UD16_HUMAN
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 03-AUG-2022, entry version 196.
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};
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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; 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 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; P19224; -.
DR PeptideAtlas; P19224; -.
DR PRIDE; P19224; -.
DR ProteomicsDB; 1419; -.
DR ProteomicsDB; 53637; -. [P19224-1]
DR Antibodypedia; 4074; 141 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 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; CHYFEEG; -.
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; 16 hits in 943 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 65 other tissues.
DR ExpressionAtlas; P19224; baseline and differential.
DR Genevisible; P19224; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0001889; P:liver development; IBA:GO_Central.
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 InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
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
