ID UD16_HUMAN Reviewed; 532 AA. AC P19224; A6NKK6; B8K289; Q96TE7; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 11-APR-2003, sequence version 2. DT 27-MAR-2024, entry version 205. DE RecName: Full=UDP-glucuronosyltransferase 1-6; DE Short=UDPGT 1-6; DE Short=UGT1*6; DE Short=UGT1-06; DE Short=UGT1.6; DE EC=2.4.1.17; DE AltName: Full=Phenol-metabolizing UDP-glucuronosyltransferase; DE AltName: Full=UDP-glucuronosyltransferase 1-F; DE Short=UGT-1F; DE Short=UGT1F; DE AltName: Full=UDP-glucuronosyltransferase 1A6; DE Flags: Precursor; GN Name=UGT1A6; Synonyms=GNT1, UGT1; 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 [GENOMIC DNA], TISSUE SPECIFICITY, AND VARIANTS TYR-70 RP AND PRO-510. RX PubMed=1339448; DOI=10.1016/s0021-9258(19)50724-4; RA Ritter J.K., Chen F., Sheen Y.Y., Tran H.M., Kimura S., Yeatman M.T., RA Owens I.S.; RT "A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP- RT glucuronosyltransferase isozymes with identical carboxyl termini."; RL J. Biol. Chem. 267:3257-3261(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=3141926; DOI=10.1073/pnas.85.22.8381; RA Harding D., Fournel-Gigleux S., Jackson M.R., Burchell B.; RT "Cloning and substrate specificity of a human phenol UDP- RT glucuronosyltransferase expressed in COS-7 cells."; RL Proc. Natl. Acad. Sci. U.S.A. 85:8381-8385(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11434514; DOI=10.1097/00008571-200106000-00011; RA Gong Q.H., Cho J.W., Huang T., Potter C., Gholami N., Basu N.K., Kubota S., RA Carvalho S., Pennington M.W., Owens I.S., Popescu N.C.; RT "Thirteen UDP-glucuronosyltransferase genes are encoded at the human UGT1 RT gene complex locus."; RL Pharmacogenetics 11:357-368(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS ALA-181 AND SER-184. RA Guillemette C., Levesque E., Girard H., Bernard O.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-488 (ISOFORM 2). 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. RX PubMed=9466822; DOI=10.1006/abbi.1997.0485; RA Muenzel P.A., Lehmkoester T., Brueck M., Ritter J.K., Bock K.W.; RT "Aryl hydrocarbon receptor-inducible or constitutive expression of human RT UDP glucuronosyltransferase UGT1A6."; RL Arch. Biochem. Biophys. 350:72-78(1998). RN [8] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=18004212; DOI=10.1097/fpc.0b013e3282f1f118; RA Girard H., Levesque E., Bellemare J., Journault K., Caillier B., RA Guillemette C.; RT "Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative RT splicing mechanism leading to nine additional UGT1A proteins that act as RT regulators of glucuronidation activity."; RL Pharmacogenet. Genomics 17:1077-1089(2007). RN [9] RP SUBUNIT. RX PubMed=20610558; DOI=10.1124/dmd.110.034835; RA Bellemare J., Rouleau M., Girard H., Harvey M., Guillemette C.; RT "Alternatively spliced products of the UGT1A gene interact with the RT enzymatically active proteins to inhibit glucuronosyltransferase activity RT in vitro."; RL Drug Metab. Dispos. 38:1785-1789(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP VARIANTS ALA-181 AND SER-184. RX PubMed=9429234; DOI=10.1097/00008571-199712000-00007; RA Ciotti M., Marrone A., Potter C., Owens I.S.; RT "Genetic polymorphism in the human UGT1A6 (planar phenol) UDP- RT glucuronosyltransferase: pharmacological implications."; RL Pharmacogenetics 7:485-495(1997). RN [12] RP VARIANTS ALA-7; ALA-181 AND SER-184. RX PubMed=15284531; DOI=10.1097/01.fpc.0000114771.78957.cb; RA Nagar S., Zalatoris J.J., Blanchard R.L.; RT "Human UGT1A6 pharmacogenetics: identification of a novel SNP, RT characterization of allele frequencies and functional analysis of RT recombinant allozymes in human liver tissue and in cultured cells."; RL Pharmacogenetics 14:487-499(2004). RN [13] RP VARIANTS ALA-181 AND SER-184. RX PubMed=19204906; DOI=10.1002/humu.20946; RA Menard V., Girard H., Harvey M., Perusse L., Guillemette C.; RT "Analysis of inherited genetic variations at the UGT1 locus in the French- RT Canadian population."; RL Hum. Mutat. 