B3GA3_HUMAN
ID B3GA3_HUMAN Reviewed; 335 AA.
AC O94766; B7ZAB3; Q96I06; Q9UEP0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3;
DE EC=2.4.1.135 {ECO:0000269|PubMed:25893793};
DE AltName: Full=Beta-1,3-glucuronyltransferase 3;
DE AltName: Full=Glucuronosyltransferase I;
DE Short=GlcAT-I;
DE AltName: Full=UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase;
DE Short=GlcUAT-I;
GN Name=B3GAT3;
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] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Placenta;
RX PubMed=9506957; DOI=10.1074/jbc.273.12.6615;
RA Kitagawa H., Tone Y., Tamura J., Neumann K.W., Ogawa T., Oka S.,
RA Kawasaki T., Sugahara K.;
RT "Molecular cloning and expression of glucuronyltransferase I involved in
RT the biosynthesis of the glycosaminoglycan-protein linkage region of
RT proteoglycans.";
RL J. Biol. Chem. 273:6615-6618(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND MUTAGENESIS.
RX PubMed=10842173; DOI=10.1074/jbc.m002182200;
RA Ouzzine M., Gulberti S., Netter P., Magdalou J., Fournel-Gigleux S.;
RT "Structure/function of the human Ga1beta1,3-glucuronosyltransferase.
RT Dimerization and functional activity are mediated by two crucial cysteine
RT residues.";
RL J. Biol. Chem. 275:28254-28260(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-335 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9927678; DOI=10.1073/pnas.96.3.974;
RA Herman T., Horvitz H.R.;
RT "Three proteins involved in Caenorhabditis elegans vulval invagination are
RT similar to components of a glycosylation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:974-979(1999).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10526176; DOI=10.1016/s0014-5793(99)01287-9;
RA Tone Y., Kitagawa H., Imiya K., Oka S., Kawasaki T., Sugahara K.;
RT "Characterization of recombinant human glucuronyltransferase I involved in
RT the biosynthesis of the glycosaminoglycan-protein linkage region of
RT proteoglycans.";
RL FEBS Lett. 459:415-420(1999).
RN [8]
RP SUBCELLULAR LOCATION, VARIANT JDSCD GLN-277, CHARACTERIZATION OF VARIANT
RP JDSCD GLN-277, AND INVOLVEMENT IN JDSCD.
RX PubMed=21763480; DOI=10.1016/j.ajhg.2011.05.021;
RA Baasanjav S., Al-Gazali L., Hashiguchi T., Mizumoto S., Fischer B.,
RA Horn D., Seelow D., Ali B.R., Aziz S.A., Langer R., Saleh A.A., Becker C.,
RA Nurnberg G., Cantagrel V., Gleeson J.G., Gomez D., Michel J.B.,
RA Stricker S., Lindner T.H., Nurnberg P., Sugahara K., Mundlos S.,
RA Hoffmann K.;
RT "Faulty initiation of proteoglycan synthesis causes cardiac and joint
RT defects.";
RL Am. J. Hum. Genet. 89:15-27(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, INTERACTION WITH PXYLP1, AND MUTAGENESIS OF GLU-281.
RX PubMed=24425863; DOI=10.1074/jbc.m113.520536;
RA Koike T., Izumikawa T., Sato B., Kitagawa H.;
RT "Identification of phosphatase that dephosphorylates xylose in the
RT glycosaminoglycan-protein linkage region of proteoglycans.";
RL J. Biol. Chem. 289:6695-6708(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 76-335 IN COMPLEX WITH
RP UDP-GLUCURONIC ACID AND GALACTOSE MOIETY OF SUBSTRATE GLYCOPROTEIN.
RC TISSUE=Liver;
RX PubMed=10946001; DOI=10.1074/jbc.m007399200;
RA Pedersen L.C., Tsuchida K., Kitagawa H., Sugahara K., Darden T.A.,
RA Negishi M.;
RT "Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human
RT glucuronyltransferase I.";
RL J. Biol. Chem. 275:34580-34585(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 76-335 IN COMPLEX WITH
RP UDP-GLUCURONIC ACID, AND ACTIVE SITE.
