B3GT6_HUMAN
ID B3GT6_HUMAN Reviewed; 329 AA.
AC Q96L58; Q5T7M5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Beta-1,3-galactosyltransferase 6 {ECO:0000305|PubMed:11551958};
DE Short=Beta-1,3-GalTase 6;
DE Short=Beta3Gal-T6;
DE Short=Beta3GalT6 {ECO:0000303|PubMed:23664118};
DE EC=2.4.1.134 {ECO:0000269|PubMed:11551958, ECO:0000269|PubMed:23664117};
DE AltName: Full=GAG GalTII;
DE AltName: Full=Galactosyltransferase II;
DE AltName: Full=Galactosylxylosylprotein 3-beta-galactosyltransferase;
DE AltName: Full=UDP-Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6;
GN Name=B3GALT6;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11551958; DOI=10.1074/jbc.m107339200;
RA Bai X., Zhou D., Brown J.R., Crawford B.E., Hennet T., Esko J.D.;
RT "Biosynthesis of the linkage region of glycosaminoglycans: cloning and
RT activity of galactosyltransferase II, the sixth member of the beta 1,3-
RT galactosyltransferase family (beta 3GalT6).";
RL J. Biol. Chem. 276:48189-48195(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP COFACTOR.
RX PubMed=9892646; DOI=10.1073/pnas.96.2.406;
RA Zhou D., Dinter A., Gutierrez Gallego R., Kamerling J.P.,
RA Vliegenthart J.F.G., Berger E.G., Hennet T.;
RT "A beta-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine
RT synthase activity is structurally related to beta-1,3-
RT galactosyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:406-411(1999).
RN [4]
RP ERRATUM OF PUBMED:9892646.
RA Zhou D., Dinter A., Gutierrez Gallego R., Kamerling J.P.,
RA Vliegenthart J.F.G., Berger E.G., Hennet T.;
RL Proc. Natl. Acad. Sci. U.S.A. 97:11673-11673(2000).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INVOLVEMENT IN SEMDJL1,
RP INVOLVEMENT IN EDSSPD2, VARIANTS SEMDJL1 GLY-65; LEU-67; ASN-156; CYS-232
RP AND SER-300, VARIANTS EDSSPD2 TRP-6; 139-MET--ALA-141 DEL AND THR-309, AND
RP CHARACTERIZATION OF VARIANTS SEMDJL1 GLY-65; LEU-67; ASN-156; CYS-232 AND
RP SER-300.
RX PubMed=23664117; DOI=10.1016/j.ajhg.2013.04.003;
RA Nakajima M., Mizumoto S., Miyake N., Kogawa R., Iida A., Ito H., Kitoh H.,
RA Hirayama A., Mitsubuchi H., Miyazaki O., Kosaki R., Horikawa R., Lai A.,
RA Mendoza-Londono R., Dupuis L., Chitayat D., Howard A., Leal G.F.,
RA Cavalcanti D., Tsurusaki Y., Saitsu H., Watanabe S., Lausch E., Unger S.,
RA Bonafe L., Ohashi H., Superti-Furga A., Matsumoto N., Sugahara K.,
RA Nishimura G., Ikegawa S.;
RT "Mutations in B3GALT6, which encodes a glycosaminoglycan linker region
RT enzyme, cause a spectrum of skeletal and connective tissue disorders.";
RL Am. J. Hum. Genet. 92:927-934(2013).
RN [6]
RP VARIANTS SEMDJL1 HIS-207 AND SER-217.
RX PubMed=23664118; DOI=10.1016/j.ajhg.2013.04.016;
RA Malfait F., Kariminejad A., Van Damme T., Gauche C., Syx D.,
RA Merhi-Soussi F., Gulberti S., Symoens S., Vanhauwaert S., Willaert A.,
RA Bozorgmehr B., Kariminejad M.H., Ebrahimiadib N., Hausser I., Huysseune A.,
RA Fournel-Gigleux S., De Paepe A.;
RT "Defective Initiation of Glycosaminoglycan Synthesis due to B3GALT6
RT Mutations causes a pleiotropic Ehlers-Danlos syndrome-like connective
RT tissue disorder.";
RL Am. J. Hum. Genet. 92:935-945(2013).
RN [7]
RP INVOLVEMENT IN ALGAZ, AND VARIANTS ALGAZ TYR-159 AND ASP-265.
