ID   CP193_PIG               Reviewed;         501 AA.
AC   P79304;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Aromatase 3;
DE            EC=1.14.14.14 {ECO:0000250|UniProtKB:P11511};
DE   AltName: Full=CYPXIXA3;
DE   AltName: Full=Cytochrome P-450AROM;
DE   AltName: Full=Cytochrome P450 19 type III;
DE   AltName: Full=Estrogen synthase;
GN   Name=CYP19A3;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Ovary;
RX   PubMed=8674811; DOI=10.1016/0303-7207(95)03607-9;
RA   Corbin C.J., Khalil M.W., Conley A.J.;
RT   "Functional ovarian and placental isoforms of porcine aromatase.";
RL   Mol. Cell. Endocrinol. 113:29-37(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Ovary;
RX   PubMed=9365218; DOI=10.1016/s0960-0760(97)80040-4;
RA   Conley A.J., Corbin C.J., Smith T., Hinshelwood M., Liu Z., Simpson E.;
RT   "Porcine aromatases: studies on tissue-specific, functionally distinct
RT   isozymes from a single gene?";
RL   J. Steroid Biochem. Mol. Biol. 61:407-413(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-96.
RC   TISSUE=Liver;
RX   PubMed=9212170; DOI=10.1089/dna.1997.16.769;
RA   Choi I., Troyer D.L., Cornwell D.L., Kirby-Dobbels K.R., Collante W.R.,
RA   Simmen F.A.;
RT   "Closely related genes encode developmental and tissue isoforms of porcine
RT   cytochrome P450 aromatase.";
RL   DNA Cell Biol. 16:769-777(1997).
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   -!- TISSUE SPECIFICITY: Ovary.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U92246; AAB51388.1; -; mRNA.
DR   EMBL; AH006584; AAC48733.1; -; Genomic_DNA.
DR   RefSeq; NP_999596.1; NM_214431.1.
DR   AlphaFoldDB; P79304; -.
DR   SMR; P79304; -.
DR   PeptideAtlas; P79304; -.
DR   PRIDE; P79304; -.
DR   GeneID; 403333; -.
DR   KEGG; ssc:403333; -.
DR   CTD; 403333; -.
DR   InParanoid; P79304; -.
DR   BRENDA; 1.14.14.14; 6170.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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: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; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..501
FT                   /note="Aromatase 3"
FT                   /id="PRO_0000051960"
FT   BINDING         435
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   501 AA;  57915 MW;  AFC6C150BD6E41F9 CRC64;
     MVLEMLNPMN ISSMVSEAVL FGSIAILLLI GLLLWVWNYE DTSSIPGPGY FLGIGPLISH
     FRFLWMGIGS ACNYYNKMYG EFMRVWIGGE ETLIISKSSS IFHIMKHNHY TCRFGSKLGL
     ECIGMHEKGI MFNNNPALWK AVRPFFTKAL SGPGLVRMVT VCADSITKHL DKLEEVRNDL
     GYVDVLTLMR RIMLDTSNNL FLGIPLDESA LVHKVQGYFD AWQALLLKPD IFFKISWLYR
     KYEKSVKDLK DAMEILIEEK RHRISTAEKL EDSMDFTTQL IFAEKRGELT KENVNQCVLE
     MMIAAPDTMS ITVFFMLFLI ANHPQVEEEL MKEIYTVVGE RDIRNDDMQK LKVVENFIYE
     SMRYQPVVDF VMRKALEDDV IDGYPVKKGT NIILNIGRMH RLEFFPKPNE FTLENFAKNV
     PYRYFQPFGF GPRACAGKYI AMVMMKVILV TLLRRFQVQT QQGQCVEKMQ KKNDLSLHPH
     ETSGLLEMIF IPRNSDKCLE H