ID CHST6_HUMAN Reviewed; 395 AA. AC Q9GZX3; D3DUK3; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 171. DE RecName: Full=Carbohydrate sulfotransferase 6; DE AltName: Full=Corneal N-acetylglucosamine-6-O-sulfotransferase; DE Short=C-GlcNAc6ST; DE Short=hCGn6ST; DE EC=2.8.2.21 {ECO:0000269|PubMed:11278593, ECO:0000269|PubMed:17690104}; DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4-beta; DE Short=GST4-beta {ECO:0000303|PubMed:11352640}; DE AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 5; DE Short=GlcNAc6ST-5; DE Short=Gn6st-5; GN Name=CHST6 {ECO:0000312|HGNC:HGNC:6938}; 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], TISSUE SPECIFICITY, AND VARIANTS RP MCD CYS-50; ARG-174; GLU-203; TRP-211 AND LYS-274. RX PubMed=11017086; DOI=10.1038/79987; RA Akama T.O., Nishida K., Nakayama J., Watanabe H., Ozaki K., Nakamura T., RA Dota A., Kawasaki S., Inoue Y., Maeda N., Yamamoto S., Fujiwara T., RA Thonar E.J.-M.A., Shimomura Y., Kinoshita S., Tanigami A., Fukuda M.N.; RT "Macular corneal dystrophy type I and type II are caused by distinct RT mutations in a new sulphotransferase gene."; RL Nat. Genet. 26:237-241(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=11181564; DOI=10.1093/glycob/11.1.75; RA Hemmerich S., Lee J.K., Bhakta S., Bistrup A., Ruddle N.R., Rosen S.D.; RT "Chromosomal localization and genomic organization for the galactose/ N- RT acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene family."; RL Glycobiology 11:75-87(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=11352640; DOI=10.1006/bbrc.2001.4668; RA Bartes A., Bhakta S., Hemmerich S.; RT "Sulfation of endothelial mucin by corneal keratan N-acetylglucosamine 6-O- RT sulfotransferase (GST-4beta)."; RL Biochem. Biophys. Res. Commun. 282:928-933(2001). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS MCD CYS-50; RP ARG-174; GLU-203; TRP-211; THR-217 AND LYS-274. RX PubMed=11278593; DOI=10.1074/jbc.m009995200; RA Akama T.O., Nakayama J., Nishida K., Hiraoka N., Suzuki M., McAuliffe J., RA Hindsgaul O., Fukuda M., Fukuda M.N.; RT "Human corneal GlcNAc 6-O-sulfotransferase and mouse intestinal GlcNAc 6-O- RT sulfotransferase both produce keratan sulfate."; RL J. Biol. Chem. 276:16271-16278(2001). RN [7] RP FUNCTION, SUBSTRATE SPECIFICITY, AND VARIANTS MCD CYS-50; ARG-174; GLU-203; RP TRP-211; THR-217 AND LYS-274. RX PubMed=12218059; DOI=10.1074/jbc.m207412200; RA Akama T.O., Misra A.K., Hindsgaul O., Fukuda M.N.; RT "Enzymatic synthesis in vitro of the disulfated disaccharide unit of RT corneal keratan sulfate."; RL J. Biol. Chem. 277:42505-42513(2002). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17690104; DOI=10.1074/jbc.m703695200; RA Kitayama K., Hayashida Y., Nishida K., Akama T.O.; RT "Enzymes responsible for synthesis of corneal keratan sulfate RT glycosaminoglycans."; RL J. Biol. Chem. 282:30085-30096(2007). RN [9] RP VARIANTS MCD VAL-128 AND PRO-166. RX PubMed=11139648; RA Liu N.