RX PubMed=25149931; DOI=10.1016/j.spen.2014.04.007;
RA Sellars E.A., Bosanko K.A., Lepard T., Garnica A., Schaefer G.B.;
RT "A newborn with complex skeletal abnormalities, joint contractures, and
RT bilateral corneal clouding with sclerocornea.";
RL Semin. Pediatr. Neurol. 21:84-87(2014).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, VARIANT ALGAZ TRP-206,
RP CHARACTERIZATION OF VARIANTS ALGAZ TYR-159; TRP-206 AND ASP-265,
RP CHARACTERIZATION OF VARIANTS SEMDJL1 GLY-65; LEU-67; ALA-79; ASN-156;
RP CYS-232; TRP-256 AND SER-300, AND CHARACTERIZATION OF VARIANTS EDSSPD2
RP TRP-6; LEU-186; HIS-207; SER-217 AND THR-309.
RX PubMed=29443383; DOI=10.1111/cge.13236;
RA Ben-Mahmoud A., Ben-Salem S., Al-Sorkhy M., John A., Ali B.R.,
RA Al-Gazali L.;
RT "A B3GALT6 variant in patient originally described as Al-Gazali syndrome
RT and implicating the endoplasmic reticulum quality control in the mechanism
RT of some beta3GalT6-pathy mutations.";
RL Clin. Genet. 93:1148-1158(2018).
RN [9]
RP VARIANTS SEMDJL1 LEU-67 AND ALA-79.
RX PubMed=24766538; DOI=10.1111/cge.12413;
RA Vorster A.A., Beighton P., Ramesar R.S.;
RT "Spondyloepimetaphyseal dysplasia with joint laxity (Beighton type);
RT mutation analysis in eight affected South African families.";
RL Clin. Genet. 87:492-495(2015).
RN [10]
RP VARIANT SEMDJL1 TRP-256.
RX PubMed=28649518; DOI=10.1016/j.ymgmr.2014.11.005;
RA Ritelli M., Chiarelli N., Zoppi N., Dordoni C., Quinzani S., Traversa M.,
RA Venturini M., Calzavara-Pinton P., Colombi M.;
RT "Insights in the etiopathology of galactosyltransferase II (GalT-II)
RT deficiency from transcriptome-wide expression profiling of skin fibroblasts
RT of two sisters with compound heterozygosity for two novel B3GALT6
RT mutations.";
RL Mol. Genet. Metab. Rep. 2:1-15(2015).
RN [11]
RP VARIANT SEMDJL1 LEU-186.
RX PubMed=27023906; DOI=10.1007/s00439-016-1660-z;
RA Alazami A.M., Al-Qattan S.M., Faqeih E., Alhashem A., Alshammari M.,
RA Alzahrani F., Al-Dosari M.S., Patel N., Alsagheir A., Binabbas B.,
RA Alzaidan H., Alsiddiky A., Alharbi N., Alfadhel M., Kentab A., Daza R.M.,
RA Kircher M., Shendure J., Hashem M., Alshahrani S., Rahbeeni Z., Khalifa O.,
RA Shaheen R., Alkuraya F.S.;
RT "Expanding the clinical and genetic heterogeneity of hereditary disorders
RT of connective tissue.";
RL Hum. Genet. 135:525-540(2016).
RN [12]
RP VARIANT SEMDJL1 LEU-186, AND VARIANT EDSSPD2 LEU-186.
RX PubMed=29620724; DOI=10.1038/gim.2018.50;
RA Maddirevula S., Alsahli S., Alhabeeb L., Patel N., Alzahrani F.,
RA Shamseldin H.E., Anazi S., Ewida N., Alsaif H.S., Mohamed J.Y.,
RA Alazami A.M., Ibrahim N., Abdulwahab F., Hashem M., Abouelhoda M.,
RA Monies D., Al Tassan N., Alshammari M., Alsagheir A., Seidahmed M.Z.,
RA Sogati S., Aglan M.S., Hamad M.H., Salih M.A., Hamed A.A., Alhashmi N.,
RA Nabil A., Alfadli F., Abdel-Salam G.M.H., Alkuraya H., Peitee W.O.,
RA Keng W.T., Qasem A., Mushiba A.M., Zaki M.S., Fassad M.R., Alfadhel M.,
RA Alexander S., Sabr Y., Temtamy S., Ekbote A.V., Ismail S., Hosny G.A.,
RA Otaify G.A., Amr K., Al Tala S., Khan A.O., Rizk T., Alaqeel A.,
RA Alsiddiky A., Singh A., Kapoor S., Alhashem A., Faqeih E., Shaheen R.,
RA Alkuraya F.S.;
RT "Expanding the phenome and variome of skeletal dysplasia.";
RL Genet. Med. 20:1609-1616(2018).
RN [13]
RP VARIANT EDSSPD2 CYS-182.
