CP343_HUMAN
ID CP343_HUMAN Reviewed; 503 AA.
AC Q9HB55; Q495Y1; Q75MK2; Q75MK3; Q9HB52; Q9HB53; Q9HB54; Q9HB57;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Cytochrome P450 3A43;
DE EC=1.14.14.1;
GN Name=CYP3A43;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP CHARACTERIZATION.
RX PubMed=11160876; DOI=10.1124/mol.59.2.386;
RA Domanski T.L., Finta C., Halpert J.R., Zaphiropoulos P.G.;
RT "cDNA cloning and initial characterization of CYP3A43, a novel human
RT cytochrome P450.";
RL Mol. Pharmacol. 59:386-392(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11243885; DOI=10.1006/bbrc.2001.4505;
RA Westlind A., Malmebo S., Johansson I., Otter C., Andersson T.B.,
RA Ingelman-Sundberg M., Oscarson M.;
RT "Cloning and tissue distribution of a novel human cytochrome P450 of the
RT CYP3A subfamily, CYP3A43.";
RL Biochem. Biophys. Res. Commun. 281:1349-1355(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Liver;
RX PubMed=11266076; DOI=10.1097/00008571-200103000-00002;
RA Gellner K., Eiselt R., Hustert E., Arnold H., Koch I., Haberl M.,
RA Deglmann C.J., Burk O., Buntefuss D., Escher S., Bishop C., Koebe H.-G.,
RA Brinkmann U., Klenk H.-P., Kleine K., Meyer U.A., Wojnowski L.;
RT "Genomic organization of the human CYP3A locus: identification of a new,
RT inducible CYP3A gene.";
RL Pharmacogenetics 11:111-121(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CYP3A43*2), AND VARIANT CYP3A43*3
RP ALA-340.
RX PubMed=14695544; DOI=10.1002/humu.9211;
RA Cauffiez C., Lo-Guidice J.-M., Chevalier D., Allorge D., Hamdan R.,
RA Lhermitte M., Lafitte J.-J., Colombel J.-F., Libersa C., Broly F.;
RT "First report of a genetic polymorphism of the cytochrome P450 3A43
RT (CYP3A43) gene: identification of a loss-of-function variant.";
RL Hum. Mutat. 23:101-101(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP TRANS-SPLICING.
RX PubMed=11726664; DOI=10.1074/jbc.m109175200;
RA Finta C., Zaphiropoulos P.G.;
RT "Intergenic mRNA molecules resulting from trans-splicing.";
RL J. Biol. Chem. 277:5882-5890(2002).
RN [9]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
CC -!- FUNCTION: Exhibits low testosterone 6-beta-hydroxylase activity.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9HB55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HB55-2; Sequence=VSP_000609;
CC Name=3;
CC IsoId=Q9HB55-3; Sequence=VSP_000610, VSP_000611;
CC Name=4;
CC IsoId=Q9HB55-4; Sequence=VSP_000612, VSP_000613;
CC Name=7;
CC IsoId=Q9HB55-6; Sequence=VSP_056736;
CC -!- TISSUE SPECIFICITY: Highest expression level in prostate. Also
CC expressed in liver, kidney, pancreas, fetal liver and fetal skeletal
CC muscle. {ECO:0000269|PubMed:11160876, ECO:0000269|PubMed:11243885}.
CC -!- INDUCTION: By rifampicin.
CC -!- POLYMORPHISM: At protein level, three alleles are known: CYP3A43*1,
CC CYP3A43*2 and CYP3A43*3. The sequence shown is that of CYP3A43*1, which
CC is the most frequent allele. The allele CYP3A43*2 is likely to be non-
CC functional.
CC -!- MISCELLANEOUS: Chimeric transcripts, characterized by CYP3A43 exon 1
CC joined at canonical splice sites to distinct sets of CYP3A4 or CYP3A5
CC exons, have been detected. All are possibly produced by trans-splicing.
