ANAG_HUMAN
ID ANAG_HUMAN Reviewed; 743 AA.
AC P54802;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Alpha-N-acetylglucosaminidase;
DE EC=3.2.1.50;
DE AltName: Full=N-acetyl-alpha-glucosaminidase;
DE Short=NAG;
DE Contains:
DE RecName: Full=Alpha-N-acetylglucosaminidase 82 kDa form;
DE Contains:
DE RecName: Full=Alpha-N-acetylglucosaminidase 77 kDa form;
DE Flags: Precursor;
GN Name=NAGLU; Synonyms=UFHSD1;
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 / MRNA], AND VARIANT GLY-737.
RC TISSUE=Testis;
RX PubMed=8650226; DOI=10.1073/pnas.93.12.6101;
RA Zhao H.G., Li H.H., Bach G., Schmidtchen A., Neufeld E.F.;
RT "The molecular basis of Sanfilippo syndrome type B.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6101-6105(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, AND
RP VARIANT GLY-737.
RX PubMed=8776591; DOI=10.1093/hmg/5.6.771;
RA Weber B., Blanch L., Clements P.R., Scott H.S., Hopwood J.J.;
RT "Cloning and expression of the gene involved in Sanfilippo B syndrome
RT (mucopolysaccharidosis III B).";
RL Hum. Mol. Genet. 5:771-777(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-737.
RX PubMed=8703123; DOI=10.1007/s003359900206;
RA Zhao Z., Yazdani A., Shen Y., Sun Z.S., Bailey J., Caskey C.T., Lee C.C.;
RT "Molecular dissection of a cosmid from a gene-rich region in 17q21 and
RT characterization of a candidate gene for alpha-N-acetylglucosaminidase with
RT two cDNA isoforms.";
RL Mamm. Genome 7:686-690(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-737.
RC TISSUE=Skin;
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 24-743, AND GLYCOSYLATION AT
RP ASN-261; ASN-272; ASN-435; ASN-503; ASN-526 AND ASN-532.
RA Birrane G., Meiyappan M., Dassier A.;
RT "Crystal structure of N-acetylglucosaminidase.";
RL Submitted (JAN-2015) to the PDB data bank.
RN [8]
RP INVOLVEMENT IN CMT2V, AND VARIANT CMT2V THR-403.
RX PubMed=25818867; DOI=10.1093/brain/awv074;
RA Tetreault M., Gonzalez M., Dicaire M.J., Allard P., Gehring K., Leblanc D.,
RA Leclerc N., Schondorf R., Mathieu J., Zuchner S., Brais B.;
RT "Adult-onset painful axonal polyneuropathy caused by a dominant NAGLU
RT mutation.";
RL Brain 138:1477-1483(2015).
RN [9]
RP VARIANTS MPS3B CYS-140; CYS-455; LEU-521; GLY-612; CYS-674 AND HIS-674.
RX PubMed=9443875; DOI=10.1086/301682;
RA Zhao H.G., Aronovich E.L., Whitley C.B.;
RT "Genotype-phenotype correspondence in Sanfilippo syndrome type B.";
RL Am. J. Hum. Genet. 62:53-63(1998).
RN [10]
RP VARIANTS MPS3B HIS-92; SER-115; CYS-140; LYS-153; LEU-358; VAL-664 AND
RP ARG-682.
RX PubMed=9443878; DOI=10.1086/301685;
RA Schmidtchen A., Greenberg D., Zhao H.G., Li H.H., Huang Y., Tieu P.,
RA Zhao H.-Z., Cheng S., Zhao Z., Whitley C.B., di Natale P., Neufeld E.F.;
RT "NAGLU mutations underlying Sanfilippo syndrome type B.";
RL Am. J. Hum. Genet. 62:64-69(1998).
RN [11]
RP VARIANTS MPS3B CYS-48; CYS-140; CYS-234; ARG-268; LEU-521; TRP-565; PRO-591
RP AND LYS-705.
RX PubMed=9832037; DOI=10.1136/jmg.35.11.910;
RA Beesley C.E., Young E.P., Vellodi A., Winchester B.G.;
RT "Identification of 12 novel mutations in the alpha-N-acetylglucosaminidase
RT gene in 14 patients with Sanfilippo syndrome type B (mucopolysaccharidosis
RT type IIIB).";
RL J. Med. Genet. 35:910-914(1998).
RN [12]
RP VARIANTS MPS3B CYS-79; ARG-100; CYS-140; PHE-142 DEL; LEU-243; PHE-277;
RP PRO-280; ARG-292; LYS-452; TRP-482; ARG-561; GLN-565; HIS-674 AND LYS-705,
RP AND VARIANT GLY-737.