-P., Dew-Knight S., Rayner M., Jonasson F., Akama T.O., Fukuda M.N., RA Bao W., Gilbert J.R., Vance J.M., Klintworth G.K.; RT "Mutations in corneal carbohydrate sulfotransferase 6 gene (CHST6) cause RT macular corneal dystrophy in Iceland."; RL Mol. Vis. 6:261-264(2000). RN [10] RP VARIANTS MCD SER-31; SER-72; SER-107; ARG-200 AND VAL-206. RX PubMed=11818380; RA El-Ashry M.F., El-Aziz M.M., Wilkins S., Cheetham M.E., Wilkie S.E., RA Hardcastle A.J., Halford S., Bayoumi A.Y., Ficker L.A., Tuft S., RA Bhattacharya S.S., Ebenezer N.D.; RT "Identification of novel mutations in the carbohydrate sulfotransferase RT gene (CHST6) causing macular corneal dystrophy."; RL Invest. Ophthalmol. Vis. Sci. 43:377-382(2002). RN [11] RP VARIANTS MCD PRO-15; THR-61; HIS-68; LEU-70; GLY-102; PRO-131; PRO-152; RP PRO-166; ARG-200 AND GLN-204. RX PubMed=12824236; DOI=10.1167/iovs.02-0740; RA Niel F., Ellies P., Dighiero P., Soria J., Sabbagh C., San C., Renard G., RA Delpech M., Valleix S.; RT "Truncating mutations in the carbohydrate sulfotransferase 6 gene (CHST6) RT result in macular corneal dystrophy."; RL Invest. Ophthalmol. Vis. Sci. 44:2949-2953(2003). RN [12] RP VARIANTS MCD HIS-177; GLN-204; LEU-205; TRP-211 AND THR-217. RX PubMed=12882769; DOI=10.1167/iovs.02-0910; RA Iida-Hasegawa N., Furuhata A., Hayatsu H., Murakami A., Fujiki K., RA Nakayasu K., Kanai A.; RT "Mutations in the CHST6 gene in patients with macular corneal dystrophy: RT immunohistochemical evidence of heterogeneity."; RL Invest. Ophthalmol. Vis. Sci. 44:3272-3277(2003). RN [13] RP VARIANT MCD GLN-211. RX PubMed=12883341; DOI=10.1097/00003226-200308000-00004; RA Ha N.T., Chau H.M., Cung le X., Thanh T.K., Fujiki K., Murakami A., RA Hiratsuka Y., Hasegawa N., Kanai A.; RT "Identification of novel mutations of the CHST6 gene in Vietnamese families RT affected with macular corneal dystrophy in two generations."; RL Cornea 22:508-511(2003). RN [14] RP VARIANTS MCD LEU-51; PRO-59; LEU-66; MET-76; GLN-211; GLN-211; CYS-268 AND RP CYS-268. RX PubMed=12882775; DOI=10.1167/iovs.03-0031; RA Ha N.T., Chau H.M., Cung le X., Thanh T.K., Fujiki K., Murakami A., RA Hiratsuka Y., Kanai A.; RT "Mutation analysis of the carbohydrate sulfotransferase gene in Vietnamese RT with macular corneal dystrophy."; RL Invest. Ophthalmol. Vis. Sci. 44:3310-3316(2003). RN [15] RP VARIANTS MCD ARG-22; TYR-42; LEU-53; HIS-93; PRO-97; TYR-102; CYS-127; RP GLN-205; THR-206; PRO-249 AND LYS-274. RX PubMed=14609920; DOI=10.1001/archopht.121.11.1608; RA Warren J.F., Aldave A.J., Srinivasan M., Thonar E.J., Kumar A.B., RA Cevallos V., Whitcher J.P., Margolis T.P.; RT "Novel mutations in the CHST6 gene associated with macular corneal RT dystrophy in southern India."; RL Arch. Ophthalmol. 121:1608-1612(2003). RN [16] RP VARIANTS MCD ASP-52; LEU-53; TRP-98; SER-107; LEU-121; SER-202; GLN-204; RP PHE-210; GLU-221 AND TYR-221. RX PubMed=14735064; RA Sultana A., Sridhar M.S., Jagannathan A., Balasubramanian D., RA Kannabiran C., Klintworth G.K.; RT "Novel mutations of the carbohydrate sulfotransferase-6 (CHST6) gene RT causing macular corneal dystrophy in India."; RL Mol. Vis. 9:730-734(2003). RN [17] RP VARIANTS MCD GLY-102; GLY-162; GLU-198 AND ARG-200. RX PubMed=14984470; DOI=10.1111/j.0009-9163.2004.00191.x; RA Abbruzzese C., Kuhn U., Molina F., Rama P., De Luca M.; RT "Novel mutations in the CHST6 gene causing macular corneal dystrophy."; RL Clin. Genet. 