RX PubMed=11950836; DOI=10.1074/jbc.m112343200;
RA Pedersen L.C., Darden T.A., Negishi M.;
RT "Crystal structure of beta 1,3-glucuronyltransferase I in complex with
RT active donor substrate UDP-GlcUA.";
RL J. Biol. Chem. 277:21869-21873(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 76-335 IN COMPLEX WITH
RP URIDINE-5'-DIPHOSPHATE AND GALACTOSE MOIETY OF SUBSTRATE GLYCOPROTEIN.
RX PubMed=18400750; DOI=10.1074/jbc.m709556200;
RA Tone Y., Pedersen L.C., Yamamoto T., Izumikawa T., Kitagawa H.,
RA Nishihara J., Tamura J., Negishi M., Sugahara K.;
RT "2-o-phosphorylation of xylose and 6-O-sulfation of galactose in the
RT protein linkage region of glycosaminoglycans influence the
RT glucuronyltransferase-I activity involved in the linkage region
RT synthesis.";
RL J. Biol. Chem. 283:16801-16807(2008).
RN [15]
RP VARIANT JDSCD GLN-277.
RX PubMed=24668659; DOI=10.1002/ajmg.a.36487;
RA von Oettingen J.E., Tan W.H., Dauber A.;
RT "Skeletal dysplasia, global developmental delay, and multiple congenital
RT anomalies in a 5-year-old boy-report of the second family with B3GAT3
RT mutation and expansion of the phenotype.";
RL Am. J. Med. Genet. A 164A:1580-1586(2014).
RN [16]
RP VARIANT JDSCD SER-223.
RX PubMed=26086840; DOI=10.1002/ajmg.a.37209;
RA Jones K.L., Schwarze U., Adam M.P., Byers P.H., Mefford H.C.;
RT "A homozygous B3GAT3 mutation causes a severe syndrome with multiple
RT fractures, expanding the phenotype of linkeropathy syndromes.";
RL Am. J. Med. Genet. A 167A:2691-2696(2015).
RN [17]
RP VARIANT JDSCD LEU-140, CHARACTERIZATION OF VARIANT JDSCD LEU-140, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=25893793; DOI=10.1007/s00439-015-1549-2;
RA Budde B.S., Mizumoto S., Kogawa R., Becker C., Altmueller J., Thiele H.,
RA Rueschendorf F., Toliat M.R., Kaleschke G., Haemmerle J.M., Hoehne W.,
RA Sugahara K., Nuernberg P., Kennerknecht I.;
RT "Skeletal dysplasia in a consanguineous clan from the island of
RT Nias/Indonesia is caused by a novel mutation in B3GAT3.";
RL Hum. Genet. 134:691-704(2015).
CC -!- FUNCTION: Glycosaminoglycans biosynthesis (PubMed:25893793). Involved
CC in forming the linkage tetrasaccharide present in heparan sulfate and
CC chondroitin sulfate. Transfers a glucuronic acid moiety from the
CC uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage
CC region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to
CC a Ser residue at the glycosaminylglycan attachment site of
CC proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1
CC carbohydrate epitope on glycoproteins. Shows strict specificity for
CC Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into
CC other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl,
CC Galbeta1-4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose
CC phosphatase activity of PXYLP1 in presence of uridine diphosphate-
CC glucuronic acid (UDP-GlcUA) during completion of linkage region
CC formation (PubMed:24425863). {ECO:0000269|PubMed:24425863,
CC ECO:0000269|PubMed:25893793}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571,
CC Rhea:RHEA-COMP:12573, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132090, ChEBI:CHEBI:132093;
CC EC=2.4.1.135; Evidence={ECO:0000269|PubMed:25893793};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- ACTIVITY REGULATION: Inhibited by EDTA.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PXYLP1; the
CC interaction increases the 2-phosphoxylose phosphatase activity of
CC PXYLP1 during completion of linkage region formation in a B3GAT3-
CC mediated manner. {ECO:0000269|PubMed:10946001,
CC ECO:0000269|PubMed:11950836, ECO:0000269|PubMed:18400750,
CC ECO:0000269|PubMed:24425863}.
CC -!- INTERACTION:
CC O94766; Q9H5K3: POMK; NbExp=2; IntAct=EBI-3917958, EBI-11337900;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21763480}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:21763480}. Golgi apparatus, cis-Golgi network
CC {ECO:0000269|PubMed:21763480, ECO:0000269|PubMed:25893793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94766-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94766-2; Sequence=VSP_056347;
CC -!- TISSUE SPECIFICITY: Ubiquitous (but weakly expressed in all tissues
CC examined).
