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 27-MAR-2024, entry version 188. 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"; 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; 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; 27. 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; DB16536; Birch bark extract. 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; DB00647; Dextropropoxyphene. 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; DB01167; Itraconazole. 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; DB00333; Methadone. 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; 9606-ENSP00000222382; -. DR PeptideAtlas; 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; 164 antibodies from 26 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 AGR; HGNC:17450; -. 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; KDGHADN; -. DR OrthoDB; 1611592at2759; -. 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; 42 hits in 1145 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 cell types or tissues. DR ExpressionAtlas; Q9HB55; baseline and differential. 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:0050649; F:testosterone 6-beta-hydroxylase activity; IBA:GO_Central. DR GO; GO:1903604; P:cytochrome metabolic process; TAS:Reactome. DR GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central. DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central. 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:SF6; CYTOCHROME P450 3A43; 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. DR Genevisible; Q9HB55; HS. 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 //