65:120-125(2004). RN [18] RP VARIANTS MCD LEU-51; SER-72; GLY-102; VAL-104; CYS-110; PRO-122; ARG-200 RP AND PRO-276. RX PubMed=15013869; DOI=10.1016/j.ajo.2003.09.036; RA Aldave A.J., Yellore V.S., Thonar E.J., Udar N., Warren J.F., Yoon M.K., RA Cohen E.J., Rapuano C.J., Laibson P.R., Margolis T.P., Small K.; RT "Novel mutations in the carbohydrate sulfotransferase gene (CHST6) in RT American patients with macular corneal dystrophy."; RL Am. J. Ophthalmol. 137:465-473(2004). RN [19] RP VARIANTS MCD ARG-200; PRO-276 AND ASP-358. RX PubMed=15652851; DOI=10.1016/j.ajo.2004.07.001; RA El-Ashry M.F., Abd El-Aziz M.M., Shalaby O., Wilkins S., RA Poopalasundaram S., Cheetham M., Tuft S.J., Hardcastle A.J., RA Bhattacharya S.S., Ebenezer N.D.; RT "Novel CHST6 nonsense and missense mutations responsible for macular RT corneal dystrophy."; RL Am. J. Ophthalmol. 139:192-193(2005). RN [20] RP VARIANT MCD HIS-358. RX PubMed=19365571; RA Dang X., Zhu Q., Wang L., Su H., Lin H., Zhou N., Liang T., Wang Z., RA Huang S., Ren Q., Qi Y.; RT "Macular corneal dystrophy in a Chinese family related with novel mutations RT of CHST6."; RL Mol. Vis. 15:700-705(2009). RN [21] RP VARIANTS MCD GLY-177; ARG-186 AND GLN-211. RX PubMed=21242781; DOI=10.1097/ico.0b013e3182012888; RA Patel D.A., Harocopos G.J., Chang S.H., Vora S.C., Lubniewski A.J., RA Huang A.J.; RT "Novel CHST6 gene mutations in 2 unrelated cases of macular corneal RT dystrophy."; RL Cornea 30:664-669(2011). RN [22] RP VARIANT MCD TRP-205. RX PubMed=24311932; DOI=10.3341/kjo.2013.27.6.454; RA Lee Y.K., Chang D.J., Chung S.K.; RT "A case of Korean patient with macular corneal dystrophy associated with RT novel mutation in the CHST6 gene."; RL Korean J. Ophthalmol. 27:454-458(2013). RN [23] RP VARIANTS MCD PHE-118; ARG-174; ARG-186; TRP-205; LYS-274; TYR-308 AND RP HIS-358. RX PubMed=26604660; RA Park S.H., Ahn Y.J., Chae H., Kim Y., Kim M.S., Kim M.; RT "Molecular analysis of the CHST6 gene in Korean patients with macular RT corneal dystrophy: Identification of three novel mutations."; RL Mol. Vis. 21:1201-1209(2015). CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate CC (PAPS) as sulfonate donor to catalyze the transfer of sulfate to CC position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of CC keratan (PubMed:11352640, PubMed:11278593, PubMed:12218059, CC PubMed:17690104). Cooperates with B4GALT4 galactosyltransferase and CC B3GNT7 N-acetylglucosaminyltransferase to construct and elongate the CC sulfated disaccharide unit [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] CC within keratan sulfate polymer. Involved in biosynthesis of keratan CC sulfate in cornea, with an impact on proteoglycan fibril organization CC and corneal transparency (PubMed:17690104, PubMed:11278593, CC PubMed:12218059). Involved in sulfation of endothelial mucins such as CC GLYCAM1 (PubMed:11352640). {ECO:0000269|PubMed:11278593, CC ECO:0000269|PubMed:11352640, ECO:0000269|PubMed:12218059, CC ECO:0000269|PubMed:17690104}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'- CC bisphosphate + keratan 6'-sulfate.; EC=2.8.2.21; CC Evidence={ECO:0000269|PubMed:11278593, ECO:0000269|PubMed:17690104}; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single- CC pass type II membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in cornea. Mainly expressed in brain. CC Also expressed in spinal cord and trachea. CC {ECO:0000269|PubMed:11017086, ECO:0000269|PubMed:11181564, CC ECO:0000269|PubMed:11352640}. CC -!- DISEASE: Macular dystrophy, corneal (MCD) [MIM:217800]: An ocular CC disease characterized by bilateral, progressive corneal opacification, CC and reduced corneal sensitivity. Onset occurs in the first decade, CC usually between ages 5 and 9. Painful attacks with photophobia, foreign CC body sensations, and recurrent erosions occur in most patients. The CC disease is due to deposition of an unsulfated keratan sulfate both CC within the intracellular space (within the keratocytes and endothelial CC cells) and in the extracellular corneal stroma. Macular corneal CC dystrophy is divided into the clinically indistinguishable types I, IA, CC and II based on analysis of the normally sulfated, or antigenic, CC keratan sulfate levels in serum and immunohistochemical evaluation of CC the cornea. Patients with types I and IA macular corneal dystrophy have CC undetectable serum levels of antigenic keratan sulfate, whereas those CC with type II macular corneal dystrophy have normal or low levels, CC depending on the population examined. {ECO:0000269|PubMed:11017086, CC ECO:0000269|PubMed:11139648, ECO:0000269|PubMed:11278593, CC ECO:0000269|PubMed:11818380, ECO:0000269|PubMed:12218059, CC ECO:0000269|PubMed:12824236, ECO:0000269|PubMed:12882769, CC ECO:0000269|PubMed:12882775, ECO:0000269|PubMed:12883341, CC ECO:0000269|PubMed:14609920, ECO:0000269|PubMed:14735064, CC ECO:0000269|PubMed:14984470, ECO:0000269|PubMed:15013869, CC ECO:0000269|PubMed:15652851, ECO:0000269|PubMed:19365571, CC ECO:0000269|PubMed:21242781, ECO:0000269|PubMed:24311932, CC ECO:0000269|PubMed:26604660}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CHST6 homozygous missense CC mutations have been observed in patients with macular corneal dystrophy CC type I, while type II patients show a large deletion and replacement in CC the upstream region of CHST6. The only missense mutation for type II is CC Cys-50, which is heterozygous with a replacement in the upstream region CC on the other allele of CHST6. CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF219990; AAG26325.1; -; mRNA. DR EMBL; AF219991; AAG26327.1; -; Genomic_DNA. DR EMBL; AF280086; AAG48244.1; -; mRNA. DR EMBL; CH471114; EAW95640.1; -; Genomic_DNA. DR EMBL; CH471114; EAW95641.1; -; Genomic_DNA. DR EMBL; BC074883; AAH74883.1; -; mRNA. DR EMBL; BC074834; AAH74834.1; -; mRNA. DR CCDS; CCDS10918.1; -. DR RefSeq; NP_067628.1; NM_021615.4. DR RefSeq; XP_005256012.1; XM_005255955.4. DR