ID HGNAT_HUMAN Reviewed; 663 AA. AC Q68CP4; B4E2V0; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 160. DE RecName: Full=Heparan-alpha-glucosaminide N-acetyltransferase; DE EC=2.3.1.78; DE AltName: Full=Transmembrane protein 76; GN Name=HGSNAT; Synonyms=TMEM76; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-663 (ISOFORMS 1/2). RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP INVOLVEMENT IN MPS3C, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, RP AND TISSUE SPECIFICITY. RX PubMed=16960811; DOI=10.1086/508068; RA Fan X., Zhang H., Zhang S., Bagshaw R.D., Tropak M.B., Callahan J.W., RA Mahuran D.J.; RT "Identification of the gene encoding the enzyme deficient in RT mucopolysaccharidosis IIIC (Sanfilippo disease type C)."; RL Am. J. Hum. Genet. 79:738-744(2006). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Placenta; RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x; RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., RA Elsaesser H.-P., Mann M., Hasilik A.; RT "Integral and associated lysosomal membrane proteins."; RL Traffic 8:1676-1686(2007). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-142. 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 [8] RP FUNCTION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS MPS3C LEU-509 AND RP THR-643, AND CHARACTERIZATION OF VARIANTS PHE-104; PRO-165; GLN-265; RP ARG-290; LYS-301; LEU-311; HIS-372; CYS-431; SER-452; LYS-499; LYS-510; RP GLU-517; PHE-546; GLN-551; CYS-567; LEU-569; VAL-590 AND LEU-599. RX PubMed=19823584; DOI=10.1371/journal.pone.0007434; RA Feldhammer M., Durand S., Pshezhetsky A.V.; RT "Protein misfolding as an underlying molecular defect in RT mucopolysaccharidosis III type C."; RL PLoS ONE 4:E7434-E7434(2009). RN [9] RP FUNCTION, ACTIVE SITE, ALTERNATIVE INITIATION (ISOFORMS 1 AND 2), SUBUNIT, RP CHARACTERIZATION OF VARIANT PHE-104, MUTAGENESIS OF CYS-107; CYS-151; RP CYS-179; LEU-236; ILE-237; HIS-297; CYS-333; CYS-402; CYS-462; HIS-479 AND RP HIS-633, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20650889; DOI=10.1074/jbc.m110.141150; RA Durand S., Feldhammer M., Bonneil E., Thibault P., Pshezhetsky A.V.; RT "Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha- RT glucosaminide N-acetyltransferase provides insights into the mechanism RT underlying its complete deficiency in mucopolysaccharidosis IIIC."; RL J. Biol. Chem. 285:31233-31242(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-245, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP INVOLVEMENT IN RP73, VARIANTS RP73 TRP-152; ALA-161 AND THR-643, AND RP CHARACTERIZATION OF VARIANT RP73 THR-643. RX PubMed=25859010; DOI=10.1093/hmg/ddv118; RA Haer-Wigman L., Newman H., Leibu R., Bax N.M., Baris H.N., Rizel L., RA Banin E., Massarweh A., Roosing S., Lefeber D.J., Zonneveld-Vrieling M.N., RA Isakov O., Shomron N., Sharon D., Den Hollander A.I., Hoyng C.B., RA Cremers F.P., Ben-Yosef T.; RT "Non-syndromic retinitis pigmentosa due to mutations in the RT mucopolysaccharidosis type IIIC gene, heparan-alpha-glucosaminide N- RT acetyltransferase (HGSNAT)."; RL Hum. Mol. Genet. 24:3742-3751(2015). RN [13] RP INVOLVEMENT IN MPS3C. 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). RN [14] RP VARIANTS MPS3C PHE-104; GLN-265; LEU-311; CYS-372; HIS-372; CYS-431; RP SER-452; LYS-499; LYS-510; GLN-551; LEU-569; VAL-590; LEU-599 AND THR-643, RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17033958; DOI=10.1086/508294; RA Hrebicek M., Mrazova L., Seyrantepe V., Durand S., Roslin N.M., Noskova L., RA Hartmannova H., Ivanek R., Cizkova A., Poupetova H., Sikora J., RA Urinovska J., Stranecky V., Zeman J., Lepage P., Roquis D., Verner A., RA Ausseil J., Beesley C.E., Maire I., Poorthuis B.J.H.M., van de Kamp J., RA van Diggelen O.P., Wevers R.A., Hudson T.J., Fujiwara T.M., Majewski J., RA Morgan K., Kmoch S., Pshezhetsky A.V.; RT "Mutations in TMEM76 cause mucopolysaccharidosis IIIC (Sanfilippo C RT syndrome)."; RL Am. J. Hum. Genet. 