CC CYP3A43-CYP3A4 chimeric transcripts exist in 3 different combinations:
CC CYP3A43 exon 1 joined in frame to CYP3A4 exons 2-13, CYP3A43 exon 1
CC joined in frame to CYP3A4 exons 4-13 and CYP3A43 exon 1 joined in frame
CC to CYP3A4 exon 7-13. The longest chimeric isoform (CYP3A43 exon 1
CC joined to CYP3A4 exons 2-13) exhibits 6-beta-hydroxylase activity,
CC while a shorter isoform (CYP3A43 exon 1 joined to CYP3A4 exons 4-13)
CC does not. CYP3A43-CYP3A5 chimeric transcripts exist in 2 different
CC combinations: CYP3A43 exon 1 joined in frame to CYP3A5 exon 11-13 and
CC CYP3A43 exon 1 joined in frame to CYP3A5 exon 12-13. All chimeric
CC transcripts are expressed at very low levels in the liver
CC (PubMed:11726664). {ECO:0000305|PubMed:11726664}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=PharmVar Pharmacogen Variation Consortium;
CC Note=CYP3A43 alleles;
CC URL="https://www.pharmvar.org/gene/CYP3A43";
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DR EMBL; AF319634; AAK00325.1; -; mRNA.
DR EMBL; AF337813; AAK38841.1; -; mRNA.
DR EMBL; AF280107; AAG32291.1; -; Genomic_DNA.
DR EMBL; AF280108; AAG33009.1; -; mRNA.
DR EMBL; AF280109; AAG33010.1; -; mRNA.
DR EMBL; AF280110; AAG33011.1; -; mRNA.
DR EMBL; AF280111; AAG33012.1; -; mRNA.
DR EMBL; AY390423; AAQ92351.1; -; mRNA.
DR EMBL; AY390424; AAQ92352.1; -; mRNA.
DR EMBL; AY390425; AAQ92353.1; -; mRNA.
DR EMBL; AY390426; AAQ92354.1; -; mRNA.
DR EMBL; AC011904; AAS07394.1; -; Genomic_DNA.
DR EMBL; AC011904; AAS07395.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76632.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76634.1; -; Genomic_DNA.
DR EMBL; BC100981; AAI00982.1; -; mRNA.
DR CCDS; CCDS5675.1; -. [Q9HB55-2]
DR CCDS; CCDS5676.1; -. [Q9HB55-1]
DR CCDS; CCDS5677.1; -. [Q9HB55-3]
DR CCDS; CCDS64723.1; -. [Q9HB55-6]
DR PIR; JC7627; JC7627.
DR RefSeq; NP_001265850.1; NM_001278921.1. [Q9HB55-6]
DR RefSeq; NP_073731.1; NM_022820.4. [Q9HB55-2]
DR RefSeq; NP_476436.1; NM_057095.2. [Q9HB55-1]
DR RefSeq; NP_476437.1; NM_057096.3. [Q9HB55-3]
DR AlphaFoldDB; Q9HB55; -.
DR SMR; Q9HB55; -.
DR BioGRID; 122311; 26.
DR IntAct; Q9HB55; 1.
DR STRING; 9606.ENSP00000222382; -.
DR BindingDB; Q9HB55; -.
DR ChEMBL; CHEMBL5792; -.
DR DrugBank; DB11703; Acalabrutinib.
DR DrugBank; DB13141; Ambroxol acefyllinate.
DR DrugBank; DB12267; Brigatinib.
DR DrugBank; DB01222; Budesonide.
DR DrugBank; DB09065; Cobicistat.
DR DrugBank; DB08865; Crizotinib.
DR DrugBank; DB09102; Daclatasvir.
DR DrugBank; DB01234; Dexamethasone.
DR DrugBank; DB14649; Dexamethasone acetate.
DR DrugBank; DB11994; Diacerein.
DR DrugBank; DB08930; Dolutegravir.
DR DrugBank; DB11742; Ebastine.
DR DrugBank; DB11979; Elagolix.
DR DrugBank; DB11574; Elbasvir.
DR DrugBank; DB00593; Ethosuximide.
DR DrugBank; DB00176; Fluvoxamine.
DR DrugBank; DB12307; Foretinib.
DR DrugBank; DB13879; Glecaprevir.
DR DrugBank; DB09054; Idelalisib.
DR DrugBank; DB11757; Istradefylline.
DR DrugBank; DB11951; Lemborexant.
DR DrugBank; DB12070; Letermovir.
DR DrugBank; DB06448; Lonafarnib.
DR DrugBank; DB01601; Lopinavir.
DR DrugBank; DB12130; Lorlatinib.
DR DrugBank; DB09212; Loxoprofen.
DR DrugBank; DB00643; Mebendazole.
DR DrugBank; DB00959; Methylprednisolone.