RX PubMed=9950362;
RA Bunge S., Knigge A., Steglich C., Kleijer W.J., van Diggelen O.P., Beck M.,
RA Gal A.;
RT "Mucopolysaccharidosis type IIIB (Sanfilippo B): identification of 18 novel
RT alpha-N-acetylglucosaminidase gene mutations.";
RL J. Med. Genet. 36:28-31(1999).
RN [13]
RP VARIANTS MPS3B LEU-48; SER-69; PRO-227; ARG-248; ARG-292; PHE-334; SER-410;
RP ARG-414; LEU-521; PRO-560; PRO-565; TRP-565; PHE-617; CYS-643; GLU-650;
RP CYS-674 AND PRO-676, AND VARIANT GLY-737.
RX PubMed=10094189; DOI=10.1038/sj.ejhg.5200242;
RA Weber B., Guo X.-H., Kleijer W.J., van de Kamp J.J.P., Poorthuis B.J.H.M.,
RA Hopwood J.J.;
RT "Sanfilippo type B syndrome (mucopolysaccharidosis III B): allelic
RT heterogeneity corresponds to the wide spectrum of clinical phenotypes.";
RL Eur. J. Hum. Genet. 7:34-44(1999).
RN [14]
RP VARIANT MPS3B LEU-48, AND CHARACTERIZATION OF VARIANT MPS3B LEU-48.
RX PubMed=11068184; DOI=10.1016/s0925-4439(00)00066-1;
RA Yogalingam G., Weber B., Meehan J., Rogers J., Hopwood J.J.;
RT "Mucopolysaccharidosis type IIIB: characterisation and expression of wild-
RT type and mutant recombinant alpha-N-acetylglucosaminidase and relationship
RT with sanfilippo phenotype in an attenuated patient.";
RL Biochim. Biophys. Acta 1502:415-425(2000).
RN [15]
RP VARIANTS MPS3B PHE-35; ASP-82; CYS-140; CYS-156; CYS-234; ARG-292; GLY-501;
RP TRP-520; TYR-534 AND CYS-649, AND CHARACTERIZATION OF VARIANTS MPS3B
RP PHE-35; ASP-82; CYS-156; GLY-501; TRP-520; TYR-534 AND CYS-649.
RX PubMed=11153910; DOI=10.1007/s004390000429;
RA Tessitore A., Villani G.R.D., Di Domenico C., Filocamo M., Gatti R.,
RA Di Natale P.;
RT "Molecular defects in the alpha-N-acetylglucosaminidase gene in Italian
RT Sanfilippo type B patients.";
RL Hum. Genet. 107:568-576(2000).
RN [16]
RP VARIANTS MPS3B SER-79; CYS-234; GLY-474; TRP-565 AND PHE-658.
RX PubMed=11286389; DOI=10.1023/a:1005627311402;
RA Coll M.J., Anton C., Chabas A.;
RT "Allelic heterogeneity in Spanish patients with Sanfilippo disease type B.
RT Identification of eight new mutations.";
RL J. Inherit. Metab. Dis. 24:83-84(2001).
RN [17]
RP VARIANTS MPS3B LYS-153; ARG-248; ILE-437 AND ARG-682.
RX PubMed=11793481; DOI=10.1002/humu.9009;
RA Emre S., Terzioglu M., Tokatli A., Coskun T., Ozalp I., Weber B.,
RA Hopwood J.J.;
RT "Sanfilippo syndrome in Turkey: identification of novel mutations in
RT subtypes A and B.";
RL Hum. Mutat. 19:184-185(2002).
RN [18]
RP VARIANTS MPS3B MET-241; LEU-314; TRP-482; PRO-565 AND TRP-565.
RX PubMed=12202988; DOI=10.1007/s100380200070;
RA Tanaka A., Kimura M., Lan H.T.N., Takaura N., Yamano T.;
RT "Molecular analysis of the alpha-N-acetylglucosaminidase gene in seven
RT Japanese patients from six unrelated families with mucopolysaccharidosis
RT IIIB (Sanfilippo type B), including two novel mutations.";
RL J. Hum. Genet. 47:484-487(2002).
RN [19]
RP VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND TRP-565, AND
RP CHARACTERIZATION OF VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND
RP TRP-565.
RX PubMed=11836372; DOI=10.1136/jmg.39.2.e3;
RA Lee-Chen G.J., Lin S.P., Lin S.Z., Chuang C.K., Hsiao K.T., Huang C.F.,
RA Lien W.C.;
RT "Identification and characterisation of mutations underlying Sanfilippo
RT syndrome type B (mucopolysaccharidosis type IIIB).";
RL J. Med. Genet. 39:E3-E3(2002).
