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 27-MAR-2024, entry version 209. 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, axonal, 2V (CMT2V) [MIM:616491]: CC An axonal form of Charcot-Marie-Tooth disease, a disorder of the CC peripheral nervous system, characterized by progressive weakness and CC atrophy, initially of the peroneal muscles and later of the distal CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two CC main groups on the basis of electrophysiologic properties and CC histopathology: primary peripheral demyelinating neuropathies CC (designated CMT1 when they are dominantly inherited) and primary CC peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group CC are characterized by signs of axonal degeneration in the absence of CC obvious myelin alterations, normal or slightly reduced nerve conduction CC velocities, and progressive distal muscle weakness and atrophy. CMT2V CC is an 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}. 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; 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; 122. 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 GlyCosmos; P54802; 7 sites, 38 glycans. DR GlyGen; P54802; 8 sites, 39 N-linked glycans (5 sites), 1 O-linked glycan (1 site). DR iPTMnet; P54802; -. DR PhosphoSitePlus; P54802; -. DR SwissPalm; P54802; -. DR BioMuta; NAGLU; -. DR DMDM; 317373322; -. DR EPD; P54802; -. DR jPOST; P54802; -. DR MassIVE; P54802; -. DR MaxQB; P54802; -. DR PaxDb; 9606-ENSP00000225927; -. DR PeptideAtlas; P54802; -. DR ProteomicsDB; 56721; -. DR Pumba; P54802; -. DR TopDownProteomics; P54802; -. DR Antibodypedia; 29263; 113 antibodies from 21 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 AGR; HGNC:7632; -. 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; YGQPFVW; -. DR OrthoDB; 1112009at2759; -. 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; 103 hits in 1164 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 191 other cell types or tissues. DR ExpressionAtlas; P54802; baseline and differential. 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:0030534; P:adult behavior; IEA:Ensembl. DR GO; GO:0042982; P:amyloid precursor protein metabolic process; IEA:Ensembl. DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl. DR GO; GO:0048143; P:astrocyte activation; IEA:Ensembl. DR GO; GO:0006914; P:autophagy; IEA:Ensembl. DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl. DR GO; GO:0044242; P:cellular lipid catabolic process; IEA:Ensembl. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl. DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl. DR GO; GO:1904390; P:cone retinal bipolar cell differentiation; IEA:Ensembl. DR GO; GO:0007028; P:cytoplasm organization; IEA:Ensembl. DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl. DR GO; GO:0003158; P:endothelium development; IEA:Ensembl. DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl. DR GO; GO:0001573; P:ganglioside metabolic process; IEA:Ensembl. DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl. DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl. DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; TAS:Reactome. DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IEA:Ensembl. DR GO; GO:0030202; P:heparin metabolic process; IEA:Ensembl. DR GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl. DR GO; GO:0060119; P:inner ear receptor cell development; IEA:Ensembl. DR GO; GO:0003220; P:left ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl. DR GO; GO:0060173; P:limb development; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl. DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl. DR GO; GO:0035633; P:maintenance of blood-brain barrier; IEA:Ensembl. DR GO; GO:0014004; P:microglia differentiation; IEA:Ensembl. DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl. DR GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl. DR GO; GO:0003183; P:mitral valve morphogenesis; IEA:Ensembl. DR GO; GO:0061744; P:motor behavior; IEA:Ensembl. DR GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IEA:Ensembl. DR GO; GO:0021675; P:nerve development; IEA:Ensembl. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl. DR GO; GO:0016485; P:protein processing; IEA:Ensembl. DR GO; GO:0097696; P:receptor signaling pathway via STAT; IEA:Ensembl. DR GO; GO:0034285; P:response to disaccharide; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IEA:Ensembl. DR GO; GO:0046548; P:retinal rod cell development; IEA:Ensembl. DR GO; GO:1904389; P:rod bipolar cell differentiation; IEA:Ensembl. DR GO; GO:0097577; P:sequestering of iron ion; IEA:Ensembl. DR GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl. DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl. DR GO; GO:0099022; P:vesicle tethering; IEA:Ensembl. DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 1.20.120.670; N-acetyl-b-d-glucoasminidase; 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; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1. DR PANTHER; PTHR12872:SF1; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1. DR Pfam; PF05089; NAGLU; 1. DR Pfam; PF12972; NAGLU_C; 1. DR Pfam; PF12971; NAGLU_N; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR Genevisible; P54802; HS. 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; results in partially degraded FT polypeptide in a 16-hour chase experiment suggesting that FT L-48 NAGLU affects the processing and stability of the FT gene; some L-48 NAGLU is being correctly sorted to the FT 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; uncertain 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 //