GCNT2_MOUSE
ID GCNT2_MOUSE Reviewed; 401 AA.
AC P97402; Q6T5E3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase;
DE Short=N-acetylglucosaminyltransferase;
DE EC=2.4.1.150;
DE AltName: Full=I-branching enzyme;
DE AltName: Full=IGNT;
DE AltName: Full=Large I antigen-forming beta-1,6-N-acetylglucosaminyltransferase;
GN Name=Gcnt2;
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].
RX PubMed=9134435; DOI=10.1093/glycob/7.2.285;
RA Magnet A.D., Fukuda M.;
RT "Expression of the large I antigen forming beta-1,6-N-
RT acetylglucosaminyltransferase in various tissues of adult mice.";
RL Glycobiology 7:285-295(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=14672974; DOI=10.1101/gr.1225204;
RA Zhang T., Haws P., Wu Q.;
RT "Multiple variable first exons: a mechanism for cell- and tissue-specific
RT gene regulation.";
RL Genome Res. 14:79-89(2004).
RN [3]
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).
CC -!- FUNCTION: Branching enzyme that converts linear into branched poly-N-
CC acetyllactosaminoglycans. Introduces the blood group I antigen during
CC embryonic development. It is closely associated with the development
CC and maturation of erythroid cells.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-GlcNAc derivative + UDP-N-acetyl-alpha-D-glucosamine = a beta-
CC D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-[beta-D-GlcNAc-(1->6)]-beta-D-Gal-
CC (1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC Xref=Rhea:RHEA:54820, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:138371, ChEBI:CHEBI:138372;
CC EC=2.4.1.150;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Gcnt2 - I
CC branching beta-6-GlcNAcT2, variant 3 (IGnT);
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_563";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Gcnt2 - I
CC branching beta-6-GlcNAcT2, variant 1 (IGnT);
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_587";
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DR EMBL; U68182; AAB39621.1; -; mRNA.
DR EMBL; AY435149; AAR95650.1; -; mRNA.
DR EMBL; AC133496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS26468.1; -.
DR RefSeq; NP_032131.2; NM_008105.3.
DR AlphaFoldDB; P97402; -.
DR SMR; P97402; -.
DR BioGRID; 199870; 2.
DR STRING; 10090.ENSMUSP00000070942; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; P97402; 4 sites.
DR iPTMnet; P97402; -.
DR PRIDE; P97402; -.
DR ProteomicsDB; 268858; -.
DR Antibodypedia; 10005; 235 antibodies from 25 providers.
DR DNASU; 14538; -.
DR Ensembl; ENSMUST00000069958; ENSMUSP00000070942; ENSMUSG00000021360.
DR GeneID; 14538; -.
DR KEGG; mmu:14538; -.
DR UCSC; uc007qem.2; mouse.
DR CTD; 2651; -.
DR MGI; MGI:1100870; Gcnt2.
DR VEuPathDB; HostDB:ENSMUSG00000021360; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000156849; -.
DR InParanoid; P97402; -.
DR OrthoDB; 791893at2759; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14538; 5 hits in 74 CRISPR screens.
DR PRO; PR:P97402; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P97402; protein.
DR Bgee; ENSMUSG00000021360; Expressed in lumbar dorsal root ganglion and 216 other tissues.
DR ExpressionAtlas; P97402; baseline and differential.
DR Genevisible; P97402; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:MGI.
DR GO; GO:0008109; F:N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity; ISO:MGI.
DR GO; GO:0036438; P:maintenance of lens transparency; ISO:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR InterPro; IPR003406; Glyco_trans_14.
DR Pfam; PF02485; Branch; 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..401
FT /note="N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-
FT transferase"
FT /id="PRO_0000191398"
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..401
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="P -> L (in Ref. 1; AAB39621)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..22
FT /note="IVFIVL -> MVCVVS (in Ref. 1; AAB39621)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..45
FT /note="MLA -> RLS (in Ref. 1; AAB39621)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="V -> G (in Ref. 1; AAB39621)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> V (in Ref. 1; AAB39621)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="Missing (in Ref. 1; AAB39621)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="H -> Q (in Ref. 1; AAB39621)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="I -> S (in Ref. 1; AAB39621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 45697 MW; 4DBD498E6EEEDF13 CRC64;
MPPSVRYFFI VSVTTVIVFI VLYVLSFGGD QSYQKLNISD SVMLAQVCSS FIDGKSRFLW
RNKLMIHEKP SCTEYVTQSH YITAPLSQEE VDFPLAYVMV IHHNFDTFAR LFRAIFMPQN
IYCVHVDEKA TAEFKGAVEQ LVSCFPNAFL ASKMEPVVYG GISRLQADLN CIKDLSTSEV
PWKYAINTCG QDFPLKTNKE IVQYLKGLKG KNLTPGVLPP AHAIGRTRYV HREHLSKELS
YVIRTTALKP PPPHNLTIYF GSAYVALSRE FANFVLRDPR AVDLLHWSKD TFSPDEHFWV
TLNRIPGVPG SMPPNASWTG NLRAVKWMDM EAKHGGCHGH YVHGICIYGN GDLQWLINSQ
SLFANKFELN TYPLTVECLE LRLRERTLNQ SEIAIQPSWY F
