain.";
RL Brain Res. Mol. Brain Res. 24:227-237(1994).
CC -!- FUNCTION: Catalyzes the formation of aromatic C18 estrogens from C19
CC androgens.
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; L81143; AAL77515.1; -; mRNA.
DR EMBL; S75898; AAB32404.1; -; mRNA.
DR PIR; I51271; I51271.
DR RefSeq; NP_001070159.1; NM_001076691.2.
DR AlphaFoldDB; Q92112; -.
DR SMR; Q92112; -.
DR STRING; 59729.ENSTGUP00000007225; -.
DR GeneID; 751777; -.
DR KEGG; tgu:751777; -.
DR CTD; 1588; -.
DR InParanoid; Q92112; -.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000007754; Unplaced.
DR GO; GO:0044297; C:cell body; IDA:AgBase.
DR GO; GO:0030425; C:dendrite; IDA:AgBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:AgBase.
DR GO; GO:0043195; C:terminal bouton; IDA:AgBase.
DR GO; GO:0070330; F:aromatase activity; IDA:AgBase.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IMP:AgBase.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:AgBase.
DR GO; GO:0006703; P:estrogen biosynthetic process; IDA:AgBase.
DR GO; GO:0007613; P:memory; IMP:AgBase.
DR GO; GO:2000844; P:negative regulation of testosterone secretion; IMP:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:AgBase.
DR GO; GO:2000866; P:positive regulation of estradiol secretion; IMP:AgBase.
DR GO; GO:2000027; P:regulation of animal organ morphogenesis; IMP:AgBase.
DR GO; GO:0061477; P:response to aromatase inhibitor; IDA:AgBase.
DR GO; GO:0035176; P:social behavior; IMP:AgBase.
DR GO; GO:0009888; P:tissue development; IMP:AgBase.
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..509
FT /note="Aromatase"
FT /id="PRO_0000051973"
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 509 AA; 58390 MW; B127ED20F18E3260 CRC64;
MVLETLNPLH YNITSLVPDT MPVATVPILI LMCFLFLIWN HEETSSIPGP GYCMGIGPLI
SHGRFLWMGV GNACNYYNKT YGDFVRVWIS GEETFIISKS SSVSHVMKHW HYVSRFGSKL
GLQCIGMYEN GIIFNNNPAH WKEIRPFFTK ALSGPGLVRM IAICVESTTE HLDRLQEVTT
ELGNINALNL MRRIMLDTSN KLFLGVPLDE NAIVLKIQNY FDAWQALLLK PDIFFKISWL
CKKYKDAVKD LKGAMEILIE QKRQKLSTVE KLDEHMDFAS QLIFAQNRGD LTAENVNQCV
LEMMIAAPDT LSVTLFFMLI LIAEHPTVEE EMMREIETVV GDRDIQSDDM PNLKIVENFI
YESMRYQPVV DLIMRKALQD DVIDGYPVKK GTNIILNIGR MHKLEFFPKP NEFSLENFEK
NVPSRYFQPF GFGPRSCVGK FIAMVMMKAI LVTLLRRCRV QTMKGRGLNN IQKNNDLSMH
PIERQPLLEM VFTPRRNANE NQGDGMDQH
