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CP19A_SHEEP
ID   CP19A_SHEEP             Reviewed;         503 AA.
AC   Q9XS28;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=11850234; DOI=10.1016/s0960-0760(01)00144-3;
RA   Vanselow J., Furbass R., Zsolnai A., Kalbe C., Said H.M., Schwerin M.;
RT   "Expression of the aromatase cytochrome P450 encoding gene in cattle and
RT   sheep.";
RL   J. Steroid Biochem. Mol. Biol. 79:279-288(2001).
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; AJ012144; CAB40563.1; -; Genomic_DNA.
DR   EMBL; AJ012145; CAB40563.1; JOINED; Genomic_DNA.
DR   EMBL; AJ012146; CAB40563.1; JOINED; Genomic_DNA.
DR   EMBL; AJ012147; CAB40563.1; JOINED; Genomic_DNA.
DR   EMBL; AJ012148; CAB40563.1; JOINED; Genomic_DNA.
DR   EMBL; AJ012149; CAB40563.1; JOINED; Genomic_DNA.
DR   EMBL; AJ012150; CAB40563.1; JOINED; Genomic_DNA.
DR   EMBL; AJ012151; CAB40563.1; JOINED; Genomic_DNA.
DR   EMBL; AJ012152; CAB40563.1; JOINED; Genomic_DNA.
DR   EMBL; AJ012153; CAB40543.1; -; mRNA.
DR   RefSeq; NP_001116472.1; NM_001123000.1.
DR   AlphaFoldDB; Q9XS28; -.
DR   SMR; Q9XS28; -.
DR   STRING; 9940.ENSOARP00000022542; -.
DR   Ensembl; ENSOART00020040485; ENSOARP00020033560; ENSOARG00020025784.
DR   GeneID; 100144423; -.
DR   KEGG; oas:100144423; -.
DR   CTD; 100144423; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   OrthoDB; 1247045at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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..503
FT                   /note="Aromatase"
FT                   /id="PRO_0000051963"
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;  57970 MW;  FA9FC7510691B3D8 CRC64;
     MLLEVLNPRH YNVTSMVSEV VPIASIAILL LTGFLLLVWN YEDTSSIPGP SYFLGIGPLI
     SHCRFLWMGI GSACNYYNKM YGEFMRVWVC GEETLIISKS SSMFHVMKHS HYISRFGSKL
     GLQFIGMHEK GIIFNNNPAL WKAVRPFFTK ALSGPGLVRM VTICADSITK HLDRLEEVCN
     DLGYVDVLTL MRRIMLDTSN ILFLGIPLDE SAIVVKIQGY FDAWQALLLK PDIFFKISWL
     CRKYEKSVKD LKDAMEILIE EKRHRISTAE KLEDCIDFAT ELIFAEKRGE LTKENVNQCI
     LEMLIAAPDT MSVSVFFMLF LIAKHPQVEE AMMREIQTVV GERDIRIDDM QKLKVVENFI
     NESMRYQPVV DLVMRKALED DVIDGYPVKK GTNIILNLGR MHRLEFFPKP NEFTLENFAK
     NVPYRYFQPF GFGPRACAGK YIAMVMMKVI LVTLLRRFHV QTLQGRCVEK MQKKNDLSLH
     PDETSDRLEM IFIPRNSDKC LEC
 
 
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