79:807-819(2006). RN [15] RP VARIANTS MPS3C PRO-165; GLN-265 AND PHE-546. RX PubMed=17397050; DOI=10.1002/humu.9488; RA Fedele A.O., Filocamo M., Di Rocco M., Sersale G., Luebke T., di Natale P., RA Cosma M.P., Ballabio A.; RT "Mutational analysis of the HGSNAT gene in Italian patients with RT mucopolysaccharidosis IIIC (Sanfilippo C syndrome). Mutation in brief #959. RT Online."; RL Hum. Mutat. 28:523-523(2007). RN [16] RP VARIANTS MPS3C PRO-165; GLN-265; ARG-280; LYS-301; CYS-372; LYS-499; RP PHE-546 AND CYS-567. RX PubMed=18024218; DOI=10.1016/j.ymgme.2007.09.011; RA Ruijter G.J.G., Valstar M.J., van de Kamp J.M., van der Helm R.M., RA Durand S., van Diggelen O.P., Wevers R.A., Poorthuis B.J., RA Pshezhetsky A.V., Wijburg F.A.; RT "Clinical and genetic spectrum of Sanfilippo type C (MPS IIIC) disease in RT The Netherlands."; RL Mol. Genet. Metab. 93:104-111(2008). RN [17] RP VARIANTS MPS3C PRO-165; GLN-265; LEU-311; CYS-372; CYS-431; LYS-499; RP LEU-509; GLU-514; GLU-517; PHE-546; GLN-551; LEU-569 AND THR-643, AND RP CHARACTERIZATION OF VARIANTS MPS3C GLN-265; CYS-431; LEU-509; GLN-551 AND RP THR-643. RX PubMed=19479962; DOI=10.1002/humu.20986; RA Feldhammer M., Durand S., Mrazova L., Boucher R.-M., Laframboise R., RA Steinfeld R., Wraith J.E., Michelakakis H., van Diggelen O.P., Hrebicek M., RA Kmoch S., Pshezhetsky A.V.; RT "Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate RT acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene."; RL Hum. Mutat. 30:918-925(2009). RN [18] RP CHARACTERIZATION OF VARIANTS MPS3C PHE-104; PRO-165; GLN-265; ARG-290; RP LEU-311; CYS-372; CYS-431; SER-452; LYS-499; LEU-509; LYS-510; GLU-514; RP GLU-517; PHE-546; GLN-551; CYS-567; LEU-569; VAL-590; LEU-599 AND THR-643. RX PubMed=20583299; DOI=10.1002/humu.21286; RA Fedele A.O., Hopwood J.J.; RT "Functional analysis of the HGSNAT gene in patients with RT mucopolysaccharidosis IIIC (Sanfilippo C Syndrome)."; RL Hum. Mutat. 31:E1574-E1586(2010). RN [19] RP VARIANTS MPS3C VAL-82; PRO-141; VAL-452 AND PRO-473, VARIANT GLN-265, RP CHARACTERIZATION OF VARIANTS MPS3C VAL-82; PRO-141; CYS-372; VAL-452; RP PRO-473 AND PHE-546, AND CHARACTERIZATION OF VARIANT GLN-265. RX PubMed=20825431; DOI=10.1111/j.1399-0004.2010.01525.x; RA Canals I., Elalaoui S.C., Pineda M., Delgadillo V., Szlago M., Jaouad I.C., RA Sefiani A., Chabas A., Coll M.J., Grinberg D., Vilageliu L.; RT "Molecular analysis of Sanfilippo syndrome type C in Spain: seven novel RT HGSNAT mutations and characterization of the mutant alleles."; RL Clin. Genet. 80:367-374(2011). CC -!- FUNCTION: Lysosomal acetyltransferase that acetylates the non-reducing CC terminal alpha-glucosamine residue of intralysosomal heparin or heparan CC sulfate, converting it into a substrate for luminal alpha-N-acetyl CC glucosaminidase. {ECO:0000269|PubMed:16960811, CC ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:19823584, CC ECO:0000269|PubMed:20650889}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucosaminyl-[heparan sulfate](n) + acetyl-CoA = N- CC acetyl-alpha-D-glucosaminyl-[heparan sulfate](n) + CoA + H(+); CC Xref=Rhea:RHEA:15125, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:11585, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:58388, ChEBI:CHEBI:70974; EC=2.3.1.78; CC Evidence={ECO:0000269|PubMed:16960811}; CC -!- SUBUNIT: Homooligomer. Homooligomerization is necessary for enzyme CC activity. {ECO:0000269|PubMed:20650889}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16960811, CC ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17897319}; Multi-pass CC membrane protein {ECO:0000269|PubMed:16960811, CC ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17897319}. CC Note=Colocalizes with the lysosomal marker LAMP2. The signal peptide is CC not cleaved upon translocation into the endoplasmic reticulum; the CC precursor is probably targeted to the lysosomes via the adapter protein CC complex-mediated pathway that involves tyrosine- and/or dileucine-based CC conserved amino acid motifs in the last C-terminus 16-amino acid CC domain. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Comment=Isoform 1 and isoform 2 are correctly targeted to the CC lysosomal compartment and are functional enzymes.; CC Name=1; CC IsoId=Q68CP4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q68CP4-2; Sequence=VSP_040504; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest level in leukocytes, CC heart, liver, skeletal muscle, lung, placenta and liver. CC {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958}. CC -!- PTM: Undergoes intralysosomal proteolytic cleavage; occurs within the CC end of the first and/or the beginning of the second luminal domain and CC is essential for the activation of the enzyme. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:19823584}. CC -!- DISEASE: Mucopolysaccharidosis 3C (MPS3C) [MIM:252930]: 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:16960811, CC ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17397050, CC ECO:0000269|PubMed:18024218, ECO:0000269|PubMed:19479962, CC ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299, CC ECO:0000269|PubMed:20825431, ECO:0000269|PubMed:28101780}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Retinitis pigmentosa 73 (RP73) [MIM:616544]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. {ECO:0000269|PubMed:25859010}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- MISCELLANEOUS: A signal sequence is predicted but has been shown not to CC be cleaved in the endoplasmic reticulum. CC -!- MISCELLANEOUS: [Isoform 1]: Intralysosomal proteolytic cleavage is CC faster and enzymatic activity higher than isoform 2. 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; AK304441; BAG65262.1; -; mRNA. DR EMBL; AC113191; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR749838; CAH18694.1; -; mRNA. DR CCDS; CCDS47852.1; -. [Q68CP4-2] DR RefSeq; NP_689632.2; NM_152419.3. [Q68CP4-2] DR PDB; 8JKV; EM; 2.87 A; A/B=1-663. DR PDB; 8JL1; EM; 2.80 A; A/B=1-663. DR PDB; 8JL3; EM; 2.59 A; A/B=1-663. DR PDB; 8JL4; EM; 2.68 A; A/B=1-663. DR PDB; 8TU9; EM; 3.26 A; A/B=29-663. DR PDB; 8VKJ; EM; 2.92 A; A/B=1-663. DR PDB; 8VLG; EM; 3.15 A; A/B=1-663. DR PDB; 8VLI; EM; 3.20 A; A/B=1-663. DR PDB; 8VLU; EM; 3.12 A; A/B=1-663. DR PDB; 8VLV; EM; 3.49 A; A/B=1-663. DR PDB; 8VLY; EM; 3.61 A; A/B=1-663. DR PDB; 8W4A; EM; 2.69 A; A/B=1-663. DR AlphaFoldDB; Q68CP4; -. DR EMDB; EMD-36376; -. DR EMDB; EMD-36386; -. DR EMDB; EMD-36387; -. DR EMDB; EMD-36388; -. DR EMDB; EMD-37264; -. DR EMDB; EMD-41620; -. DR EMDB; EMD-43319; -. DR EMDB; EMD-43338; -. DR EMDB; EMD-43339; -. DR EMDB; EMD-43344; -. DR EMDB; EMD-43345; -. DR EMDB; EMD-43348; -. DR SMR; Q68CP4; -. DR BioGRID; 126499; 12. DR FunCoup; Q68CP4; 677. DR IntAct; Q68CP4; 10. DR MINT; Q68CP4; -. DR NDEx; IQUERY-CP-HGSNAT; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000368965; -. DR TCDB; 9.B.169.4.1; the integral membrane protein (8 -10 tmss) yeib or duf418 (yeib) family. DR GlyConnect; Q68CP4; 5 N-Linked glycans (2 sites). DR GlyCosmos; Q68CP4; 4 sites, 5 glycans. DR GlyGen; Q68CP4; 6 sites, 19 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q68CP4; -. DR PhosphoSitePlus; Q68CP4; -. DR SwissPalm; Q68CP4; -. DR BioMuta; HGSNAT; -. DR DMDM; 124007195; -. DR jPOST; Q68CP4; -. DR MassIVE; Q68CP4; -. DR PaxDb; 9606-ENSP00000368965; -. DR PeptideAtlas; Q68CP4; -. DR ProteomicsDB; 66009; -. [Q68CP4-1] DR ProteomicsDB; 66010; -. [Q68CP4-2] DR Pumba; Q68CP4; -. DR Antibodypedia; 24209; 42 antibodies from 15 providers. DR DNASU; 138050; -. DR Ensembl; ENST00000379644.9; ENSP00000368965.4; ENSG00000165102.16. [Q68CP4-2] DR GeneID; 138050; -. DR MANE-Select; ENST00000379644.9; ENSP00000368965.4; NM_152419.3; NP_689632.2. [Q68CP4-2] DR UCSC; uc003xpx.5; human. [Q68CP4-1] DR