DR DrugBank; DB06595; Midostaurin.
DR DrugBank; DB11792; Mirodenafil.
DR DrugBank; DB09205; Moxisylyte.
DR DrugBank; DB11605; Myrrh.
DR DrugBank; DB11691; Naldemedine.
DR DrugBank; DB01149; Nefazodone.
DR DrugBank; DB09048; Netupitant.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB09568; Omega-3-carboxylic acids.
DR DrugBank; DB06412; Oxymetholone.
DR DrugBank; DB00780; Phenelzine.
DR DrugBank; DB13878; Pibrentasvir.
DR DrugBank; DB01058; Praziquantel.
DR DrugBank; DB14631; Prednisolone phosphate.
DR DrugBank; DB00635; Prednisone.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB11853; Relugolix.
DR DrugBank; DB00409; Remoxipride.
DR DrugBank; DB13174; Rhein.
DR DrugBank; DB01045; Rifampicin.
DR DrugBank; DB01201; Rifapentine.
DR DrugBank; DB15305; Risdiplam.
DR DrugBank; DB12332; Rucaparib.
DR DrugBank; DB15685; Selpercatinib.
DR DrugBank; DB15569; Sotorasib.
DR DrugBank; DB12887; Tazemetostat.
DR DrugBank; DB00624; Testosterone.
DR DrugBank; DB13943; Testosterone cypionate.
DR DrugBank; DB13944; Testosterone enanthate.
DR DrugBank; DB13946; Testosterone undecanoate.
DR DrugBank; DB00599; Thiopental.
DR DrugBank; DB13179; Troleandomycin.
DR DrugBank; DB11652; Tucatinib.
DR DrugBank; DB01586; Ursodeoxycholic acid.
DR DrugBank; DB15035; Zanubrutinib.
DR DrugCentral; Q9HB55; -.
DR iPTMnet; Q9HB55; -.
DR PhosphoSitePlus; Q9HB55; -.
DR BioMuta; CYP3A43; -.
DR DMDM; 20137481; -.
DR jPOST; Q9HB55; -.
DR MassIVE; Q9HB55; -.
DR PaxDb; Q9HB55; -.
DR PeptideAtlas; Q9HB55; -.
DR PRIDE; Q9HB55; -.
DR ProteomicsDB; 61978; -.
DR ProteomicsDB; 81485; -. [Q9HB55-1]
DR ProteomicsDB; 81486; -. [Q9HB55-2]
DR ProteomicsDB; 81487; -. [Q9HB55-3]
DR ProteomicsDB; 81488; -. [Q9HB55-4]
DR Antibodypedia; 30450; 135 antibodies from 25 providers.
DR DNASU; 64816; -.
DR Ensembl; ENST00000222382.5; ENSP00000222382.5; ENSG00000021461.18. [Q9HB55-2]
DR Ensembl; ENST00000312017.9; ENSP00000312110.5; ENSG00000021461.18. [Q9HB55-3]
DR Ensembl; ENST00000354829.7; ENSP00000346887.3; ENSG00000021461.18. [Q9HB55-1]
DR Ensembl; ENST00000417625.5; ENSP00000416581.1; ENSG00000021461.18. [Q9HB55-6]
DR Ensembl; ENST00000434806.5; ENSP00000411653.1; ENSG00000021461.18. [Q9HB55-4]
DR GeneID; 64816; -.
DR KEGG; hsa:64816; -.
DR MANE-Select; ENST00000354829.7; ENSP00000346887.3; NM_057095.3; NP_476436.1.
DR UCSC; uc003urx.3; human. [Q9HB55-1]
DR CTD; 64816; -.
DR DisGeNET; 64816; -.
DR GeneCards; CYP3A43; -.
DR HGNC; HGNC:17450; CYP3A43.
DR HPA; ENSG00000021461; Tissue enriched (liver).
DR MIM; 606534; gene.
DR neXtProt; NX_Q9HB55; -.
DR OpenTargets; ENSG00000021461; -.
DR PharmGKB; PA427; -.
DR VEuPathDB; HostDB:ENSG00000021461; -.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00950000182958; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q9HB55; -.
DR OMA; CITWFGT; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; Q9HB55; -.
DR TreeFam; TF105087; -.
DR PathwayCommons; Q9HB55; -.
DR Reactome; R-HSA-211958; Miscellaneous substrates.