CC -!- PTM: N-glycosylated.
CC -!- DISEASE: Multiple joint dislocations, short stature, and craniofacial
CC dysmorphism with or without congenital heart defects (JDSCD)
CC [MIM:245600]: An autosomal recessive disease characterized by
CC dysmorphic facies, bilateral dislocations of the elbows, hips, and
CC knees, clubfeet, and short stature, as well as cardiovascular defects.
CC {ECO:0000269|PubMed:21763480, ECO:0000269|PubMed:24668659,
CC ECO:0000269|PubMed:25893793, ECO:0000269|PubMed:26086840}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AB009598; BAA34537.1; -; mRNA.
DR EMBL; AK316228; BAH14599.1; -; mRNA.
DR EMBL; AP001458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007906; AAH07906.1; -; mRNA.
DR EMBL; BC071961; AAH71961.1; -; mRNA.
DR EMBL; AJ005865; CAA06742.1; -; mRNA.
DR CCDS; CCDS76418.1; -. [O94766-2]
DR CCDS; CCDS8025.1; -. [O94766-1]
DR RefSeq; NP_001275652.1; NM_001288723.1. [O94766-2]
DR RefSeq; NP_036332.2; NM_012200.3. [O94766-1]
DR PDB; 1FGG; X-ray; 2.30 A; A/B=76-335.
DR PDB; 1KWS; X-ray; 2.10 A; A/B=76-335.
DR PDB; 3CU0; X-ray; 1.90 A; A/B=76-335.
DR PDBsum; 1FGG; -.
DR PDBsum; 1KWS; -.
DR PDBsum; 3CU0; -.
DR AlphaFoldDB; O94766; -.
DR SMR; O94766; -.
DR BioGRID; 117620; 134.
DR IntAct; O94766; 27.
DR MINT; O94766; -.
DR STRING; 9606.ENSP00000265471; -.
DR DrugBank; DB03041; UDP-alpha-D-glucuronic acid.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyGen; O94766; 1 site.
DR iPTMnet; O94766; -.
DR PhosphoSitePlus; O94766; -.
DR BioMuta; B3GAT3; -.
DR EPD; O94766; -.
DR jPOST; O94766; -.
DR MassIVE; O94766; -.
DR MaxQB; O94766; -.
DR PaxDb; O94766; -.
DR PeptideAtlas; O94766; -.
DR PRIDE; O94766; -.
DR ProteomicsDB; 50431; -. [O94766-1]
DR ProteomicsDB; 7058; -.
DR Antibodypedia; 28557; 134 antibodies from 20 providers.
DR DNASU; 26229; -.
DR Ensembl; ENST00000265471.10; ENSP00000265471.5; ENSG00000149541.10. [O94766-1]
DR Ensembl; ENST00000534026.5; ENSP00000432474.1; ENSG00000149541.10. [O94766-2]
DR GeneID; 26229; -.
DR KEGG; hsa:26229; -.
DR MANE-Select; ENST00000265471.10; ENSP00000265471.5; NM_012200.4; NP_036332.2.
DR UCSC; uc001ntw.3; human. [O94766-1]
DR CTD; 26229; -.
DR DisGeNET; 26229; -.
DR GeneCards; B3GAT3; -.
DR HGNC; HGNC:923; B3GAT3.
DR HPA; ENSG00000149541; Low tissue specificity.
DR MalaCards; B3GAT3; -.
DR MIM; 245600; phenotype.
DR MIM; 606374; gene.
DR neXtProt; NX_O94766; -.
DR OpenTargets; ENSG00000149541; -.
DR Orphanet; 284139; Larsen-like syndrome, B3GAT3 type.
DR PharmGKB; PA25217; -.
DR VEuPathDB; HostDB:ENSG00000149541; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000156954; -.
DR HOGENOM; CLU_045177_0_1_1; -.
DR InParanoid; O94766; -.
DR OMA; LMYALLQ; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; O94766; -.
DR TreeFam; TF313522; -.
DR BioCyc; MetaCyc:HS07624-MON; -.
DR BRENDA; 2.4.1.135; 2681.
DR PathwayCommons; O94766; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR SABIO-RK; O94766; -.