AGR; HGNC:26527; -. DR ClinPGx; PA162390851; -. DR CTD; 138050; -. DR DisGeNET; 138050; -. DR GeneCards; HGSNAT; -. DR GeneReviews; HGSNAT; -. DR HGNC; HGNC:26527; HGSNAT. DR HPA; ENSG00000165102; Low tissue specificity. DR MalaCards; HGSNAT; -. DR MIM; 252930; phenotype. DR MIM; 610453; gene. DR MIM; 616544; phenotype. DR OpenTargets; ENSG00000165102; -. DR Orphanet; 791; Retinitis pigmentosa. DR Orphanet; 79271; Sanfilippo syndrome type C. DR VEuPathDB; HostDB:ENSG00000165102; -. DR eggNOG; KOG4683; Eukaryota. DR GeneTree; ENSGT00390000001491; -. DR HOGENOM; CLU_029171_3_2_1; -. DR InParanoid; Q68CP4; -. DR OMA; CHQCLYQ; -. DR OrthoDB; 2149840at2759; -. DR PAN-GO; Q68CP4; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q68CP4; -. DR BRENDA; 2.3.1.78; 2681. DR PathwayCommons; Q68CP4; -. DR Reactome; R-HSA-2024096; HS-GAG degradation. DR Reactome; R-HSA-2206291; MPS IIIC - Sanfilippo syndrome C. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SABIO-RK; Q68CP4; -. DR SignaLink; Q68CP4; -. DR Agora; ENSG00000165102; -. DR BioGRID-ORCS; 138050; 12 hits in 1159 CRISPR screens. DR ChiTaRS; HGSNAT; human. DR GeneWiki; HGSNAT; -. DR GenomeRNAi; 138050; -. DR Pharos; Q68CP4; Tbio. DR PRO; PR:Q68CP4; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q68CP4; protein. DR Bgee; ENSG00000165102; Expressed in mucosa of stomach and 200 other cell types or tissues. DR ExpressionAtlas; Q68CP4; baseline and differential. DR GO; GO:0043202; C:lysosomal lumen; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0016746; F:acyltransferase activity; IDA:UniProtKB. DR GO; GO:0015019; F:heparan-alpha-glucosaminide N-acetyltransferase activity; TAS:Reactome. DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IEA:Ensembl. DR GO; GO:0007041; P:lysosomal transport; IDA:UniProtKB. DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB. DR InterPro; IPR012429; HGSNAT_cat. DR PANTHER; PTHR31061:SF37; HEPARAN-ALPHA-GLUCOSAMINIDE N-ACETYLTRANSFERASE; 1. DR PANTHER; PTHR31061; LD22376P; 1. DR Pfam; PF07786; HGSNAT_cat; 1. DR PDBsum; 8JKV; -. DR PDBsum; 8JL1; -. DR PDBsum; 8JL3; -. DR PDBsum; 8JL4; -. DR PDBsum; 8TU9; -. DR PDBsum; 8VKJ; -. DR PDBsum; 8VLG; -. DR PDBsum; 8VLI; -. DR PDBsum; 8VLU; -. DR PDBsum; 8VLV; -. DR PDBsum; 8VLY; -. DR PDBsum; 8W4A; -. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Alternative initiation; Disease variant; KW Disulfide bond; Glycoprotein; Lysosome; Membrane; Mucopolysaccharidosis; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Retinitis pigmentosa; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..663 FT /note="Heparan-alpha-glucosaminide N-acetyltransferase" FT /id="PRO_0000273153" FT TOPO_DOM 1..190 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 191..211 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 212..275 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 276..296 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 297..302 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 303..323 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 324..345 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 346..366 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 367..374 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 375..395 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 396..420 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 421..441 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 442..500 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 501..521 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 522..529 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 530..550 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 551..564 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 565..585 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 586..592 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 593..613 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 614..634 