B3GLT_MOUSE
ID B3GLT_MOUSE Reviewed; 489 AA.
AC Q8BHT6; E9QMK8; Q0PCR7; Q149S5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Beta-1,3-glucosyltransferase;
DE Short=Beta3Glc-T;
DE EC=2.4.1.-;
DE AltName: Full=Beta 3-glucosyltransferase {ECO:0000312|MGI:MGI:2685903};
DE AltName: Full=Beta-3-glycosyltransferase-like;
GN Name=B3glct {ECO:0000312|MGI:MGI:2685903};
GN Synonyms=B3galtl {ECO:0000250|UniProtKB:Q6Y288}, Gm1057;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-352 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|PROSITE-ProRule:PRU10138}; Single-pass type II membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BHT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHT6-2; Sequence=VSP_020936;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AB253762; BAF02833.1; -; mRNA.
DR EMBL; AC114342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115781; AAI15782.1; -; mRNA.
DR EMBL; BC117522; AAI17523.1; -; mRNA.
DR EMBL; AK089440; BAC40885.1; -; mRNA.
DR CCDS; CCDS39410.1; -. [Q8BHT6-1]
DR RefSeq; NP_001074673.1; NM_001081204.1. [Q8BHT6-1]
DR AlphaFoldDB; Q8BHT6; -.
DR SMR; Q8BHT6; -.
DR BioGRID; 238051; 2.
DR STRING; 10090.ENSMUSP00000097972; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyConnect; 2149; 3 N-Linked glycans (1 site).
DR GlyGen; Q8BHT6; 2 sites, 3 N-linked glycans (1 site).
DR PhosphoSitePlus; Q8BHT6; -.
DR EPD; Q8BHT6; -.
DR MaxQB; Q8BHT6; -.
DR PaxDb; Q8BHT6; -.
DR PeptideAtlas; Q8BHT6; -.
DR PRIDE; Q8BHT6; -.
DR ProteomicsDB; 277146; -. [Q8BHT6-1]
DR ProteomicsDB; 277147; -. [Q8BHT6-2]
DR Antibodypedia; 2712; 108 antibodies from 25 providers.
DR Ensembl; ENSMUST00000100404; ENSMUSP00000097972; ENSMUSG00000051950. [Q8BHT6-1]
DR GeneID; 381694; -.
DR KEGG; mmu:381694; -.
DR UCSC; uc009aqc.1; mouse. [Q8BHT6-1]
DR UCSC; uc009aqd.1; mouse. [Q8BHT6-2]
DR CTD; 145173; -.
DR MGI; MGI:2685903; B3glct.
DR VEuPathDB; HostDB:ENSMUSG00000051950; -.
DR eggNOG; KOG2246; Eukaryota.
DR GeneTree; ENSGT00940000155499; -.
DR HOGENOM; CLU_030081_1_1_1; -.
DR InParanoid; Q8BHT6; -.
DR OMA; CATYPRF; -.
DR OrthoDB; 935669at2759; -.
DR PhylomeDB; Q8BHT6; -.
DR TreeFam; TF313496; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 381694; 3 hits in 74 CRISPR screens.
DR ChiTaRS; B3glct; mouse.
DR PRO; PR:Q8BHT6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BHT6; protein.
DR Bgee; ENSMUSG00000051950; Expressed in ciliary body and 218 other tissues.
DR Genevisible; Q8BHT6; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 Alternative splicing; Carbohydrate metabolism; Endoplasmic reticulum;
KW Fucose metabolism; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..489
FT /note="Beta-1,3-glucosyltransferase"
FT /id="PRO_0000252400"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 486..489
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..386
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020936"
FT CONFLICT 128
FT /note="L -> I (in Ref. 1; BAF02833)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="V -> I (in Ref. 1; BAF02833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55358 MW; 3FAD6846B25DB080 CRC64;
MRPPALLALF SCSAAFALMS EEIKEKVTPS QDLRQSSLPG RHDIDLKEIV FVIQSQSNSF
HAKRAEQLKK NILKQAANLT QDLPRVLLLH QLAKQEGAWT ILPLLPHFSV TYSKNSAWIF
FCEEETRLQI PRLLDTLRRY DPSKEWFLGK ALYDEESTII HHYAFSENPT VFKYPDFAAG
WALSIPLVNK LAKRLKSEAL KSDFTIDLKH EIALYIWDKG GGPALTPVPE FCTEDVDPRC
VTTFHSFLPL CGVPVKKEEI FVAVKTCKKF HADRIPIVKK TWAAQASLIE YYSDYAETAI
PTVDLGIPNT DRGHCGKTFA ILEKFLNHSH NKISWLVIVD DDTLISISRL RHLLSCYDSS
DPVFLGERYG YGLGTGGYSY VTGGGGMVFS REAIRRLLVS SCRCYSNDAP DDMVLGMCFS
GLGVPVTHSP LFHQARPVDY PKDYLAHQIP VSFHKHWHID PVKVYLTWLA PSEEDQATQE
TQKDPREEL