RefSeq; XP_011521387.1; XM_011523085.2. DR AlphaFoldDB; Q9GZX3; -. DR BioGRID; 110334; 65. DR IntAct; Q9GZX3; 13. DR STRING; 9606.ENSP00000328983; -. DR GlyCosmos; Q9GZX3; 4 sites, No reported glycans. DR GlyGen; Q9GZX3; 4 sites. DR iPTMnet; Q9GZX3; -. DR PhosphoSitePlus; Q9GZX3; -. DR BioMuta; CHST6; -. DR EPD; Q9GZX3; -. DR jPOST; Q9GZX3; -. DR MassIVE; Q9GZX3; -. DR PaxDb; 9606-ENSP00000328983; -. DR PeptideAtlas; Q9GZX3; -. DR ProteomicsDB; 80165; -. DR Antibodypedia; 30313; 240 antibodies from 24 providers. DR DNASU; 4166; -. DR Ensembl; ENST00000332272.9; ENSP00000328983.4; ENSG00000183196.10. DR Ensembl; ENST00000390664.3; ENSP00000375079.2; ENSG00000183196.10. DR Ensembl; ENST00000649341.1; ENSP00000497635.1; ENSG00000183196.10. DR Ensembl; ENST00000649824.1; ENSP00000496806.1; ENSG00000183196.10. DR GeneID; 4166; -. DR KEGG; hsa:4166; -. DR MANE-Select; ENST00000332272.9; ENSP00000328983.4; NM_021615.5; NP_067628.1. DR UCSC; uc002fef.4; human. DR AGR; HGNC:6938; -. DR CTD; 4166; -. DR DisGeNET; 4166; -. DR GeneCards; CHST6; -. DR HGNC; HGNC:6938; CHST6. DR HPA; ENSG00000183196; Tissue enhanced (adrenal gland, brain, cervix). DR MalaCards; CHST6; -. DR MIM; 217800; phenotype. DR MIM; 605294; gene. DR neXtProt; NX_Q9GZX3; -. DR OpenTargets; ENSG00000183196; -. DR Orphanet; 98969; Macular corneal dystrophy. DR PharmGKB; PA26506; -. DR VEuPathDB; HostDB:ENSG00000183196; -. DR eggNOG; ENOG502QQMD; Eukaryota. DR GeneTree; ENSGT00940000162788; -. DR HOGENOM; CLU_028381_3_1_1; -. DR InParanoid; Q9GZX3; -. DR OMA; RVMQEIC; -. DR OrthoDB; 3031241at2759; -. DR PhylomeDB; Q9GZX3; -. DR TreeFam; TF342871; -. DR PathwayCommons; Q9GZX3; -. DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis. DR Reactome; R-HSA-3656225; Defective CHST6 causes MCDC1. DR SignaLink; Q9GZX3; -. DR BioGRID-ORCS; 4166; 14 hits in 1151 CRISPR screens. DR ChiTaRS; CHST6; human. DR GeneWiki; CHST6; -. DR GenomeRNAi; 4166; -. DR Pharos; Q9GZX3; Tbio. DR PRO; PR:Q9GZX3; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9GZX3; Protein. DR Bgee; ENSG00000183196; Expressed in bronchial epithelial cell and 118 other cell types or tissues. DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central. DR GO; GO:0045130; F:keratan sulfotransferase activity; IDA:UniProtKB. DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0018146; P:keratan sulfate biosynthetic process; IDA:UniProtKB. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB. DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:UniProtKB. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR016469; Carbohydrate_sulfotransferase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000863; Sulfotransferase_dom. DR PANTHER; PTHR10704; CARBOHYDRATE SULFOTRANSFERASE; 1. DR PANTHER; PTHR10704:SF4; CARBOHYDRATE SULFOTRANSFERASE 6; 1. DR Pfam; PF00685; Sulfotransfer_1; 1. DR PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q9GZX3; HS. