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 24-JAN-2024, entry version 112. 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 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}. 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 PaxDb; 9823-ENSSSCP00000025837; -. DR GeneID; 403332; -. DR KEGG; ssc:403332; -. DR CTD; 403332; -. DR eggNOG; KOG0157; Eukaryota. DR InParanoid; P79430; -. DR OrthoDB; 5385594at2759; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; 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 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; 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 //