DR Reactome; R-HSA-211981; Xenobiotics.
DR SignaLink; Q9HB55; -.
DR BioGRID-ORCS; 64816; 41 hits in 1064 CRISPR screens.
DR GeneWiki; CYP3A43; -.
DR GenomeRNAi; 64816; -.
DR Pharos; Q9HB55; Tclin.
DR PRO; PR:Q9HB55; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9HB55; protein.
DR Bgee; ENSG00000021461; Expressed in liver and 115 other tissues.
DR ExpressionAtlas; Q9HB55; baseline and differential.
DR Genevisible; Q9HB55; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; IBA:GO_Central.
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 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 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..503
FT /note="Cytochrome P450 3A43"
FT /id="PRO_0000051814"
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"
FT VAR_SEQ 56..224
FT /note="GLWNFDRECNEKYGEMWGLYEGQQPMLVIMDPDMIKTVLVKECYSVFTNQMP
FT LGPMGFLKSALSFAEDEEWKRIRTLLSPAFTSVKFKEMVPIISQCGDMLVRSLRQEAEN
FT SKSINLKDFFGAYTMDVITGTLFGVNLDSLNNPQDPFLKNMKKLLKLDFLDPFLLLIS
FT -> RSLNKIPSWAWWLTPVIPALWEAEAGGSPKVRSSRPALPTWVFGILTENVMKNTEK
FT CGA (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056736"
FT VAR_SEQ 224..250
FT /note="SLFPFLTPVFEALNIGLFPKDVTHFLK -> YRVSLCCLGRSAWCDLGSLKP
FT PPPGFE (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_000612"
FT VAR_SEQ 251..503
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_000613"
FT VAR_SEQ 417
FT /note="E -> ES (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000609"
FT VAR_SEQ 419..420
FT /note="FS -> SH (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_000610"
FT VAR_SEQ 421..503
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_000611"
FT VARIANT 25..88
FT /note="YGTHSHKLFKKLGIPGPTPLPFLGTILFYLRGLWNFDRECNEKYGEMWGLYE
FT GQQPMLVIMDPD -> LGPIHINFLRSWEFLGQPLCLFWELFCSTLGVFGILTENVMKN
FT TEKCGGCMRGNSPCWSSWIPT (in allele CYP3A43*2)"
FT /id="VAR_018050"
FT VARIANT 27
FT /note="T -> A (in dbSNP:rs45558032)"
FT /id="VAR_048449"
FT VARIANT 89..503
FT /note="Missing (in allele CYP3A43*2)"
FT /id="VAR_018051"
FT VARIANT 145
FT /note="M -> I (in dbSNP:rs45450092)"
FT /id="VAR_048450"
FT VARIANT 275
FT /note="M -> I (in dbSNP:rs45621431)"
FT /id="VAR_048451"
FT VARIANT 340
FT /note="P -> A (in allele CYP3A43*3; dbSNP:rs680055)"
FT /evidence="ECO:0000269|PubMed:14695544"
FT /id="VAR_018052"
SQ SEQUENCE 503 AA; 57670 MW; 2C585B9DC573F634 CRC64;
MDLIPNFAME TWVLVATSLV LLYIYGTHSH KLFKKLGIPG PTPLPFLGTI LFYLRGLWNF
DRECNEKYGE MWGLYEGQQP MLVIMDPDMI KTVLVKECYS VFTNQMPLGP MGFLKSALSF
AEDEEWKRIR TLLSPAFTSV KFKEMVPIIS QCGDMLVRSL RQEAENSKSI NLKDFFGAYT
MDVITGTLFG VNLDSLNNPQ DPFLKNMKKL LKLDFLDPFL LLISLFPFLT PVFEALNIGL
FPKDVTHFLK NSIERMKESR LKDKQKHRVD FFQQMIDSQN SKETKSHKAL SDLELVAQSI
IIIFAAYDTT STTLPFIMYE LATHPDVQQK LQEEIDAVLP NKAPVTYDAL VQMEYLDMVV
NETLRLFPVV SRVTRVCKKD IEINGVFIPK GLAVMVPIYA LHHDPKYWTE PEKFCPERFS
KKNKDSIDLY RYIPFGAGPR NCIGMRFALT NIKLAVIRAL QNFSFKPCKE TQIPLKLDNL
PILQPEKPIV LKVHLRDGIT SGP