RN [20]
RP VARIANTS MPS3B CYS-140; PRO-242; ARG-292; ARG-414; LYS-446; LYS-452;
RP GLN-482 AND LEU-516, AND CHARACTERIZATION OF VARIANTS MPS3B PRO-242;
RP ARG-414; LYS-446; GLN-482 AND LEU-516.
RX PubMed=14984474; DOI=10.1111/j.0009-9163.2004.00210.x;
RA Beesley C., Moraitou M., Winchester B., Schulpis K., Dimitriou E.,
RA Michelakakis H.;
RT "Sanfilippo B syndrome: molecular defects in Greek patients.";
RL Clin. Genet. 65:143-149(2004).
RN [21]
RP VARIANT MPS3B PRO-565.
RX PubMed=15933803; DOI=10.1007/s10038-005-0258-4;
RA Chinen Y., Tohma T., Izumikawa Y., Uehara H., Ohta T.;
RT "Sanfilippo type B syndrome: five patients with an R565P homozygous
RT mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa islands
RT in Japan.";
RL J. Hum. Genet. 50:357-359(2005).
RN [22]
RP VARIANTS MPS3B TRP-38; GLY-77; CYS-79; CYS-130; PRO-246; CYS-309; CYS-335;
RP ARG-414; LYS-452; TRP-482; TRP-520; LEU-521 AND TRP-565, AND
RP CHARACTERIZATION OF VARIANTS MPS3B TRP-38; GLY-77 AND CYS-335.
RX PubMed=16151907; DOI=10.1007/s10545-005-0093-y;
RA Beesley C.E., Jackson M., Young E.P., Vellodi A., Winchester B.G.;
RT "Molecular defects in Sanfilippo syndrome type B (mucopolysaccharidosis
RT IIIB).";
RL J. Inherit. Metab. Dis. 28:759-767(2005).
RN [23]
RP VARIANTS MPS3B 153-GLU--TRP-743 DEL AND PRO-550.
RX PubMed=28101780; DOI=10.1007/s12519-017-0005-x;
RA Ouesleti S., Coutinho M.F., Ribeiro I., Miled A., Mosbahi D.S., Alves S.;
RT "Update of the spectrum of mucopolysaccharidoses type III in Tunisia:
RT identification of three novel mutations and in silico structural analysis
RT of the missense mutations.";
RL World J. Pediatr. 13:374-380(2017).
CC -!- FUNCTION: Involved in the degradation of heparan sulfate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine
CC residues in N-acetyl-alpha-D-glucosaminides.; EC=3.2.1.50;
CC -!- SUBUNIT: Monomer and homodimer.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Liver, ovary, peripheral blood leukocytes, testis,
CC prostate, spleen, colon, lung, placenta and kidney.
CC -!- DISEASE: Mucopolysaccharidosis 3B (MPS3B) [MIM:252920]: A form of
CC mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage
CC disease due to impaired degradation of heparan sulfate. MPS3 is
CC characterized by severe central nervous system degeneration, but only
CC mild somatic disease. Onset of clinical features usually occurs between
CC 2 and 6 years; severe neurologic degeneration occurs in most patients
CC between 6 and 10 years of age, and death occurs typically during the
CC second or third decade of life. {ECO:0000269|PubMed:10094189,
CC ECO:0000269|PubMed:11068184, ECO:0000269|PubMed:11153910,
CC ECO:0000269|PubMed:11286389, ECO:0000269|PubMed:11793481,
CC ECO:0000269|PubMed:11836372, ECO:0000269|PubMed:12202988,
CC ECO:0000269|PubMed:14984474, ECO:0000269|PubMed:15933803,
CC ECO:0000269|PubMed:16151907, ECO:0000269|PubMed:28101780,
CC ECO:0000269|PubMed:9443875, ECO:0000269|PubMed:9443878,
CC ECO:0000269|PubMed:9832037, ECO:0000269|PubMed:9950362}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2V (CMT2V) [MIM:616491]: An axonal
CC form of Charcot-Marie-Tooth disease, a disorder of the peripheral
CC nervous system, characterized by progressive weakness and atrophy,
CC initially of the peroneal muscles and later of the distal muscles of
CC the arms. Charcot-Marie-Tooth disease is classified in two main groups
CC on the basis of electrophysiologic properties and histopathology:
CC primary peripheral demyelinating neuropathies (designated CMT1 when
CC they are dominantly inherited) and primary peripheral axonal
CC neuropathies (CMT2). Neuropathies of the CMT2 group are characterized
CC by signs of axonal degeneration in the absence of obvious myelin
CC alterations, normal or slightly reduced nerve conduction velocities,
CC and progressive distal muscle weakness and atrophy. CMT2V is an
CC autosomal dominant sensory neuropathy with late onset. The main
CC clinical feature is recurrent leg pain that progresses to constant
CC painful paraesthesias in the feet and later the hands. As it evolves,
CC some patients develop a mild sensory ataxia.