RX PubMed=29931299; DOI=10.1093/hmg/ddy234;
RA Van Damme T., Pang X., Guillemyn B., Gulberti S., Syx D., De Rycke R.,
RA Kaye O., de Die-Smulders C.E.M., Pfundt R., Kariminejad A., Nampoothiri S.,
RA Pierquin G., Bulk S., Larson A.A., Chatfield K.C., Simon M., Legrand A.,
RA Gerard M., Symoens S., Fournel-Gigleux S., Malfait F.;
RT "Biallelic B3GALT6 mutations cause spondylodysplastic Ehlers-Danlos
RT syndrome.";
RL Hum. Mol. Genet. 27:3475-3487(2018).
CC -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from
CC UDP-galactose to substrates with a terminal beta-linked galactose
CC residue. Has a preference for galactose-beta-1,4-xylose that is found
CC in the linker region of glycosaminoglycans, such as heparan sulfate and
CC chondroitin sulfate. Has no activity towards substrates with terminal
CC glucosamine or galactosamine residues. {ECO:0000269|PubMed:11551958,
CC ECO:0000269|PubMed:23664117, ECO:0000269|PubMed:29443383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-
CC [protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:11780, Rhea:RHEA-COMP:12570, Rhea:RHEA-
CC COMP:12571, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:132088, ChEBI:CHEBI:132090; EC=2.4.1.134;
CC Evidence={ECO:0000269|PubMed:11551958, ECO:0000269|PubMed:23664117};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11781;
CC Evidence={ECO:0000269|PubMed:11551958};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9892646};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000269|PubMed:11551958}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000269|PubMed:11551958}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:11551958, ECO:0000269|PubMed:29443383}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:11551958}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11551958}.
CC -!- DISEASE: Ehlers-Danlos syndrome, spondylodysplastic type, 2 (EDSSPD2)
CC [MIM:615349]: A form of Ehlers-Danlos syndrome, a group of connective
CC tissue disorders characterized by skin hyperextensibility, articular
CC hypermobility, and tissue fragility. EDSSPD2 is an autosomal recessive
CC form characterized by an aged appearance, developmental delay, short
CC stature, craniofacial disproportion, generalized osteopenia, defective
CC wound healing, hypermobile joints, hypotonic muscles, and loose but
CC elastic skin. {ECO:0000269|PubMed:23664117,
CC ECO:0000269|PubMed:24766538, ECO:0000269|PubMed:29443383,
CC ECO:0000269|PubMed:29620724, ECO:0000269|PubMed:29931299}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spondyloepimetaphyseal dysplasia with joint laxity, 1, with or
CC without fractures (SEMDJL1) [MIM:271640]: A bone disease characterized
CC by vertebral abnormalities and ligamentous laxity that result in spinal
CC misalignment and progressive severe kyphoscoliosis, thoracic asymmetry,
CC and respiratory compromise resulting in early death. Additional
CC skeletal features include elbow deformities with radial head
CC dislocation, dislocated hips, clubfeet, and tapered fingers with
CC spatulate distal phalanges. Many affected children have an oval face,
CC flat midface, prominent eyes with blue sclerae, and a long philtrum.
CC Palatal abnormalities and congenital heart disease are also observed.
CC {ECO:0000269|PubMed:23664117, ECO:0000269|PubMed:23664118,
CC ECO:0000269|PubMed:24766538, ECO:0000269|PubMed:27023906,
CC ECO:0000269|PubMed:28649518, ECO:0000269|PubMed:29443383,
CC ECO:0000269|PubMed:29620724}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Al-Gazali syndrome (ALGAZ) [MIM:609465]: A severe disorder
CC characterized by prenatal growth retardation, large joints
CC contractures, camptodactyly, bilateral talipes equinovarus, small
CC mouth, anterior segment anomalies of the eyes, and early lethality. The
CC transmission pattern of the disorder is consistent with autosomal
CC recessive inheritance. {ECO:0000269|PubMed:25149931,
CC ECO:0000269|PubMed:29443383}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:9892646 describes the wrong protein; the cDNAs used had
CC been switched inadvertently. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,3-
CC galactosyltransferase 6;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_433";
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DR EMBL; AY050570; AAL11442.1; -; mRNA.
DR EMBL; AL162741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS13.1; -.
DR RefSeq; NP_542172.2; NM_080605.3.
DR AlphaFoldDB; Q96L58; -.
DR SMR; Q96L58; -.
DR BioGRID; 126016; 28.
DR IntAct; Q96L58; 6.
