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   27-MAR-2024, entry version 109.
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}.
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; U59378; AAB02657.1; -; mRNA.
DR   RefSeq; NP_001123376.1; NM_001129904.1.
DR   AlphaFoldDB; Q29496; -.
DR   SMR; Q29496; -.
DR   STRING; 9940.ENSOARP00000019638; -.
DR   PaxDb; 9940-ENSOARP00000019638; -.
DR   Ensembl; ENSOART00020033672; ENSOARP00020027805; ENSOARG00020021603.
DR   GeneID; 100170111; -.
DR   KEGG; oas:100170111; -.
DR   CTD; 517246; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   OrthoDB; 1611592at2759; -.
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   CDD; cd20650; CYP3A; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24302:SF38; CYTOCHROME P450 3A7; 1.
DR   PANTHER; PTHR24302; CYTOCHROME P450 FAMILY 3; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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
//