CC {ECO:0000269|PubMed:25818867}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 89 family. {ECO:0000305}.
CC -!- CAUTION: A MPS3B mutation at position 100 was erroneously reported
CC (PubMed:9950362) as an amino acid change from Arg to His. The right
CC amino acid change is from His to Arg. {ECO:0000305|PubMed:9950362}.
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DR EMBL; U43572; AAC50512.1; -; Genomic_DNA.
DR EMBL; U43573; AAC50513.1; -; mRNA.
DR EMBL; U40846; AAB06188.1; -; mRNA.
DR EMBL; L78464; AAB36604.1; -; mRNA.
DR EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053991; AAH53991.1; -; mRNA.
DR CCDS; CCDS11427.1; -.
DR PIR; G02270; G02270.
DR RefSeq; NP_000254.2; NM_000263.3.
DR PDB; 4XWH; X-ray; 2.32 A; A=24-743.
DR PDBsum; 4XWH; -.
DR AlphaFoldDB; P54802; -.
DR SMR; P54802; -.
DR BioGRID; 110750; 119.
DR IntAct; P54802; 23.
DR MINT; P54802; -.
DR STRING; 9606.ENSP00000225927; -.
DR DrugBank; DB06773; Human calcitonin.
DR DrugBank; DB00141; N-Acetylglucosamine.
DR CAZy; GH89; Glycoside Hydrolase Family 89.
DR GlyConnect; 803; 36 N-Linked glycans (5 sites).
DR GlyGen; P54802; 7 sites, 38 N-linked glycans (5 sites).
DR iPTMnet; P54802; -.
DR PhosphoSitePlus; P54802; -.
DR BioMuta; NAGLU; -.
DR DMDM; 317373322; -.
DR EPD; P54802; -.
DR jPOST; P54802; -.
DR MassIVE; P54802; -.
DR MaxQB; P54802; -.
DR PaxDb; P54802; -.
DR PeptideAtlas; P54802; -.
DR PRIDE; P54802; -.
DR ProteomicsDB; 56721; -.
DR TopDownProteomics; P54802; -.
DR Antibodypedia; 29263; 98 antibodies from 20 providers.
DR DNASU; 4669; -.
DR Ensembl; ENST00000225927.7; ENSP00000225927.1; ENSG00000108784.10.
DR GeneID; 4669; -.
DR KEGG; hsa:4669; -.
DR MANE-Select; ENST00000225927.7; ENSP00000225927.1; NM_000263.4; NP_000254.2.
DR UCSC; uc002hzv.4; human.
DR CTD; 4669; -.
DR DisGeNET; 4669; -.
DR GeneCards; NAGLU; -.
DR GeneReviews; NAGLU; -.
DR HGNC; HGNC:7632; NAGLU.
DR HPA; ENSG00000108784; Low tissue specificity.
DR MalaCards; NAGLU; -.
DR MIM; 252920; phenotype.
DR MIM; 609701; gene.
DR MIM; 616491; phenotype.
DR neXtProt; NX_P54802; -.
DR OpenTargets; ENSG00000108784; -.
DR Orphanet; 447964; Autosomal dominant Charcot-Marie-Tooth disease type 2V.
DR Orphanet; 79270; Sanfilippo syndrome type B.
DR PharmGKB; PA31437; -.
DR VEuPathDB; HostDB:ENSG00000108784; -.
DR eggNOG; KOG2233; Eukaryota.
DR GeneTree; ENSGT00390000005900; -.
DR HOGENOM; CLU_011988_2_1_1; -.
DR InParanoid; P54802; -.
DR OMA; SNHIFFC; -.
DR OrthoDB; 584128at2759; -.
DR PhylomeDB; P54802; -.
DR TreeFam; TF300689; -.
DR BRENDA; 3.2.1.50; 2681.
DR PathwayCommons; P54802; -.
DR Reactome; R-HSA-2024096; HS-GAG degradation.
DR Reactome; R-HSA-2206282; MPS IIIB - Sanfilippo syndrome B.
DR SignaLink; P54802; -.
DR BioGRID-ORCS; 4669; 101 hits in 1082 CRISPR screens.
DR ChiTaRS; NAGLU; human.
DR GenomeRNAi; 4669; -.
DR Pharos; P54802; Tbio.
DR PRO; PR:P54802; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P54802; protein.
DR Bgee; ENSG00000108784; Expressed in stromal cell of endometrium and 190 other tissues.
DR ExpressionAtlas; P54802; baseline and differential.
