CHST6_HUMAN
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 03-AUG-2022, entry version 163.
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 -!- CAUTION: PubMed:12824236 reported a Gly-204 variant, however according
CC to their results reported in figure 1, it is a Gln-204 variant.
CC {ECO:0000305}.
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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; 64.
DR IntAct; Q9GZX3; 13.
DR STRING; 9606.ENSP00000328983; -.
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; Q9GZX3; -.
DR PeptideAtlas; Q9GZX3; -.
DR PRIDE; Q9GZX3; -.
DR ProteomicsDB; 80165; -.
DR Antibodypedia; 30313; 210 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 CTD; 4166; -.
DR DisGeNET; 4166; -.
DR GeneCards; CHST6; -.
DR HGNC; HGNC:6938; CHST6.
DR HPA; ENSG00000183196; Tissue enhanced (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; 1246608at2759; -.
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 1071 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 117 other tissues.
DR Genevisible; Q9GZX3; HS.
DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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; unknown pathological 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; unknown pathological 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
