ID   CP3AS_BOVIN             Reviewed;         507 AA.
AC   P79102;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Cytochrome P450 3A28;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA28;
GN   Name=CYP3A28;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hereford; TISSUE=Liver;
RA   Natsuhori M., van Raak M., Ligtenberg M., Kleij L., ten Berge D.,
RA   Zweers-Zeilmaker W.M., de Groene E.M., van Miert A.S.J.P.A., Witkamp R.F.,
RA   Horbach G.J.M.J.;
RT   "Isolation of a bovine full length cytochrome P450 (CYP3A) cDNA sequence
RT   and its functional expression in V79 cells.";
RL   Environ. Toxicol. Pharmacol. 3:17-24(1997).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       In liver microsomes, this enzyme is involved in an NADPH-dependent
CC       electron transport pathway. It oxidizes a variety of structurally
CC       unrelated compounds, including steroids, fatty acids, and xenobiotics.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: P450 can be induced to high levels in liver and other
CC       tissues by various foreign compounds, including drugs, pesticides, and
CC       carcinogens.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; Y10214; CAA71266.1; -; mRNA.
DR   AlphaFoldDB; P79102; -.
DR   SMR; P79102; -.
DR   STRING; 9913.ENSBTAP00000016177; -.
DR   PaxDb; P79102; -.
DR   PeptideAtlas; P79102; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   InParanoid; P79102; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR008072; Cyt_P450_E_CYP3A.
DR   InterPro; IPR002402; Cyt_P450_E_grp-II.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..507
FT                   /note="Cytochrome P450 3A28"
FT                   /id="PRO_0000051807"
FT   BINDING         442
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   507 AA;  58152 MW;  FDFD8465CC96DF57 CRC64;
     MELIPSFSME TWVLLATSLV LLYIYGTYSY GLFKKLGIPG PRPVPYFGST MAYHKGIPEF
     DNQCFKKYGK MWGFYEGRQP MLAITDPDII KTVLVKECYS VFTNRRIFGP MGIMKYAISL
     AWDEQWKRIR TLLSPAFTSG KLKEMFPIIG QYGDMLVRNL RKEAEKGNPV NMKDMFGAYS
     MDVITGTAFG VNIDSLNNPH DPFVEHSKNL LRFRPFDPFI LSIILFPFLN PVFEILNITL
     FPKSTVDFFT KSVKKIKESR LTDKQMNRVD LLQLMINSQN SKEIDNHKAL SDIELVAQST
     IFIFGGYETT SSTLSFIIYE LTTHPHVQQK LQEEIDATFP NKAPPTYDAL VQMEYLDMVV
     NETLRMFPIA GRLERVCKKD VEIHGVTIPK GTTVLVPLFV LHNNPELWPE PEEFRPERFS
     KNNKDSINPY VYLPFGTGPR NCLGMRFAIM NIKLALVRIL QNFSFKPCKE TQIPLKLYTQ
     GLTQPEQPVI LKVVPRGLGP QVEPDFL