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Corneal dystrophy; Disease variant; Glycoprotein; KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..395 FT /note="Carbohydrate sulfotransferase 6" FT /id="PRO_0000085197" FT TOPO_DOM 1..5 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 6..26 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 27..395 FT /note="Lumenal" FT /evidence="ECO:0000255" FT BINDING 49..55 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250" FT BINDING 202..210 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 229 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 305 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 328 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 15 FT /note="L -> P (in MCD)" FT /evidence="ECO:0000269|PubMed:12824236" FT /id="VAR_021417" FT VARIANT 22 FT /note="L -> R (in MCD; dbSNP:rs68043642)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021418" FT VARIANT 31 FT /note="P -> S (in MCD; dbSNP:rs72547549)" FT /evidence="ECO:0000269|PubMed:11818380" FT /id="VAR_021419" FT VARIANT 42 FT /note="H -> Y (in MCD)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021420" FT VARIANT 50 FT /note="R -> C (in MCD; abolishes the ability to sulfate FT keratan; dbSNP:rs28937877)" FT /evidence="ECO:0000269|PubMed:11017086, FT ECO:0000269|PubMed:11278593, ECO:0000269|PubMed:12218059" FT /id="VAR_021421" FT VARIANT 51 FT /note="S -> L (in MCD; dbSNP:rs370335460)" FT /evidence="ECO:0000269|PubMed:12882775, FT ECO:0000269|PubMed:15013869" FT /id="VAR_021422" FT VARIANT 52 FT /note="G -> D (in MCD)" FT /evidence="ECO:0000269|PubMed:14735064" FT /id="VAR_021423" FT VARIANT 53 FT /note="S -> L (in MCD)" FT /evidence="ECO:0000269|PubMed:14609920, FT ECO:0000269|PubMed:14735064" FT /id="VAR_021424" FT VARIANT 59 FT /note="L -> P (in MCD)" FT /evidence="ECO:0000269|PubMed:12882775" FT /id="VAR_021425" FT VARIANT 61 FT /note="N -> T (in MCD; dbSNP:rs72547548)" FT /evidence="ECO:0000269|PubMed:12824236" FT /id="VAR_021426" FT VARIANT 66 FT /note="V -> L (in MCD; dbSNP:rs72547547)" FT /evidence="ECO:0000269|PubMed:12882775" FT /id="VAR_021427" FT VARIANT 68 FT /note="Y -> H (in MCD; dbSNP:rs775742450)" FT /evidence="ECO:0000269|PubMed:12824236" FT /id="VAR_021428" FT VARIANT 70 FT /note="M -> L (in MCD)" FT /evidence="ECO:0000269|PubMed:12824236" FT /id="VAR_021429" FT VARIANT 72 FT /note="P -> S (in MCD; dbSNP:rs377617168)" FT /evidence="ECO:0000269|PubMed:11818380, FT ECO:0000269|PubMed:15013869" FT /id="VAR_021430" FT VARIANT 76 FT /note="V -> M (in MCD)" FT /evidence="ECO:0000269|PubMed:12882775" FT /id="VAR_021431" FT VARIANT 93 FT /note="R -> H (in MCD)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021432" FT VARIANT 97 FT /note="R -> P (in MCD; dbSNP:rs72547546)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021433" FT VARIANT 98 FT /note="S -> W (in MCD)" FT /evidence="ECO:0000269|PubMed:14735064" FT /id="VAR_021434" FT VARIANT 102 FT /note="C -> G (in MCD; dbSNP:rs121917822)" FT /evidence="ECO:0000269|PubMed:12824236, FT ECO:0000269|PubMed:14984470, ECO:0000269|PubMed:15013869" FT /id="VAR_021435" FT VARIANT 102 FT /note="C -> Y (in MCD)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021436" FT VARIANT 104 FT /note="M -> V (in