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   24-JAN-2024, entry version 145.
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.ENSMUSP00000105820; -.
DR   CAZy; GT14; Glycosyltransferase Family 14.
DR   GlyCosmos; P97402; 4 sites, No reported glycans.
DR   GlyGen; P97402; 4 sites.
DR   iPTMnet; P97402; -.
DR   PaxDb; 10090-ENSMUSP00000070942; -.
DR   ProteomicsDB; 268858; -.
DR   Antibodypedia; 10005; 268 antibodies from 25 providers.
DR   DNASU; 14538; -.
DR   Ensembl; ENSMUST00000069958.15; ENSMUSP00000070942.8; ENSMUSG00000021360.17.
DR   GeneID; 14538; -.
DR   KEGG; mmu:14538; -.
DR   UCSC; uc007qem.2; mouse.
DR   AGR; MGI:1100870; -.
DR   CTD; 2651; -.
DR   MGI; MGI:1100870; Gcnt2.
DR   VEuPathDB; HostDB:ENSMUSG00000021360; -.
DR   eggNOG; KOG0799; Eukaryota.
DR   GeneTree; ENSGT00940000156849; -.
DR   InParanoid; P97402; -.
DR   OrthoDB; 5403607at2759; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 14538; 5 hits in 79 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 219 other cell types or tissues.
DR   ExpressionAtlas; P97402; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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 phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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   PANTHER; PTHR19297; GLYCOSYLTRANSFERASE 14 FAMILY MEMBER; 1.
DR   PANTHER; PTHR19297:SF183; N-ACETYLLACTOSAMINIDE BETA-1,6-N-ACETYLGLUCOSAMINYL-TRANSFERASE; 1.
DR   Pfam; PF02485; Branch; 1.
DR   Genevisible; P97402; MM.
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
//