B3GLT_HUMAN
ID B3GLT_HUMAN Reviewed; 498 AA.
AC Q6Y288; A8K5F8; Q5W0H2; Q6NUI3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Beta-1,3-glucosyltransferase;
DE Short=Beta3Glc-T;
DE EC=2.4.1.-;
DE AltName: Full=Beta 3-glucosyltransferase {ECO:0000312|HGNC:HGNC:20207};
DE AltName: Full=Beta-3-glycosyltransferase-like;
GN Name=B3GLCT {ECO:0000312|HGNC:HGNC:20207}; Synonyms=B3GALTL, B3GTL;
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], TISSUE SPECIFICITY, AND VARIANT LYS-370.
RX PubMed=12943678; DOI=10.1016/s0006-291x(03)01540-7;
RA Heinonen T.Y.K., Pasternack L., Lindfors K., Breton C., Gastinel L.N.,
RA Maeki M., Kainulainen H.;
RT "A novel human glycosyltransferase: primary structure and characterization
RT of the gene and transcripts.";
RL Biochem. Biophys. Res. Commun. 309:166-174(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 495-ARG--LEU-498, AND VARIANT
RP LYS-370.
RX PubMed=16899492; DOI=10.1093/glycob/cwl035;
RA Sato T., Sato M., Kiyohara K., Sogabe M., Shikanai T., Kikuchi N.,
RA Togayachi A., Ishida H., Ito H., Kameyama A., Gotoh M., Narimatsu H.;
RT "Molecular cloning and characterization of a novel human beta1,3-
RT glucosyltransferase, which is localized at the endoplasmic reticulum and
RT glucosylates O-linked fucosylglycan on thrombospondin type 1 repeat
RT domain.";
RL Glycobiology 16:1194-1206(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-370.
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=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-370.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP INVOLVEMENT IN PTRPLS.
RX PubMed=16909395; DOI=10.1086/507567;
RA Lesnik Oberstein S.A., Kriek M., White S.J., Kalf M.E., Szuhai K.,
RA den Dunnen J.T., Breuning M.H., Hennekam R.C.M.;
RT "Peters plus syndrome is caused by mutations in B3GALTL, a putative
RT glycosyltransferase.";
RL Am. J. Hum. Genet. 79:562-566(2006).
CC -!- FUNCTION: O-glucosyltransferase that transfers glucose toward fucose
CC with a beta-1,3 linkage. Specifically glucosylates O-linked
CC fucosylglycan on TSP type-1 domains of proteins, thereby contributing
CC to elongation of O-fucosylglycan. {ECO:0000269|PubMed:16899492}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:16899492};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:16899492}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in testis and
CC uterus. {ECO:0000269|PubMed:12943678, ECO:0000269|PubMed:16899492}.
CC -!- DISEASE: Peters-plus syndrome (PTRPLS) [MIM:261540]: An autosomal
CC recessive disorder characterized by anterior eye-chamber abnormalities,
CC disproportionate short stature, developmental delay, characteristic
CC craniofacial features, cleft lip and/or palate.
CC {ECO:0000269|PubMed:16909395}. 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}.
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DR EMBL; AY190526; AAO37647.1; -; mRNA.
DR EMBL; AB101481; BAD13528.1; -; mRNA.
DR EMBL; AK291273; BAF83962.1; -; mRNA.
DR EMBL; AL137142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08483.1; -; Genomic_DNA.
DR EMBL; BC068595; AAH68595.1; -; mRNA.
DR CCDS; CCDS9341.1; -.
DR RefSeq; NP_919299.3; NM_194318.3.
DR AlphaFoldDB; Q6Y288; -.
DR SMR; Q6Y288; -.
DR BioGRID; 126890; 35.
DR IntAct; Q6Y288; 13.
DR STRING; 9606.ENSP00000343002; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q6Y288; 1 site.
DR iPTMnet; Q6Y288; -.
DR PhosphoSitePlus; Q6Y288; -.
DR SwissPalm; Q6Y288; -.
DR BioMuta; B3GLCT; -.
DR DMDM; 116243011; -.
DR EPD; Q6Y288; -.
DR jPOST; Q6Y288; -.
DR MassIVE; Q6Y288; -.
DR MaxQB; Q6Y288; -.
DR PaxDb; Q6Y288; -.
DR PeptideAtlas; Q6Y288; -.