MCD; dbSNP:rs1158093021)" FT /evidence="ECO:0000269|PubMed:15013869" FT /id="VAR_021437" FT VARIANT 107 FT /note="F -> S (in MCD; dbSNP:rs72547545)" FT /evidence="ECO:0000269|PubMed:11818380, FT ECO:0000269|PubMed:14735064" FT /id="VAR_021438" FT VARIANT 110 FT /note="Y -> C (in MCD; dbSNP:rs72547544)" FT /evidence="ECO:0000269|PubMed:15013869" FT /id="VAR_021439" FT VARIANT 118 FT /note="S -> F (in MCD; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26604660" FT /id="VAR_075522" FT VARIANT 121 FT /note="F -> L (in MCD; dbSNP:rs1265310255)" FT /evidence="ECO:0000269|PubMed:14735064" FT /id="VAR_021440" FT VARIANT 122 FT /note="Q -> P (in MCD; dbSNP:rs758105699)" FT /evidence="ECO:0000269|PubMed:15013869" FT /id="VAR_021441" FT VARIANT 127 FT /note="R -> C (in MCD)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021442" FT VARIANT 128 FT /note="A -> V (in MCD; dbSNP:rs72547543)" FT /evidence="ECO:0000269|PubMed:11139648" FT /id="VAR_021443" FT VARIANT 131 FT /note="S -> P (in MCD)" FT /evidence="ECO:0000269|PubMed:12824236" FT /id="VAR_021444" FT VARIANT 152 FT /note="L -> P (in MCD; dbSNP:rs142954809)" FT /evidence="ECO:0000269|PubMed:12824236" FT /id="VAR_021445" FT VARIANT 162 FT /note="R -> G (in MCD; dbSNP:rs117435647)" FT /evidence="ECO:0000269|PubMed:14984470" FT /id="VAR_021446" FT VARIANT 166 FT /note="R -> P (in MCD; dbSNP:rs72547542)" FT /evidence="ECO:0000269|PubMed:11139648, FT ECO:0000269|PubMed:12824236" FT /id="VAR_021447" FT VARIANT 174 FT /note="K -> R (in MCD; abolishes the ability to sulfate FT keratan; dbSNP:rs28937877)" FT /evidence="ECO:0000269|PubMed:11017086, FT ECO:0000269|PubMed:12218059, ECO:0000269|PubMed:26604660" FT /id="VAR_021448" FT VARIANT 177 FT /note="R -> G (in MCD)" FT /evidence="ECO:0000269|PubMed:21242781" FT /id="VAR_075523" FT VARIANT 177 FT /note="R -> H (in MCD)" FT /evidence="ECO:0000269|PubMed:12882769" FT /id="VAR_021449" FT VARIANT 186 FT /note="P -> R (in MCD; dbSNP:rs376162109)" FT /evidence="ECO:0000269|PubMed:21242781, FT ECO:0000269|PubMed:26604660" FT /id="VAR_075524" FT VARIANT 198 FT /note="V -> E (in MCD)" FT /evidence="ECO:0000269|PubMed:14984470" FT /id="VAR_021450" FT VARIANT 200 FT /note="L -> R (in MCD; dbSNP:rs28937879)" FT /evidence="ECO:0000269|PubMed:11818380, FT ECO:0000269|PubMed:12824236, ECO:0000269|PubMed:14984470, FT ECO:0000269|PubMed:15013869, ECO:0000269|PubMed:15652851" FT /id="VAR_021451" FT VARIANT 202 FT /note="R -> S (in MCD)" FT /evidence="ECO:0000269|PubMed:14735064" FT /id="VAR_021452" FT VARIANT 203 FT /note="D -> E (in MCD; abolishes the ability to sulfate FT keratan; dbSNP:rs28937878)" FT /evidence="ECO:0000269|PubMed:11017086, FT ECO:0000269|PubMed:11278593, ECO:0000269|PubMed:12218059" FT /id="VAR_021453" FT VARIANT 204 FT /note="P -> Q (in MCD; dbSNP:rs759870075)" FT /evidence="ECO:0000269|PubMed:12824236, FT ECO:0000269|PubMed:12882769, ECO:0000269|PubMed:14735064" FT /id="VAR_021454" FT VARIANT 205 FT /note="R -> L (in MCD)" FT /evidence="ECO:0000269|PubMed:12882769" FT /id="VAR_021455" FT VARIANT 205 FT /note="R -> Q (in