DR Genevisible; P54802; HS.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR GO; GO:0004561; F:alpha-N-acetylglucosaminidase activity; TAS:Reactome.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:Reactome.
DR GO; GO:0060119; P:inner ear receptor cell development; IEA:Ensembl.
DR GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0046548; P:retinal rod cell development; IEA:Ensembl.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR007781; NAGLU.
DR InterPro; IPR024732; NAGLU_C.
DR InterPro; IPR024240; NAGLU_N.
DR InterPro; IPR024733; NAGLU_tim-barrel.
DR PANTHER; PTHR12872; PTHR12872; 1.
DR Pfam; PF05089; NAGLU; 1.
DR Pfam; PF12972; NAGLU_C; 1.
DR Pfam; PF12971; NAGLU_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Charcot-Marie-Tooth disease; Direct protein sequencing;
KW Disease variant; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Mucopolysaccharidosis; Neurodegeneration; Neuropathy; Reference proteome;
KW Signal.
FT SIGNAL 1..23
FT CHAIN 24..743
FT /note="Alpha-N-acetylglucosaminidase 82 kDa form"
FT /id="PRO_0000020728"
FT CHAIN 59..743
FT /note="Alpha-N-acetylglucosaminidase 77 kDa form"
FT /id="PRO_0000020729"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:4XWH"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:4XWH"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:4XWH"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:4XWH"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:4XWH"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218, ECO:0000269|Ref.7,
FT ECO:0007744|PDB:4XWH"
FT VARIANT 35
FT /note="L -> F (in MPS3B; no enzyme activity; synthesizes a
FT polypeptide with a molecular size similar to that of the
FT wild-type)"
FT /evidence="ECO:0000269|PubMed:11153910"
FT /id="VAR_054699"
FT VARIANT 38
FT /note="R -> W (in MPS3B; decreases the enzyme activity
FT markedly; dbSNP:rs1460260015)"
FT /evidence="ECO:0000269|PubMed:16151907"
FT /id="VAR_054700"
FT VARIANT 48
FT /note="F -> C (in MPS3B; dbSNP:rs867910252)"
FT /evidence="ECO:0000269|PubMed:9832037"
FT /id="VAR_054701"
FT VARIANT 48
FT /note="F -> L (in MPS3B; associated with a partially
FT degraded polypeptide in a 16-hour chase experiment
FT suggesting that L-48 NAGLU affects the processing and
FT stability of the gene; some L-48 NAGLU is being correctly
FT sorted to the lysosomal compartment; dbSNP:rs104894599)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:11068184"
FT /id="VAR_025489"
FT VARIANT 69
FT /note="G -> S (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_054702"
FT VARIANT 77
FT /note="V -> G (in MPS3B; decreases the enzyme activity
FT markedly; dbSNP:rs1599253805)"
FT /evidence="ECO:0000269|PubMed:16151907"
FT /id="VAR_054703"
FT VARIANT 79
FT /note="G -> C (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:16151907,
FT ECO:0000269|PubMed:9950362"
FT /id="VAR_008979"
FT VARIANT 79
FT /note="G -> S (in MPS3B; dbSNP:rs1276484671)"
FT /evidence="ECO:0000269|PubMed:11286389"
FT /id="VAR_054704"
FT VARIANT 82
FT /note="G -> D (in MPS3B; no enzyme activity; synthesizes a
FT polypeptide with a molecular size similar to that of the
FT wild-type; dbSNP:rs1599253815)"
FT /evidence="ECO:0000269|PubMed:11153910"
FT /id="VAR_054705"
FT VARIANT 92
FT /note="Y -> H (in MPS3B; dbSNP:rs1555621454)"
FT /evidence="ECO:0000269|PubMed:9443878"
FT /id="VAR_005007"
FT VARIANT 100
FT /note="H -> R (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:9950362"
FT /id="VAR_008980"
FT VARIANT 115
FT /note="P -> S (in MPS3B; dbSNP:rs758785463)"
FT /evidence="ECO:0000269|PubMed:9443878"
FT /id="VAR_005008"
FT VARIANT 130
FT /note="R -> C (in MPS3B; does not yield active enzyme)"
FT /evidence="ECO:0000269|PubMed:11836372,
FT ECO:0000269|PubMed:16151907"
FT /id="VAR_054706"
FT VARIANT 140
FT /note="Y -> C (in MPS3B; dbSNP:rs753520553)"
FT /evidence="ECO:0000269|PubMed:11153910,