30:677-687(2009). CC -!- FUNCTION: UDPGT is of major importance in the conjugation and CC subsequent elimination of potentially toxic xenobiotics and endogenous CC compounds. This isoform has specificity for phenols. Isoform 3 lacks CC transferase activity but acts as a negative regulator of isoform 1 (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor CC beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; CC -!- SUBUNIT: Isoform 1 interacts with isoform 3/i2 suggesting that CC oligomerization is involved in negative regulation of transferase CC activity by isoform 3. Isoform 1 also interacts with respective i2 CC isoforms of UGT1A1, UGT1A3, UGT1A4, UGT1A7, UGT1A8, UGT1A9 and UGT1A10. CC {ECO:0000269|PubMed:20610558}. CC -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=i1; CC IsoId=P19224-1; Sequence=Displayed; CC Name=2; CC IsoId=P19224-2; Sequence=VSP_045779; CC Name=3; Synonyms=i2, UGT1A6s; CC IsoId=P19224-3; Sequence=VSP_053962; CC -!- TISSUE SPECIFICITY: Expressed in skin. Isoforms 1 and 3 are expressed CC in kidney and liver. Isoform 1 but not isoform 2 is expressed in colon, CC esophagus and small intestine. {ECO:0000269|PubMed:1339448, CC ECO:0000269|PubMed:18004212}. CC -!- POLYMORPHISM: Polymorphisms in the UGT1A6 gene define four common CC haplotypes: UGT1A6*1, UGT1A6*2, UGT1A6*3 and UGT1A6*4. Liver tissue CC samples that were homozygous for UGT1A6*2 exhibited a high rate of CC glucuronidation relative to tissues with other genotypes. Biochemical CC kinetic studies indicate that the UGT1A6*2 allozyme, expressed CC homozygously, had almost two-fold greater activity toward p-nitrophenol CC than UGT1A6*1 and when expressed heterozygously (UGT1A6*1/*2) it is CC associated with low enzyme activity. Common genetic variation in UGT1A6 CC confers functionally significant differences in biochemical phenotype. CC This genetic variation might impact clinical efficacy or toxicity of CC drugs metabolized by UGT1A6. {ECO:0000269|PubMed:15284531, CC ECO:0000269|PubMed:9429234}. CC -!- MISCELLANEOUS: The gene is part of the UGT1A complex locus which CC displays alternative use of promoters, first exons and terminal exons. CC The locus is defined by 13 first exons, which are alternatively spliced CC to 3 other common exons and 2 alternative terminal exons 5. From the 27 CC possible mRNA isoforms, 9 produce functionally active polypeptides CC (UGT1A1, 1A3, 1A4, 1A5, 1A6, 1A7, 1A8, 1A9 and 1A10) called isoforms 1 CC (i1). Use of an alternative exon 5 (5b) as terminal exon is leading to CC 9 additional alternatively spliced products termed isoforms i2 and CC which lack transferase activity. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BM924331; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC Sequence=BM924331; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BM924331; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={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; M84130; AAC41717.1; -; Genomic_DNA. DR EMBL; M84124; AAA61247.1; ALT_SEQ; Genomic_DNA. DR EMBL; M84122; AAA61247.1; JOINED; Genomic_DNA. DR EMBL; M84123; AAA61247.1; JOINED; Genomic_DNA. DR EMBL; J04093; AAA61251.1; -; mRNA. DR EMBL; AF297093; AAG30420.1; -; Genomic_DNA. DR EMBL; DQ364250; ABC96774.1; -; mRNA. DR EMBL; AC006985; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC114812; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BM924331; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF014112; AAB87411.1; -; Genomic_DNA. DR CCDS; CCDS2507.1; -. [P19224-1] DR CCDS; CCDS2508.1; -. [P19224-2] DR PIR; A31340; A31340. DR RefSeq; NP_001063.2; NM_001072.3. [P19224-1] DR AlphaFoldDB; P19224; -. DR SMR; P19224; -. DR BioGRID; 120056; 1. DR IntAct; P19224; 7. DR STRING; 9606.ENSP00000303174; -. DR BindingDB; P19224; -. DR ChEMBL; CHEMBL1743316; -. DR DrugBank; DB00316; Acetaminophen. DR DrugBank; DB00945; Acetylsalicylic acid. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB00564; Carbamazepine. DR DrugBank; DB14635; Curcumin sulfate. DR DrugBank; DB08826; Deferiprone. DR DrugBank; DB12243; Edaravone. DR DrugBank; DB00783; Estradiol. DR DrugBank; DB15598; Ferric maltol. DR DrugBank; DB01320; Fosphenytoin. DR DrugBank; DB11796; Fostemsavir. DR DrugBank; DB12471; Ibrexafungerp. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB00688; Mycophenolate mofetil. DR DrugBank; DB01024; Mycophenolic acid. DR DrugBank; DB00788; Naproxen. DR DrugBank; DB00252; Phenytoin. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB00794; Primidone. DR DrugBank; DB09288; Propacetamol. DR DrugBank; DB00818; Propofol. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB00871; Terbutaline. DR DrugBank; DB00197; Troglitazone. DR DrugBank; DB00313; Valproic acid. DR DrugCentral; P19224; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR GlyConnect; 1878; 2 N-Linked glycans (1 site). DR GlyCosmos; P19224; 2 sites, 2 glycans. DR GlyGen; P19224; 2 sites, 2 N-linked glycans (1 site). DR iPTMnet; P19224; -. DR PhosphoSitePlus; P19224; -. DR BioMuta; UGT1A6; -. DR DMDM; 29840832; -. DR EPD; P19224; -. DR jPOST; P19224; -. DR MassIVE; P19224; -. DR MaxQB; P19224; -. DR PaxDb; 9606-ENSP00000303174; -. DR PeptideAtlas; P19224; -. DR ProteomicsDB; 1419; -. DR ProteomicsDB; 53637; -. [P19224-1] DR Antibodypedia; 4074; 157 antibodies from 27 providers. DR DNASU; 54578; -. DR Ensembl; ENST00000305139.11; ENSP00000303174.6; ENSG00000167165.19. [P19224-1] DR Ensembl; ENST00000373424.5; ENSP00000362523.1; ENSG00000167165.19. [P19224-2] DR GeneID; 54578; -. DR KEGG; hsa:54578; -. DR MANE-Select; ENST00000305139.11; ENSP00000303174.6; NM_001072.4; NP_001063.2. DR UCSC; uc002vuu.4; human. [P19224-1] DR AGR; HGNC:12538; -. DR CTD; 54578; -. DR DisGeNET; 54578; -. DR GeneCards; UGT1A6; -. DR HGNC; HGNC:12538; UGT1A6. DR HPA; ENSG00000167165; Group enriched (kidney, liver, urinary bladder). DR MalaCards; UGT1A6; -. DR MIM; 191740; gene. DR MIM; 606431; gene. DR neXtProt; NX_P19224; -. DR OpenTargets; ENSG00000167165; -. DR PharmGKB; PA37181; -. DR VEuPathDB; HostDB:ENSG00000167165; -. DR eggNOG; KOG1192; Eukaryota. DR GeneTree; ENSGT00940000163820; -. DR HOGENOM; CLU_012949_2_1_1; -. DR InParanoid; P19224; -. DR OMA; NRYRSFG; -. DR OrthoDB; 382054at2759; -. DR PhylomeDB; P19224; -. DR TreeFam; TF315472; -. DR BRENDA; 2.4.1.17; 2681. DR PathwayCommons; P19224; -. DR Reactome; R-HSA-156588; Glucuronidation. DR Reactome; R-HSA-9749641; Aspirin ADME. DR Reactome; R-HSA-9753281; Paracetamol ADME. DR SABIO-RK; P19224; -. DR SignaLink; P19224; -. DR BioGRID-ORCS; 54578; 18 hits in 1012 CRISPR screens. DR ChiTaRS; UGT1A6; human. DR GeneWiki; UGT1A6; -. DR GenomeRNAi; 54578; -. DR Pharos; P19224; Tbio. DR PRO; PR:P19224; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P19224; Protein. DR Bgee; ENSG00000167165; Expressed in liver and 66 other cell types or tissues. DR ExpressionAtlas; P19224; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0052695; P:cellular glucuronidation; IDA:UniProtKB. DR GO; GO:2001030; P:negative regulation of cellular glucuronidation; ISS:BHF-UCL. DR