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Database: UniProt
Entry: F6UET4_HORSE
LinkDB: F6UET4_HORSE
Original site: F6UET4_HORSE 
ID   F6UET4_HORSE            Unreviewed;       503 AA.
AC   F6UET4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Cytochrome P450 3A {ECO:0000256|RuleBase:RU368049};
DE            EC=1.14.14.- {ECO:0000256|RuleBase:RU368049};
GN   Name=LOC102149219 {ECO:0000313|Ensembl:ENSECAP00000018171.2};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000018171.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000018171.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018171.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000018171.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018171.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00037347, ECO:0000256|RuleBase:RU368049}.
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         Evidence={ECO:0000256|RuleBase:RU368049};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602402-1, ECO:0000256|RuleBase:RU368049};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU368049}. Microsome membrane
CC       {ECO:0000256|RuleBase:RU368049}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   AlphaFoldDB; F6UET4; -.
DR   Ensembl; ENSECAT00000022011.4; ENSECAP00000018171.2; ENSECAG00000037404.3.
DR   GeneTree; ENSGT00950000182958; -.
DR   HOGENOM; CLU_001570_5_2_1; -.
DR   OMA; TCLEYRK; -.
DR   OrthoDB; 1611592at2759; -.
DR   TreeFam; TF105087; -.
DR   Proteomes; UP000002281; Chromosome 13.
DR   Bgee; ENSECAG00000037404; Expressed in liver and 9 other cell types or tissues.
DR   ExpressionAtlas; F6UET4; baseline.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
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 3A4; 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   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU368049};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602402-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602402-1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602402-1};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848, ECO:0000256|RuleBase:RU368049};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
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:0000256|PIRSR:PIRSR602402-1"
SQ   SEQUENCE   503 AA;  57503 MW;  4607DBD1C42A909A CRC64;
     MDLIPSFSTE TWVLLATSLV LIYLYGTYTH GLFKKLGIPG PTPLPFFGNV LSYRKGIWNF
     DRKCFKKYGK MWGVYDGRRP VLAVTDPDMI KTVLVKECYS VFTNRRPFRP VGFMKSAISL
     SEDEEWKRIR TLLSPTFTSG KLKEMFTIIG QYGDVLVRNL RKEAEKGKPV TLKDIFGAYS
     MDVITSTSFG VNIDSLNNPQ DPFVENSNKL LRFDFLNPLI LLMVLFPFLQ PIFEVLNISL
     FPKSAIDFFT KSVKRMKESR LKDKDKHRVD FLQLMINSQN SKELDTHKGL SDLELVAQSI
     VFIFAGYETT STSLSFLLYL LATHPDVQQK LQEEIDAIFP NKAPPTYDAL VQMDYLDMVL
     NESLRLFPVA VRLERVCKKD AEINGVFIPK GTVVMVPTFS LHRASEFWPE PEEFRPERFS
     KKNKDNINPC IYMPFGNGPR NCIGMRFAMV NMKLALVRVL QNFSFKPCKE TQIPLKLGNQ
     GLLQPQKPIV LKVESRDGTV NGA
//
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