ID   CP192_PIG               Reviewed;         503 AA.
AC   P79430; O02847;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Aromatase 2;
DE            EC=1.14.14.14 {ECO:0000250|UniProtKB:P11511};
DE   AltName: Full=CYPXIXA2;
DE   AltName: Full=Cytochrome P-450AROM;
DE   AltName: Full=Cytochrome P450 19 type II;
DE   AltName: Full=Estrogen synthase;
GN   Name=CYP19A2;
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=Placenta;
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=Liver, and Placenta;
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   -!- 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; U92245; AAB51387.1; -; mRNA.
DR   EMBL; AH006583; AAC48732.1; -; Genomic_DNA.
DR   EMBL; U52142; AAB61697.1; -; mRNA.
DR   RefSeq; NP_999595.1; NM_214430.1.
DR   AlphaFoldDB; P79430; -.
DR   SMR; P79430; -.
DR   STRING; 9823.ENSSSCP00000025837; -.
DR   PaxDb; P79430; -.
DR   GeneID; 403332; -.
DR   KEGG; ssc:403332; -.
DR   CTD; 403332; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   InParanoid; P79430; -.
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..503
FT                   /note="Aromatase 2"
FT                   /id="PRO_0000051959"
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"
FT   CONFLICT        79
FT                   /note="E -> K (in Ref. 1; AAB51387)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        502
FT                   /note="D -> E (in Ref. 1; AAB51387)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  58063 MW;  FAC8821A68AC5F77 CRC64;
     MVLEMLNPMY YKITSMVSEV VPFASIAVLL LTGFLLLLWN YENTSSIPSP GYFLGIGPLI
     SHFRFLWMGI GSACNYYNEM YGEFMRVWIG GEETLIISKS SSVFHVMKHS HYTSRFGSKP
     GLECIGMYEK GIIFNNDPAL WKAVRTYFMK ALSGPGLVRM VTVCADSITK HLDKLEEVRN
     DLGYVDVLTL MRRIMLDTSN NLFLGIPLDE KAIVCKIQGY FDAWQALLLK PEFFFKFSWL
     YKKHKESVKD LKENMEILIE KKRCSIITAE KLEDCMDFAT ELILAEKRGE LTKENVNQCI
     LEMLIAAPDT LSVTVFFMLF LIAKHPQVEE AIVKEIQTVI GERDIRNDDM QKLKVVENFI
     YESMRYQPVV DLVMRKALED DVIDGYPVKK GTNIILNIGR MHRLEFFPKP NEFTLENFAK
     NVPYRYFQPF GFGPRACAGK YIAMVMMKVT LVILLRRFQV QTPQDRCVEK MQKKNDLSLH
     PDETSGLLEM IFIPRNSDKS LDH