FT ECO:0000269|PubMed:14984474, ECO:0000269|PubMed:9443875,
FT ECO:0000269|PubMed:9443878, ECO:0000269|PubMed:9832037,
FT ECO:0000269|PubMed:9950362"
FT /id="VAR_005009"
FT VARIANT 142
FT /note="Missing (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:9950362"
FT /id="VAR_008981"
FT VARIANT 153..743
FT /note="Missing (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:28101780"
FT /id="VAR_079424"
FT VARIANT 153
FT /note="E -> K (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:11793481,
FT ECO:0000269|PubMed:9443878"
FT /id="VAR_005010"
FT VARIANT 154
FT /note="I -> R (in MPS3B; does not yield active enzyme;
FT dbSNP:rs770684838)"
FT /evidence="ECO:0000269|PubMed:11836372"
FT /id="VAR_054707"
FT VARIANT 156
FT /note="W -> C (in MPS3B; no enzyme activity; synthesizes a
FT polypeptide with a molecular size similar to that of the
FT wild-type)"
FT /evidence="ECO:0000269|PubMed:11153910"
FT /id="VAR_054708"
FT VARIANT 227
FT /note="H -> P (in MPS3B; dbSNP:rs747155746)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_054709"
FT VARIANT 234
FT /note="R -> C (in MPS3B; dbSNP:rs104894601)"
FT /evidence="ECO:0000269|PubMed:11153910,
FT ECO:0000269|PubMed:11286389, ECO:0000269|PubMed:9832037"
FT /id="VAR_054710"
FT VARIANT 241
FT /note="V -> M (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:12202988"
FT /id="VAR_054711"
FT VARIANT 242
FT /note="L -> P (in MPS3B; no enzyme activity)"
FT /evidence="ECO:0000269|PubMed:14984474"
FT /id="VAR_054712"
FT VARIANT 243
FT /note="P -> L (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:9950362"
FT /id="VAR_008982"
FT VARIANT 246
FT /note="A -> P (in MPS3B; produces 12.7% residual enzyme
FT activity)"
FT /evidence="ECO:0000269|PubMed:16151907"
FT /id="VAR_054713"
FT VARIANT 248
FT /note="H -> R (in MPS3B; dbSNP:rs1465855291)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:11793481"
FT /id="VAR_054714"
FT VARIANT 268
FT /note="W -> R (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:9832037"
FT /id="VAR_054715"
FT VARIANT 277
FT /note="C -> F (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:9950362"
FT /id="VAR_008983"
FT VARIANT 280
FT /note="L -> P (in MPS3B; dbSNP:rs1392732615)"
FT /evidence="ECO:0000269|PubMed:9950362"
FT /id="VAR_008984"
FT VARIANT 292
FT /note="G -> R (in MPS3B; dbSNP:rs1358994052)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:11153910, ECO:0000269|PubMed:14984474,
FT ECO:0000269|PubMed:9950362"
FT /id="VAR_008985"
FT VARIANT 309
FT /note="Y -> C (in MPS3B; does not yield active enzyme;
FT dbSNP:rs1305299665)"
FT /evidence="ECO:0000269|PubMed:11836372,
FT ECO:0000269|PubMed:16151907"
FT /id="VAR_054716"
FT VARIANT 314
FT /note="F -> L (in MPS3B; dbSNP:rs104894600)"
FT /evidence="ECO:0000269|PubMed:12202988"
FT /id="VAR_025490"
FT VARIANT 334
FT /note="V -> F (in MPS3B; dbSNP:rs749140168)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_054717"
FT VARIANT 335
FT /note="Y -> C (in MPS3B; decreases the enzyme activity
FT markedly; dbSNP:rs768918822)"
FT /evidence="ECO:0000269|PubMed:16151907"
FT /id="VAR_054718"
FT VARIANT 358
FT /note="P -> L (in MPS3B; dbSNP:rs368687817)"
FT /evidence="ECO:0000269|PubMed:9443878"
FT /id="VAR_005011"
FT VARIANT 403
FT /note="I -> T (in CMT2V; dbSNP:rs796052122)"
FT /evidence="ECO:0000269|PubMed:25818867"
FT /id="VAR_074607"
FT VARIANT 410
FT /note="F -> S (in MPS3B; dbSNP:rs574688121)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_054719"
FT VARIANT 412
FT /note="G -> E (in MPS3B; does not yield active enzyme)"
FT /evidence="ECO:0000269|PubMed:11836372"
FT /id="VAR_054720"
FT VARIANT 414
FT /note="H -> R (in MPS3B; no enzyme activity;
FT dbSNP:rs768814260)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:14984474, ECO:0000269|PubMed:16151907"
FT /id="VAR_054721"
FT VARIANT 437
FT /note="T -> I (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:11793481"