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 635..655 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 656..663 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 624..635 FT /note="Lysosomal targeting region" FT ACT_SITE 297 FT /evidence="ECO:0000269|PubMed:20650889" FT MOD_RES 243 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 245 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 142 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 162 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 151..462 FT /evidence="ECO:0000305" FT VAR_SEQ 1..28 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_040504" FT VARIANT 82 FT /note="A -> V (in MPS3C; shows practically no enzyme FT activity)" FT /evidence="ECO:0000269|PubMed:20825431" FT /id="VAR_075812" FT VARIANT 104 FT /note="C -> F (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum; loss of intralysosomal FT proteolytic cleavage)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299, FT ECO:0000269|PubMed:20650889" FT /id="VAR_063983" FT VARIANT 141 FT /note="L -> P (in MPS3C; shows practically no enzyme FT activity)" FT /evidence="ECO:0000269|PubMed:20825431" FT /id="VAR_075813" FT VARIANT 152 FT /note="R -> W (in RP73)" FT /evidence="ECO:0000269|PubMed:25859010" FT /id="VAR_075814" FT VARIANT 161 FT /note="G -> A (in RP73)" FT /evidence="ECO:0000269|PubMed:25859010" FT /id="VAR_075815" FT VARIANT 165 FT /note="L -> P (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:17397050, FT ECO:0000269|PubMed:18024218, ECO:0000269|PubMed:19479962, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_063984" FT VARIANT 265 FT /note="P -> Q (in MPS3C; likely benign; does not influence FT stability; does not influence activity; does not influence FT cellular localization of the enzyme)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:17397050, ECO:0000269|PubMed:18024218, FT ECO:0000269|PubMed:19479962, ECO:0000269|PubMed:19823584, FT ECO:0000269|PubMed:20583299, ECO:0000269|PubMed:20825431" FT /id="VAR_063985" FT VARIANT 280 FT /note="I -> R (in MPS3C)" FT /evidence="ECO:0000269|PubMed:18024218" FT /id="VAR_063986" FT VARIANT 290 FT /note="G -> R (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:18024218, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_063987" FT VARIANT 301 FT /note="N -> K (in MPS3C; retained in the endoplasmic FT reticulum; loss of enzymatic activity)" FT /evidence="ECO:0000269|PubMed:18024218, FT ECO:0000269|PubMed:19823584" FT /id="VAR_063988" FT VARIANT 311 FT /note="P -> L (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19479962, ECO:0000269|PubMed:19823584, FT ECO:0000269|PubMed:20583299" FT /id="VAR_030083" FT VARIANT 372 FT /note="R -> C (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:18024218, ECO:0000269|PubMed:19479962, FT ECO:0000269|PubMed:20583299" FT /id="VAR_030084" FT VARIANT 372 FT /note="R -> H (in MPS3C; retained in the endoplasmic FT reticulum; loss of enzymatic activity)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19823584" FT /id="VAR_063989" FT VARIANT 431 FT /note="W -> C (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19479962, ECO:0000269|PubMed:19823584, FT ECO:0000269|PubMed:20583299" FT /id="VAR_063990" FT VARIANT 452 FT /note="G -> S (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_030085" FT VARIANT 452 FT /note="G -> V (in MPS3C; shows practically no enzyme FT activity)" FT /evidence="ECO:0000269|PubMed:20825431" FT /id="VAR_075816" FT VARIANT 473 FT /note="L -> P (in MPS3C; shows practically no enzyme FT activity)" FT /evidence="ECO:0000269|PubMed:20825431" FT /id="VAR_075817" FT VARIANT 499 FT /note="E -> K (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:18024218, ECO:0000269|PubMed:19479962, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_030086" FT VARIANT 509 FT /note="V -> L (in MPS3C; likely benign; no loss of FT enzymatic activity)" FT /evidence="ECO:0000269|PubMed:19479962, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_063991" FT VARIANT 510 FT /note="M -> K (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_030087" FT VARIANT 514 FT /note="G -> E (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:19479962, FT ECO:0000269|PubMed:20583299" FT /id="VAR_063992" FT VARIANT 517 FT /note="A -> E (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:19479962, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_063993" FT VARIANT 546 FT /note="S -> F (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:17397050, FT ECO:0000269|PubMed:18024218, ECO:0000269|PubMed:19479962, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299, FT ECO:0000269|PubMed:20825431" FT /id="VAR_063994" FT VARIANT 551 FT /note="K -> Q (in MPS3C; likely benign; no loss of FT enzymatic activity; dbSNP:rs73569592)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19479962, ECO:0000269|PubMed:19823584, FT ECO:0000269|PubMed:20583299" FT /id="VAR_063995" FT VARIANT 567 FT /note="S -> C (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity; retained in FT the endoplasmic reticulum)" FT /evidence="ECO:0000269|PubMed:18024218, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_063996" FT VARIANT 569 FT /note="S -> L (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19479962, ECO:0000269|PubMed:19823584, FT ECO:0000269|PubMed:20583299" FT /id="VAR_030088" FT VARIANT 590 FT /note="D -> V (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_030089" FT VARIANT 599 FT /note="P -> L (in MPS3C; results in a negligible amount of FT protein synthesis; very low enzyme activity)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299" FT /id="VAR_030090" FT VARIANT 643 FT /note="A -> T (in RP73 and MPS3C; uncertain significance; FT may act as a modifier of disease severity in patients with FT retinitis pigmentosa; has a negligible effect on the enzyme FT expression; moderately reduced enzyme activity; FT dbSNP:rs112029032)" FT /evidence="ECO:0000269|PubMed:17033958, FT ECO:0000269|PubMed:19479962, ECO:0000269|PubMed:19823584, FT ECO:0000269|PubMed:20583299, ECO:0000269|PubMed:25859010" FT /id="VAR_063997" FT MUTAGEN 107 FT /note="C->S: Loss of intralysosomal proteolytic cleavage FT and enzymatic activity. Reduced oligomer formation." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 151 FT /note="C->S: Loss of intralysosomal proteolytic cleavage FT and enzymatic activity. Reduced oligomer formation." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 179 FT /note="C->S: Loss of intralysosomal proteolytic cleavage FT and enzymatic activity." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 236 FT /note="L->A: Displayed both lysosomal and plasma membrane FT localization, reduced intralysosomal proteolytic cleavage FT and enzymatic activity; when associated with A-209." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 237 FT /note="I->A: Displayed both lysosomal and plasma membrane FT localization, reduced intralysosomal proteolytic cleavage FT and enzymatic activity; when associated with A-208." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 297 FT /note="H->A: Loss of enzymatic activity, but correctly FT targeted and processed." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 333 FT /note="C->S: No loss of intralysosomal proteolytic cleavage FT and enzymatic activity." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 402 FT /note="C->S: No loss of intralysosomal proteolytic cleavage FT and enzymatic activity." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 462 FT /note="C->S: Complete loss of intralysosomal proteolytic FT cleavage and enzymatic activity. Reduced oligomer FT formation." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 479 FT /note="H->A: Loss of intralysosomal proteolytic cleavage FT and enzymatic activity, retained in the endoplasmic FT reticulum." