B3GN4_MOUSE
ID B3GN4_MOUSE Reviewed; 350 AA.
AC Q1RLK6; E9QPF4; Q923H4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4;
DE EC=2.4.1.149 {ECO:0000250|UniProtKB:Q9C0J1};
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 4;
DE Short=BGnT-4;
DE Short=Beta-1,3-Gn-T4;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 4;
DE Short=Beta3Gn-T4;
DE EC=2.4.1.-;
GN Name=B3gnt4;
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].
RC STRAIN=129/Sv;
RA Zhou D., Hennet T.;
RT "Mouse beta1,3 N-acetylglucosaminyltransferase-4.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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].
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).
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the
CC synthesis of poly-N-acetyllactosamine. Has activity for type 2
CC oligosaccharides. {ECO:0000250|UniProtKB:Q9C0J1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:14389,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:134090; EC=2.4.1.149;
CC Evidence={ECO:0000250|UniProtKB:Q9C0J1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AY037786; AAK68856.1; -; mRNA.
DR EMBL; AC157931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114987; AAI14988.1; -; mRNA.
DR EMBL; BC115755; AAI15756.1; -; mRNA.
DR CCDS; CCDS19665.1; -.
DR RefSeq; NP_941013.2; NM_198611.2.
DR RefSeq; XP_006530374.1; XM_006530311.3.
DR RefSeq; XP_006530376.1; XM_006530313.3.
DR RefSeq; XP_011246502.1; XM_011248200.2.
DR AlphaFoldDB; Q1RLK6; -.
DR SMR; Q1RLK6; -.
DR STRING; 10090.ENSMUSP00000031384; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q1RLK6; 2 sites.
DR PhosphoSitePlus; Q1RLK6; -.
DR PaxDb; Q1RLK6; -.
DR PRIDE; Q1RLK6; -.
DR Antibodypedia; 31630; 88 antibodies from 19 providers.
DR DNASU; 231727; -.
DR Ensembl; ENSMUST00000031384; ENSMUSP00000031384; ENSMUSG00000029431.
DR GeneID; 231727; -.
DR KEGG; mmu:231727; -.
DR UCSC; uc008znw.1; mouse.
DR CTD; 79369; -.
DR MGI; MGI:2680208; B3gnt4.
DR VEuPathDB; HostDB:ENSMUSG00000029431; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000162236; -.
DR HOGENOM; CLU_036849_5_3_1; -.
DR InParanoid; Q1RLK6; -.
DR OMA; WDFAEDF; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q1RLK6; -.
DR TreeFam; TF318639; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 231727; 1 hit in 75 CRISPR screens.
DR ChiTaRS; B3gnt4; mouse.
DR PRO; PR:Q1RLK6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q1RLK6; protein.
DR Bgee; ENSMUSG00000029431; Expressed in animal zygote and 35 other tissues.
DR Genevisible; Q1RLK6; MM.
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:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..350
FT /note="N-acetyllactosaminide beta-1,3-N-
FT acetylglucosaminyltransferase 4"
FT /id="PRO_0000289208"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..350
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="P -> S (in Ref. 1; AAK68856 and 3; AAI14988/
FT AAI15756)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="M -> R (in Ref. 1; AAK68856)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="M -> T (in Ref. 3; AAI14988/AAI15756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 39873 MW; 3086DAE555E1C336 CRC64;
MLPRLGCVLF CSLVVLLLSC LLLLKERIPA GSSKAHQQFL ALPRSHHSQC SPNLTVVNTS
LSLPSRHRLF LTYRHCRNFS ILLEPSECAR DTFLLLVIKS QPAHIEQRSA IRSTWGRAGS
WARGRQLKLV FLLGVAGPVP PAQLLVYESW QFDDILQWDF AEDFFNLTLK ELHVQRWIAA
ACTQAHFILK GDDDVFIHVP NVLEFLEGWD PAQDFLVGDV IRLARPNRNT KVKYFIPFSM
YRARHYPPYA GGGGYVMSQA TVRHLHMAME EAELFPIDDV FVGMCLRKLG VTPIHHAGFK
TFGIQQPLNP RDPCLYKGLL LVHRLSPLEM WTMWALVTDE RLKCAATHKP