DR PRIDE; Q6Y288; -.
DR ProteomicsDB; 67832; -.
DR Antibodypedia; 2712; 108 antibodies from 25 providers.
DR DNASU; 145173; -.
DR Ensembl; ENST00000343307.5; ENSP00000343002.4; ENSG00000187676.8.
DR GeneID; 145173; -.
DR KEGG; hsa:145173; -.
DR MANE-Select; ENST00000343307.5; ENSP00000343002.4; NM_194318.4; NP_919299.3.
DR UCSC; uc010aaz.4; human.
DR CTD; 145173; -.
DR DisGeNET; 145173; -.
DR GeneCards; B3GLCT; -.
DR GeneReviews; B3GLCT; -.
DR HGNC; HGNC:20207; B3GLCT.
DR HPA; ENSG00000187676; Low tissue specificity.
DR MalaCards; B3GLCT; -.
DR MIM; 261540; phenotype.
DR MIM; 610308; gene.
DR neXtProt; NX_Q6Y288; -.
DR OpenTargets; ENSG00000187676; -.
DR Orphanet; 709; Peters plus syndrome.
DR PharmGKB; PA144596515; -.
DR VEuPathDB; HostDB:ENSG00000187676; -.
DR eggNOG; KOG2246; Eukaryota.
DR GeneTree; ENSGT00940000155499; -.
DR HOGENOM; CLU_030081_1_1_1; -.
DR InParanoid; Q6Y288; -.
DR OMA; CATYPRF; -.
DR OrthoDB; 935669at2759; -.
DR PhylomeDB; Q6Y288; -.
DR TreeFam; TF313496; -.
DR PathwayCommons; Q6Y288; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q6Y288; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 145173; 16 hits in 1070 CRISPR screens.
DR ChiTaRS; B3GLCT; human.
DR GeneWiki; B3GALTL; -.
DR GenomeRNAi; 145173; -.
DR Pharos; Q6Y288; Tbio.
DR PRO; PR:Q6Y288; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q6Y288; protein.
DR Bgee; ENSG00000187676; Expressed in left ventricle myocardium and 146 other tissues.
DR Genevisible; Q6Y288; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; TAS:Reactome.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0036066; P:protein O-linked fucosylation; TAS:Reactome.
DR InterPro; IPR003378; Fringe-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF02434; Fringe; 2.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Congenital disorder of glycosylation; Dwarfism;
KW Endoplasmic reticulum; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..498
FT /note="Beta-1,3-glucosyltransferase"
FT /id="PRO_0000252399"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..498
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 495..498
FT /note="Prevents secretion from ER"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 370
FT /note="E -> K (in dbSNP:rs1041073)"
FT /evidence="ECO:0000269|PubMed:12943678,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:16899492,
FT ECO:0000269|Ref.5"
FT /id="VAR_027849"
FT MUTAGEN 495..498
FT /note="Missing: Abolishes endoplasmic reticulum
FT localization."
FT /evidence="ECO:0000269|PubMed:16899492"
FT CONFLICT 284
FT /note="I -> M (in Ref. 6; AAH68595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 56564 MW; CDC6A479A1564D48 CRC64;
MRPPACWWLL APPALLALLT CSLAFGLASE DTKKEVKQSQ DLEKSGISRK NDIDLKGIVF
VIQSQSNSFH AKRAEQLKKS ILKQAADLTQ ELPSVLLLHQ LAKQEGAWTI LPLLPHFSVT
YSRNSSWIFF CEEETRIQIP KLLETLRRYD PSKEWFLGKA LHDEEATIIH HYAFSENPTV
FKYPDFAAGW ALSIPLVNKL TKRLKSESLK SDFTIDLKHE IALYIWDKGG GPPLTPVPEF
CTNDVDFYCA TTFHSFLPLC RKPVKKKDIF VAVKTCKKFH GDRIPIVKQT WESQASLIEY
YSDYTENSIP TVDLGIPNTD RGHCGKTFAI LERFLNRSQD KTAWLVIVDD DTLISISRLQ
HLLSCYDSGE PVFLGERYGY GLGTGGYSYI TGGGGMVFSR EAVRRLLASK CRCYSNDAPD
DMVLGMCFSG LGIPVTHSPL FHQARPVDYP KDYLSHQVPI SFHKHWNIDP VKVYFTWLAP
SDEDKARQET QKGFREEL