DR STRING; 9606.ENSP00000368496; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyConnect; 1030; 2 N-Linked glycans (1 site).
DR GlyGen; Q96L58; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q96L58; -.
DR PhosphoSitePlus; Q96L58; -.
DR BioMuta; B3GALT6; -.
DR DMDM; 61211870; -.
DR EPD; Q96L58; -.
DR jPOST; Q96L58; -.
DR MassIVE; Q96L58; -.
DR MaxQB; Q96L58; -.
DR PaxDb; Q96L58; -.
DR PeptideAtlas; Q96L58; -.
DR PRIDE; Q96L58; -.
DR ProteomicsDB; 77152; -.
DR Antibodypedia; 26175; 163 antibodies from 26 providers.
DR DNASU; 126792; -.
DR Ensembl; ENST00000379198.5; ENSP00000368496.2; ENSG00000176022.7.
DR GeneID; 126792; -.
DR KEGG; hsa:126792; -.
DR MANE-Select; ENST00000379198.5; ENSP00000368496.2; NM_080605.4; NP_542172.2.
DR UCSC; uc001adk.4; human.
DR CTD; 126792; -.
DR DisGeNET; 126792; -.
DR GeneCards; B3GALT6; -.
DR HGNC; HGNC:17978; B3GALT6.
DR HPA; ENSG00000176022; Low tissue specificity.
DR MalaCards; B3GALT6; -.
DR MIM; 271640; phenotype.
DR MIM; 609465; phenotype.
DR MIM; 615291; gene.
DR MIM; 615349; phenotype.
DR neXtProt; NX_Q96L58; -.
DR OpenTargets; ENSG00000176022; -.
DR Orphanet; 536467; B3GALT6-related spondylodysplastic Ehlers-Danlos syndrome.
DR Orphanet; 2725; Eye defects-arachnodactyly-cardiopathy syndrome.
DR Orphanet; 93359; Spondyloepimetaphyseal dysplasia with joint laxity.
DR PharmGKB; PA25214; -.
DR VEuPathDB; HostDB:ENSG00000176022; -.
DR eggNOG; KOG2288; Eukaryota.
DR GeneTree; ENSGT00940000162229; -.
DR HOGENOM; CLU_046589_0_0_1; -.
DR InParanoid; Q96L58; -.
DR OMA; VKLVQFT; -.
DR OrthoDB; 640360at2759; -.
DR PhylomeDB; Q96L58; -.
DR TreeFam; TF314311; -.
DR BioCyc; MetaCyc:HS10991-MON; -.
DR BRENDA; 2.4.1.134; 2681.
DR PathwayCommons; Q96L58; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR SignaLink; Q96L58; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR BioGRID-ORCS; 126792; 38 hits in 1069 CRISPR screens.
DR ChiTaRS; B3GALT6; human.
DR GenomeRNAi; 126792; -.
DR Pharos; Q96L58; Tbio.
DR PRO; PR:Q96L58; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96L58; protein.
DR Bgee; ENSG00000176022; Expressed in Brodmann (1909) area 23 and 178 other tissues.
DR Genevisible; Q96L58; HS.
DR GO; GO:0005794; C:Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0047220; F:galactosylxylosylprotein 3-beta-galactosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IEA:Ensembl.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IMP:UniProtKB.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; TAS:Reactome.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Disease variant; Dwarfism; Ehlers-Danlos syndrome; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..329
FT /note="Beta-1,3-galactosyltransferase 6"
FT /id="PRO_0000219168"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..329
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 6
FT /note="R -> W (in EDSSPD2; no effect on Golgi apparatus
FT subcellular localization; dbSNP:rs397514722)"
FT /evidence="ECO:0000269|PubMed:23664117,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_070132"
FT VARIANT 65
FT /note="S -> G (in SEMDJL1; decreased
FT galactosylxylosylprotein 3-beta-galactosyltransferase
FT activity; decreased localization to the Golgi apparatus;
FT dbSNP:rs397514719)"
FT /evidence="ECO:0000269|PubMed:23664117,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_070133"
FT VARIANT 67
FT /note="P -> L (in SEMDJL1; loss of galactosylxylosylprotein
FT 3-beta-galactosyltransferase activity; decreased
FT localization to the Golgi apparatus; dbSNP:rs397514720)"
FT /evidence="ECO:0000269|PubMed:23664117,
FT ECO:0000269|PubMed:24766538, ECO:0000269|PubMed:29443383"
FT /id="VAR_070134"
FT VARIANT 79
FT /note="T -> A (in SEMDJL1; decreased localization to the