FT /id="VAR_054722"
FT VARIANT 446
FT /note="E -> K (in MPS3B; no enzyme activity;
FT dbSNP:rs114625063)"
FT /evidence="ECO:0000269|PubMed:14984474"
FT /id="VAR_054723"
FT VARIANT 452
FT /note="E -> K (in MPS3B; dbSNP:rs1183634153)"
FT /evidence="ECO:0000269|PubMed:14984474,
FT ECO:0000269|PubMed:16151907, ECO:0000269|PubMed:9950362"
FT /id="VAR_008986"
FT VARIANT 455
FT /note="Y -> C (in MPS3B; dbSNP:rs375103824)"
FT /evidence="ECO:0000269|PubMed:9443875"
FT /id="VAR_054724"
FT VARIANT 474
FT /note="W -> G (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:11286389"
FT /id="VAR_054725"
FT VARIANT 482
FT /note="R -> Q (in MPS3B; no enzyme activity;
FT dbSNP:rs200909691)"
FT /evidence="ECO:0000269|PubMed:14984474"
FT /id="VAR_054726"
FT VARIANT 482
FT /note="R -> W (in MPS3B; dbSNP:rs104894596)"
FT /evidence="ECO:0000269|PubMed:12202988,
FT ECO:0000269|PubMed:16151907, ECO:0000269|PubMed:9950362"
FT /id="VAR_008987"
FT VARIANT 501
FT /note="V -> G (in MPS3B; no enzyme activity; synthesizes a
FT polypeptide with a molecular size similar to that of the
FT wild-type)"
FT /evidence="ECO:0000269|PubMed:11153910"
FT /id="VAR_054727"
FT VARIANT 516
FT /note="P -> L (in MPS3B; no enzyme activity;
FT dbSNP:rs773054539)"
FT /evidence="ECO:0000269|PubMed:14984474"
FT /id="VAR_054728"
FT VARIANT 520
FT /note="R -> W (in MPS3B; no enzyme activity; synthesizes a
FT polypeptide with a molecular size similar to that of the
FT wild-type; dbSNP:rs992677795)"
FT /evidence="ECO:0000269|PubMed:11153910,
FT ECO:0000269|PubMed:16151907"
FT /id="VAR_054729"
FT VARIANT 521
FT /note="P -> L (in MPS3B; accounts for approximately 6% of
FT mutations in Australasian patients with MPS3B;
FT dbSNP:rs104894595)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:16151907, ECO:0000269|PubMed:9443875,
FT ECO:0000269|PubMed:9832037"
FT /id="VAR_025491"
FT VARIANT 534
FT /note="S -> Y (in MPS3B; no enzyme activity; synthesizes a
FT polypeptide with a molecular size similar to that of the
FT wild-type)"
FT /evidence="ECO:0000269|PubMed:11153910"
FT /id="VAR_054730"
FT VARIANT 550
FT /note="L -> P (in MPS3B; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28101780"
FT /id="VAR_079425"
FT VARIANT 560
FT /note="L -> P (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_054731"
FT VARIANT 561
FT /note="L -> R (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:9950362"
FT /id="VAR_008988"
FT VARIANT 565
FT /note="R -> P (in MPS3B; does not yield active enzyme;
FT dbSNP:rs104894598)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:12202988, ECO:0000269|PubMed:15933803"
FT /id="VAR_025492"
FT VARIANT 565
FT /note="R -> Q (in MPS3B; dbSNP:rs104894598)"
FT /evidence="ECO:0000269|PubMed:9950362"
FT /id="VAR_008989"
FT VARIANT 565
FT /note="R -> W (in MPS3B; accounts for approximately 6% of
FT the mutant alleles in Australasian patients with MPS3B;
FT dbSNP:rs104894597)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:11286389, ECO:0000269|PubMed:11836372,
FT ECO:0000269|PubMed:12202988, ECO:0000269|PubMed:16151907,
FT ECO:0000269|PubMed:9832037"
FT /id="VAR_025493"
FT VARIANT 591
FT /note="L -> P (in MPS3B; dbSNP:rs1215582852)"
FT /evidence="ECO:0000269|PubMed:9832037"
FT /id="VAR_054732"
FT VARIANT 612
FT /note="S -> G (in MPS3B; dbSNP:rs148881970)"
FT /evidence="ECO:0000269|PubMed:9443875"
FT /id="VAR_054733"
FT VARIANT 617
FT /note="L -> F (in MPS3B; dbSNP:rs1555622482)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_054734"
FT VARIANT 643
FT /note="R -> C (in MPS3B; accounts for approximately 20% of
FT MPS3B alleles in a Dutch patient group; dbSNP:rs104894594)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_025494"
FT VARIANT 643
FT /note="R -> H (in MPS3B; dbSNP:rs104894593)"
FT /id="VAR_005012"
FT VARIANT 649
FT /note="W -> C (in MPS3B; no enzyme activity; synthesizes a