GO; GO:0045922; P:negative regulation of fatty acid metabolic process; ISS:BHF-UCL. DR GO; GO:1904224; P:negative regulation of glucuronosyltransferase activity; ISS:BHF-UCL. DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB. DR CDD; cd03784; GT1_Gtf-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR002213; UDP_glucos_trans. DR InterPro; IPR035595; UDP_glycos_trans_CS. DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1. DR PANTHER; PTHR48043:SF157; UDP GLUCURONOSYLTRANSFERASE 1 FAMILY POLYPEPTIDE A3 PRECURSOR-RELATED; 1. DR Pfam; PF00201; UDPGT; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00375; UDPGT; 1. DR Genevisible; P19224; HS. PE 1: Evidence at protein level; KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; KW Glycosyltransferase; Membrane; Microsome; Reference proteome; Signal; KW Transferase; Transmembrane; Transmembrane helix. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..532 FT /note="UDP-glucuronosyltransferase 1-6" FT /id="PRO_0000036005" FT TRANSMEM 490..506 FT /note="Helical" FT /evidence="ECO:0000255" FT CARBOHYD 294 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 346 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..267 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045779" FT VAR_SEQ 434..532 FT /note="SYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQY FT HSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH -> RKKQQSGR FT QM (in isoform 3)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_053962" FT VARIANT 7 FT /note="S -> A (in allele UGT1A6*2, allele UGT1A6*3 and FT allele UGT1A6*4; dbSNP:rs6759892)" FT /evidence="ECO:0000269|PubMed:15284531" FT /id="VAR_024685" FT VARIANT 70 FT /note="S -> Y (in dbSNP:rs1042708)" FT /evidence="ECO:0000269|PubMed:1339448" FT /id="VAR_026628" FT VARIANT 181 FT /note="T -> A (in allele UGT1A6*2; dbSNP:rs2070959)" FT /evidence="ECO:0000269|PubMed:15284531, FT ECO:0000269|PubMed:19204906, ECO:0000269|PubMed:9429234, FT ECO:0000269|Ref.4" FT /id="VAR_014784" FT VARIANT 184 FT /note="R -> S (in allele UGT1A6*2 and allele UGT1A6*4; FT dbSNP:rs1105879)" FT /evidence="ECO:0000269|PubMed:15284531, FT ECO:0000269|PubMed:19204906, ECO:0000269|PubMed:9429234, FT ECO:0000269|Ref.4" FT /id="VAR_015559" FT VARIANT 510 FT /note="A -> P (in dbSNP:rs1042709)" FT /evidence="ECO:0000269|PubMed:1339448" FT /id="VAR_026629" FT CONFLICT 231 FT /note="E -> K (in Ref. 1; AAA61251)" FT /evidence="ECO:0000305" FT CONFLICT 247..249 FT /note="YQK -> SE (in Ref. 1; AAA61251)" FT /evidence="ECO:0000305" FT CONFLICT 328 FT /note="I -> N (in Ref. 1; AAA61251)" FT /evidence="ECO:0000305" FT CONFLICT 419 FT /note="S -> F (in Ref. 6; BM924331)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="H -> S (in Ref. 6; BM924331)" FT /evidence="ECO:0000305" FT CONFLICT 468 FT /note="K -> Q (in Ref. 6; BM924331)" FT /evidence="ECO:0000305" FT CONFLICT 476..477 FT /note="AA -> GS (in Ref. 6; BM924331)" FT /evidence="ECO:0000305" FT CONFLICT 514 FT /note="R -> P (in Ref. 1; AAA61251)" FT /evidence="ECO:0000305" SQ SEQUENCE 532 AA; 60751 MW; 4A9EA6A88CBC3136 CRC64; MACLLRSFQR ISAGVFFLAL WGMVVGDKLL VVPQDGSHWL SMKDIVEVLS DRGHEIVVVV PEVNLLLKES KYYTRKIYPV PYDQEELKNR YQSFGNNHFA ERSFLTAPQT EYRNNMIVIG LYFINCQSLL QDRDTLNFFK ESKFDALFTD PALPCGVILA EYLGLPSVYL FRGFPCSLEH TFSRSPDPVS YIPRCYTKFS DHMTFSQRVA NFLVNLLEPY LFYCLFSKYE ELASAVLKRD VDIITLYQKV SVWLLRYDFV LEYPRPVMPN MVFIGGINCK KRKDLSQEFE AYINASGEHG IVVFSLGSMV SEIPEKKAMA IADALGKIPQ TVLWRYTGTR PSNLANNTIL VKWLPQNDLL GHPMTRAFIT HAGSHGVYES ICNGVPMVMM PLFGDQMDNA KRMETKGAGV TLNVLEMTSE DLENALKAVI NDKSYKENIM RLSSLHKDRP VEPLDLAVFW VEFVMRHKGA PHLRPAAHDL TWYQYHSLDV IGFLLAVVLT VAFITFKCCA YGYRKCLGKK GRVKKAHKSK TH //