FT Golgi apparatus)"
FT /evidence="ECO:0000269|PubMed:24766538,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_084154"
FT VARIANT 139..141
FT /note="Missing (in EDSSPD2)"
FT /evidence="ECO:0000269|PubMed:23664117"
FT /id="VAR_070135"
FT VARIANT 156
FT /note="D -> N (in SEMDJL1; loss of galactosylxylosylprotein
FT 3-beta-galactosyltransferase activity; normal Golgi
FT apparatus subcellular localization; dbSNP:rs397514718)"
FT /evidence="ECO:0000269|PubMed:23664117,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_070136"
FT VARIANT 159
FT /note="S -> Y (in ALGAZ; unknown pathological significance;
FT normal Golgi apparatus subcellular localization)"
FT /evidence="ECO:0000269|PubMed:25149931,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_084155"
FT VARIANT 174
FT /note="E -> D (in dbSNP:rs12085009)"
FT /id="VAR_059317"
FT VARIANT 182
FT /note="Y -> C (in EDSSPD2; unknown pathological
FT significance; dbSNP:rs1314046622)"
FT /evidence="ECO:0000269|PubMed:29931299"
FT /id="VAR_084156"
FT VARIANT 186
FT /note="F -> L (in SEMDJL1; also found in patients with
FT EDSSPD2; decreased localization to the Golgi apparatus;
FT dbSNP:rs1553151294)"
FT /evidence="ECO:0000269|PubMed:27023906,
FT ECO:0000269|PubMed:29443383, ECO:0000269|PubMed:29620724"
FT /id="VAR_084157"
FT VARIANT 206
FT /note="C -> W (in ALGAZ; normal Golgi apparatus subcellular
FT localization; proteoglycans maturation altered;
FT dbSNP:rs763080896)"
FT /evidence="ECO:0000269|PubMed:29443383"
FT /id="VAR_084158"
FT VARIANT 207
FT /note="D -> H (in SEMDJL1; normal Golgi apparatus
FT subcellular localization; dbSNP:rs397514723)"
FT /evidence="ECO:0000269|PubMed:23664118,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_070137"
FT VARIANT 217
FT /note="G -> S (in SEMDJL1; normal Golgi apparatus
FT subcellular localization; dbSNP:rs397514724)"
FT /evidence="ECO:0000269|PubMed:23664118,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_070138"
FT VARIANT 232
FT /note="R -> C (in SEMDJL1; the activity of the enzyme is
FT significantly decreased; decreased localization to the
FT Golgi apparatus; dbSNP:rs397514717)"
FT /evidence="ECO:0000269|PubMed:23664117,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_070139"
FT VARIANT 256
FT /note="R -> W (in SEMDJL1; decreased localization to the
FT Golgi apparatus)"
FT /evidence="ECO:0000269|PubMed:28649518,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_084159"
FT VARIANT 265
FT /note="E -> D (in ALGAZ; unknown pathological significance;
FT normal Golgi apparatus subcellular localization;
FT dbSNP:rs374677519)"
FT /evidence="ECO:0000269|PubMed:25149931,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_084160"
FT VARIANT 300
FT /note="C -> S (in SEMDJL1; loss of galactosylxylosylprotein
FT 3-beta-galactosyltransferase activity; normal Golgi
FT apparatus subcellular localization; dbSNP:rs786200939)"
FT /evidence="ECO:0000269|PubMed:23664117,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_070140"
FT VARIANT 309
FT /note="S -> T (in EDSSPD2; normal Golgi apparatus
FT subcellular localization; dbSNP:rs397514721)"
FT /evidence="ECO:0000269|PubMed:23664117,
FT ECO:0000269|PubMed:29443383"
FT /id="VAR_070141"
FT CONFLICT 2
FT /note="K -> N (in Ref. 1; AAL11442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 37138 MW; F4E2A219B1DC11F7 CRC64;
MKLLRRAWRR RAALGLGTLA LCGAALLYLA RCAAEPGDPR AMSGRSPPPP APARAAAFLA
VLVASAPRAA ERRSVIRSTW LARRGAPGDV WARFAVGTAG LGAEERRALE REQARHGDLL
LLPALRDAYE NLTAKVLAML AWLDEHVAFE FVLKADDDSF ARLDALLAEL RAREPARRRR
LYWGFFSGRG RVKPGGRWRE AAWQLCDYYL PYALGGGYVL SADLVHYLRL SRDYLRAWHS
EDVSLGAWLA PVDVQREHDP RFDTEYRSRG CSNQYLVTHK QSLEDMLEKH ATLAREGRLC
KREVQLRLSY VYDWSAPPSQ CCQRREGIP