FT polypeptide with a molecular size similar to that of the
FT wild-type)"
FT /evidence="ECO:0000269|PubMed:11153910"
FT /id="VAR_054735"
FT VARIANT 650
FT /note="G -> E (in MPS3B; dbSNP:rs527236037)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_054736"
FT VARIANT 658
FT /note="Y -> F (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:11286389"
FT /id="VAR_054737"
FT VARIANT 664
FT /note="A -> V (in MPS3B; dbSNP:rs746006696)"
FT /evidence="ECO:0000269|PubMed:9443878"
FT /id="VAR_005013"
FT VARIANT 674
FT /note="R -> C (in MPS3B; dbSNP:rs763299645)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:9443875"
FT /id="VAR_054738"
FT VARIANT 674
FT /note="R -> H (in MPS3B; dbSNP:rs104894590)"
FT /evidence="ECO:0000269|PubMed:9443875,
FT ECO:0000269|PubMed:9950362"
FT /id="VAR_005014"
FT VARIANT 676
FT /note="R -> P (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:10094189"
FT /id="VAR_054739"
FT VARIANT 682
FT /note="L -> R (in MPS3B)"
FT /evidence="ECO:0000269|PubMed:11793481,
FT ECO:0000269|PubMed:9443878"
FT /id="VAR_005015"
FT VARIANT 705
FT /note="E -> K (in MPS3B; dbSNP:rs1364203992)"
FT /evidence="ECO:0000269|PubMed:9832037,
FT ECO:0000269|PubMed:9950362"
FT /id="VAR_008990"
FT VARIANT 737
FT /note="R -> G (in dbSNP:rs86312)"
FT /evidence="ECO:0000269|PubMed:10094189,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8650226,
FT ECO:0000269|PubMed:8703123, ECO:0000269|PubMed:8776591,
FT ECO:0000269|PubMed:9950362"
FT /id="VAR_008991"
FT CONFLICT 551
FT /note="A -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="S -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 171..182
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 216..235
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4XWH"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 324..339
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:4XWH"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 363..370
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:4XWH"
FT TURN 383..387
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 420..432
FT /evidence="ECO:0007829|PDB:4XWH"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 452..461
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 471..483
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 488..499
FT /evidence="ECO:0007829|PDB:4XWH"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 533..545
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 554..584
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 588..600
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 602..610
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 618..628
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 632..646
FT /evidence="ECO:0007829|PDB:4XWH"
FT TURN 654..659
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 671..687
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 694..710
FT /evidence="ECO:0007829|PDB:4XWH"
FT HELIX 723..740
FT /evidence="ECO:0007829|PDB:4XWH"
SQ SEQUENCE 743 AA; 82266 MW; 6D8D6A42C7BA7CF3 CRC64;
MEAVAVAAAV GVLLLAGAGG AAGDEAREAA AVRALVARLL GPGPAADFSV SVERALAAKP
GLDTYSLGGG GAARVRVRGS TGVAAAAGLH RYLRDFCGCH VAWSGSQLRL PRPLPAVPGE
LTEATPNRYR YYQNVCTQSY SFVWWDWARW EREIDWMALN GINLALAWSG QEAIWQRVYL
ALGLTQAEIN EFFTGPAFLA WGRMGNLHTW DGPLPPSWHI KQLYLQHRVL DQMRSFGMTP
VLPAFAGHVP EAVTRVFPQV NVTKMGSWGH FNCSYSCSFL LAPEDPIFPI IGSLFLRELI
KEFGTDHIYG ADTFNEMQPP SSEPSYLAAA TTAVYEAMTA VDTEAVWLLQ GWLFQHQPQF
WGPAQIRAVL GAVPRGRLLV LDLFAESQPV YTRTASFQGQ PFIWCMLHNF GGNHGLFGAL
EAVNGGPEAA RLFPNSTMVG TGMAPEGISQ NEVVYSLMAE LGWRKDPVPD LAAWVTSFAA
RRYGVSHPDA GAAWRLLLRS VYNCSGEACR GHNRSPLVRR PSLQMNTSIW YNRSDVFEAW
RLLLTSAPSL ATSPAFRYDL LDLTRQAVQE LVSLYYEEAR SAYLSKELAS LLRAGGVLAY
ELLPALDEVL ASDSRFLLGS WLEQARAAAV SEAEADFYEQ NSRYQLTLWG PEGNILDYAN
KQLAGLVANY YTPRWRLFLE ALVDSVAQGI PFQQHQFDKN VFQLEQAFVL SKQRYPSQPR
GDTVDLAKKI FLKYYPRWVA GSW