DR SignaLink; O94766; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 26229; 42 hits in 1073 CRISPR screens.
DR ChiTaRS; B3GAT3; human.
DR EvolutionaryTrace; O94766; -.
DR GeneWiki; B3GAT3; -.
DR GenomeRNAi; 26229; -.
DR Pharos; O94766; Tbio.
DR PRO; PR:O94766; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O94766; protein.
DR Bgee; ENSG00000149541; Expressed in right hemisphere of cerebellum and 137 other tissues.
DR ExpressionAtlas; O94766; baseline and differential.
DR Genevisible; O94766; HS.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IBA:GO_Central.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072542; F:protein phosphatase activator activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IDA:MGI.
DR GO; GO:0050651; P:dermatan sulfate proteoglycan biosynthetic process; IDA:MGI.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd00218; GlcAT-I; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005027; Glyco_trans_43.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..335
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 3"
FT /id="PRO_0000195176"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..335
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 243..252
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT REGION 312..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:11950836"
FT BINDING 82..84
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 113
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 156
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 161
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 194..196
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 308..310
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT SITE 227
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT SITE 318
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 33
FT /note="Interchain"
FT VAR_SEQ 304..335
FT /note="VLVWHTRTEKPKMKQEEQLQRQGRGSDPAIEV -> TESRCVTQAGVQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056347"
FT VARIANT 140
FT /note="P -> L (in JDSCD; reduced glucuronyltransferase
FT activity; patient fibroblasts have decreased levels of
FT dermatan sulfate, chondroitin sulfate and heparan sulfate
FT proteoglycans; dbSNP:rs879255269)"
FT /evidence="ECO:0000269|PubMed:25893793"
FT /id="VAR_075370"
FT VARIANT 223
FT /note="G -> S (in JDSCD; unknown pathological significance;
FT dbSNP:rs372487178)"
FT /evidence="ECO:0000269|PubMed:26086840"
FT /id="VAR_075371"
FT VARIANT 277
FT /note="R -> Q (in JDSCD; reduced glucuronyltransferase
FT activity; patient fibroblasts have decreased levels of
FT dermatan sulfate, chondroitin sulfate and heparan sulfate
FT proteoglycans; dbSNP:rs387906937)"
FT /evidence="ECO:0000269|PubMed:21763480,
FT ECO:0000269|PubMed:24668659"
FT /id="VAR_066624"
FT MUTAGEN 33
FT /note="C->A: Loss of dimer formation and reduced activity."
FT /evidence="ECO:0000269|PubMed:10842173"
FT MUTAGEN 281
FT /note="E->A: Absence of enzymatic activity in presence of
FT uridine diphosphate-glucuronic acid (UDP-GlcUA). Does not
FT increase PXYLP1-induced 2-phosphoxylose phosphatase
FT activity in presence of uridine diphosphate-glucuronic acid
FT (UDP-GlcUA)."
FT /evidence="ECO:0000269|PubMed:24425863,
FT ECO:0000303|PubMed:24425863"
FT MUTAGEN 301
FT /note="C->A: Enzyme inactivation and loss of
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:10842173"
FT CONFLICT 204
FT /note="F -> S (in Ref. 1; BAA34537)"
FT /evidence="ECO:0000305"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 103..116
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3CU0"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:3CU0"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:3CU0"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:3CU0"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:3CU0"
SQ SEQUENCE 335 AA; 37122 MW; 5EC45408597F1C0F CRC64;
MKLKLKNVFL AYFLVSIAGL LYALVQLGQP CDCLPPLRAA AEQLRQKDLR ISQLQAELRR
PPPAPAQPPE PEALPTIYVV TPTYARLVQK AELVRLSQTL SLVPRLHWLL VEDAEGPTPL
VSGLLAASGL LFTHLVVLTP KAQRLREGEP GWVHPRGVEQ RNKALDWLRG RGGAVGGEKD
PPPPGTQGVV YFADDDNTYS RELFEEMRWT RGVSVWPVGL VGGLRFEGPQ VQDGRVVGFH
TAWEPSRPFP VDMAGFAVAL PLLLDKPNAQ FDSTAPRGHL ESSLLSHLVD PKDLEPRAAN
CTRVLVWHTR TEKPKMKQEE QLQRQGRGSD PAIEV