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 633 FT /note="H->A: Loss of intralysosomal proteolytic cleavage FT and enzymatic activity, retained in the endoplasmic FT reticulum." FT /evidence="ECO:0000269|PubMed:20650889" FT MUTAGEN 652..663 FT /note="Missing: Loss of intralysosomal proteolytic cleavage FT and enzymatic activity. Localized in the plasma membrane." FT STRAND 81..88 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 95..101 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 110..115 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 125..132 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:8JL3" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 149..155 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 162..169 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:8W4A" FT STRAND 177..185 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 192..214 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:8VLV" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:8W4A" FT HELIX 269..286 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 309..330 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 335..352 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 353..357 FT /evidence="ECO:0007829|PDB:8JL3" FT TURN 361..363 FT /evidence="ECO:0007829|PDB:8W4A" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 376..393 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 397..399 FT /evidence="ECO:0007829|PDB:8JL1" FT TURN 401..404 FT /evidence="ECO:0007829|PDB:8VLG" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:8VLG" FT HELIX 412..415 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 418..437 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 438..440 FT /evidence="ECO:0007829|PDB:8JL1" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:8TU9" FT TURN 452..454 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 455..457 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 458..461 FT /evidence="ECO:0007829|PDB:8TU9" FT TURN 463..465 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 466..474 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 477..479 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 487..490 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 498..503 FT /evidence="ECO:0007829|PDB:8TU9" FT HELIX 504..523 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 524..526 FT /evidence="ECO:0007829|PDB:8VLG" FT HELIX 528..550 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 552..555 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 557..559 FT /evidence="ECO:0007829|PDB:8JL3" FT TURN 563..566 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 568..585 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 586..591 FT /evidence="ECO:0007829|PDB:8JL3" FT TURN 598..600 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 601..604 FT /evidence="ECO:0007829|PDB:8JL3" FT HELIX 607..616 FT /evidence="ECO:0007829|PDB:8JL3" FT TURN 617..619 FT /evidence="ECO:0007829|PDB:8JL3" FT TURN 621..623 FT /evidence="ECO:0007829|PDB:8JL3" FT STRAND 628..631 FT /evidence="ECO:0007829|PDB:8VLV" FT HELIX 633..656 FT /evidence="ECO:0007829|PDB:8JL3" SQ SEQUENCE 663 AA; 73293 MW; B05648474A3587B5 CRC64; MTGARASAAE QRRAGRSGQA RAAERAAGMS GAGRALAALL LAASVLSAAL LAPGGSSGRD AQAAPPRDLD KKRHAELKMD QALLLIHNEL LWTNLTVYWK SECCYHCLFQ VLVNVPQSPK AGKPSAAAAS VSTQHGSILQ LNDTLEEKEV CRLEYRFGEF GNYSLLVKNI HNGVSEIACD LAVNEDPVDS NLPVSIAFLI GLAVIIVISF LRLLLSLDDF NNWISKAISS RETDRLINSE LGSPSRTDPL DGDVQPATWR LSALPPRLRS VDTFRGIALI LMVFVNYGGG KYWYFKHASW NGLTVADLVF PWFVFIMGSS IFLSMTSILQ RGCSKFRLLG KIAWRSFLLI CIGIIIVNPN YCLGPLSWDK VRIPGVLQRL GVTYFVVAVL ELLFAKPVPE HCASERSCLS LRDITSSWPQ WLLILVLEGL WLGLTFLLPV PGCPTGYLGP GGIGDFGKYP NCTGGAAGYI DRLLLGDDHL YQHPSSAVLY HTEVAYDPEG ILGTINSIVM AFLGVQAGKI LLYYKARTKD ILIRFTAWCC ILGLISVALT KVSENEGFIP VNKNLWSLSY VTTLSSFAFF ILLVLYPVVD VKGLWTGTPF FYPGMNSILV YVGHEVFENY FPFQWKLKDN QSHKEHLTQN IVATALWVLI AYILYRKKIF WKI //