CP3AO_SHEEP
ID CP3AO_SHEEP Reviewed; 503 AA.
AC Q29496;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome P450 3A24;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA24;
GN Name=CYP3A24;
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 [MRNA].
RC TISSUE=Liver;
RA Ching M.S., Chun-Jing J., Ghabrial H., Wookey P.J., Smallwood R.A.,
RA Morgan D.J.;
RT "Ovine foetal liver CYP3A24.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
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; U59378; AAB02657.1; -; mRNA.
DR RefSeq; NP_001123376.1; NM_001129904.1.
DR AlphaFoldDB; Q29496; -.
DR SMR; Q29496; -.
DR STRING; 9940.ENSOARP00000019638; -.
DR Ensembl; ENSOART00020033672; ENSOARP00020027805; ENSOARG00020021603.
DR GeneID; 100170111; -.
DR KEGG; oas:100170111; -.
DR CTD; 517246; -.
DR eggNOG; KOG0158; Eukaryota.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000002356; 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:0004497; F:monooxygenase activity; ISS:UniProtKB.
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..503
FT /note="Cytochrome P450 3A24"
FT /id="PRO_0000051804"
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 503 AA; 57360 MW; 804223EAD0304238 CRC64;
MELIPSFSLE TWVLLAISLV LLYLYGTYSH GLFKKLGVSG PRPLPYFGNV LSYRKGVCEF
DEECFKKYGK MWGVFEGKQP LLVITDPDVI KTVLVKECYS VFTNRRVFGP MGIMKNAVSV
AEDEQWKRIR TLLSPTFTSG KLKDMFPIIG KYGDVLVRNL RKEAEKGKSV NMKDIFGAYS
MDVITSTSFG VNIDSLGNPQ DPFVENAKKL LRFNILDPFL LSVVLFPFLV PIFEVLNITM
FPKSAVDFLT KSVKRIKESR LKDNQKPRVD FLQLMINSQN SKETDNHKAL SDQELMAQSV
IFIFAGYETT SNTLSFLLYI LATHPDVQQK LQEEIDATFP NKAPPTYDVL AQMEYLDMVV
NETLRMFPIA VRLDRLCKKD VEIHGVSIPK GTAVTVPIFV LHRDPQLWPE PEEFRPERFS
KKNKDSINPY VYLPFGTGPR NCIGMRFAIM NMKLAIVRVL QNFSFKPCKE TQIPLKINSQ
GLIRPEKPIF LKVVLRDETI SGA