MCD; dbSNP:rs377706989)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021456" FT VARIANT 205 FT /note="R -> W (in MCD; dbSNP:rs750219546)" FT /evidence="ECO:0000269|PubMed:24311932, FT ECO:0000269|PubMed:26604660" FT /id="VAR_075525" FT VARIANT 206 FT /note="A -> T (in MCD; dbSNP:rs374493344)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021457" FT VARIANT 206 FT /note="A -> V (in MCD)" FT /evidence="ECO:0000269|PubMed:11818380" FT /id="VAR_021458" FT VARIANT 210 FT /note="S -> F (in MCD; dbSNP:rs745571211)" FT /evidence="ECO:0000269|PubMed:14735064" FT /id="VAR_021459" FT VARIANT 211 FT /note="R -> Q (in MCD; dbSNP:rs771397083)" FT /evidence="ECO:0000269|PubMed:12882775, FT ECO:0000269|PubMed:12883341, ECO:0000269|PubMed:21242781" FT /id="VAR_021460" FT VARIANT 211 FT /note="R -> W (in MCD; abolishes the ability to sulfate FT keratan; dbSNP:rs202175444)" FT /evidence="ECO:0000269|PubMed:11017086, FT ECO:0000269|PubMed:11278593, ECO:0000269|PubMed:12218059, FT ECO:0000269|PubMed:12882769" FT /id="VAR_021461" FT VARIANT 217 FT /note="A -> T (in MCD; abolishes ability to sulfate FT keratan; dbSNP:rs752785520)" FT /evidence="ECO:0000269|PubMed:11278593, FT ECO:0000269|PubMed:12218059, ECO:0000269|PubMed:12882769" FT /id="VAR_021462" FT VARIANT 221 FT /note="D -> E (in MCD)" FT /evidence="ECO:0000269|PubMed:14735064" FT /id="VAR_021463" FT VARIANT 221 FT /note="D -> Y (in MCD)" FT /evidence="ECO:0000269|PubMed:14735064" FT /id="VAR_021464" FT VARIANT 249 FT /note="H -> P (in MCD; dbSNP:rs72547540)" FT /evidence="ECO:0000269|PubMed:14609920" FT /id="VAR_021465" FT VARIANT 268 FT /note="Y -> C (in MCD; dbSNP:rs72547539)" FT /evidence="ECO:0000269|PubMed:12882775" FT /id="VAR_021466" FT VARIANT 274 FT /note="E -> K (in MCD; abolishes the ability to sulfate FT keratan; dbSNP:rs72547538)" FT /evidence="ECO:0000269|PubMed:11017086, FT ECO:0000269|PubMed:11278593, ECO:0000269|PubMed:12218059, FT ECO:0000269|PubMed:14609920, ECO:0000269|PubMed:26604660" FT /id="VAR_021467" FT VARIANT 276 FT /note="L -> P (in MCD; dbSNP:rs121917824)" FT /evidence="ECO:0000269|PubMed:15013869, FT ECO:0000269|PubMed:15652851" FT /id="VAR_021468" FT VARIANT 308 FT /note="H -> Y (in MCD; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26604660" FT /id="VAR_075526" FT VARIANT 358 FT /note="Y -> D (in MCD)" FT /evidence="ECO:0000269|PubMed:15652851" FT /id="VAR_021469" FT VARIANT 358 FT /note="Y -> H (in MCD; dbSNP:rs1384294258)" FT /evidence="ECO:0000269|PubMed:19365571, FT ECO:0000269|PubMed:26604660" FT /id="VAR_075527" FT VARIANT 369 FT /note="N -> D (in dbSNP:rs35036798)" FT /id="VAR_033735" SQ SEQUENCE 395 AA; 44099 MW; 433CA60248A48F67 CRC64; MWLPRVSSTA VTALLLAQTF LLLFLVSRPG PSSPAGGEAR VHVLVLSSWR SGSSFVGQLF NQHPDVFYLM EPAWHVWTTL SQGSAATLHM AVRDLVRSVF LCDMDVFDAY LPWRRNLSDL FQWAVSRALC SPPACSAFPR GAISSEAVCK PLCARQSFTL AREACRSYSH VVLKEVRFFN LQVLYPLLSD PALNLRIVHL VRDPRAVLRS REQTAKALAR DNGIVLGTNG TWVEADPGLR VVREVCRSHV RIAEAATLKP PPFLRGRYRL VRFEDLAREP LAEIRALYAF TGLSLTPQLE AWIHNITHGS GPGARREAFK TSSRNALNVS QAWRHALPFA KIRRVQELCA GALQLLGYRP VYSEDEQRNL ALDLVLPRGL NGFTWASSTA SHPRN //