ID   BAGT_LYMST              Reviewed;         490 AA.
AC   Q09323;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Beta-N-acetyl-D-glucosaminide beta-1,4-N-acetylglucosaminyl-transferase;
DE            EC=2.4.1.-;
DE   AltName: Full=Beta-1,4-GlcNAcT;
DE   AltName: Full=UDP-GlcNAc:GlcNAc beta-R beta-1,4-N-acetylglucosaminyl-transferase;
GN   Name=GNT;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Prostate;
RX   PubMed=7527028; DOI=10.1016/s0021-9258(18)43816-1;
RA   Bakker H., Agterberg M., van Tetering A., Koeleman C.A.M.,
RA   van den Eijnden D.H., van Die I.;
RT   "A Lymnaea stagnalis gene, with sequence similarity to that of mammalian
RT   beta 1-->4-galactosyltransferases, encodes a novel UDP-GlcNAc:GlcNAc beta-R
RT   beta 1-->4-N-acetylglucosaminyltransferase.";
RL   J. Biol. Chem. 269:30326-30333(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-
CC         alpha-D-glucosamine = an N-acetyl-beta-D-glucosaminyl-(1->4)-N-
CC         acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC         Xref=Rhea:RHEA:52816, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:136857;
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 7 family. {ECO:0000305}.
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DR   EMBL; X80228; CAA56514.1; -; mRNA.
DR   PIR; A55141; A55141.
DR   AlphaFoldDB; Q09323; -.
DR   SMR; Q09323; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   PRIDE; Q09323; -.
DR   UniPathway; UPA00378; -.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003859; Galactosyl_T.
DR   InterPro; IPR027791; Galactosyl_T_C.
DR   InterPro; IPR027995; Galactosyl_T_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR19300; PTHR19300; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..490
FT                   /note="Beta-N-acetyl-D-glucosaminide beta-1,4-N-
FT                   acetylglucosaminyl-transferase"
FT                   /id="PRO_0000080553"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..50
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..490
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   490 AA;  55418 MW;  3A4B88FB16671CB8 CRC64;
     MYLVVCWGRV TGNMISTRHC FSRCKSRSVR VIKATAMLFV AAMLFLALHM NFSHEASQQN
     LHRAAPISSP TTISRSTVQI RNATHDFLPA SSTPMKDELI ETESEFVDGF QRNEVIACSD
     TSEEFRTDSK RITLVNSQSG VPCPIRPPAL AGRFVPSKKS STYHELAAMF PDVQDGGHYT
     PRMCTPAEKT AIIIPYRNRC RHLYTLLPNL IPMLMRQNVD FTIFVIEQTT PETFNKGILF
     NAGYLEALKV DNYDCFILHD VDMIPIDDRN MYRCNKMGPV HFSPGVNKFK YKLFYSGLFG
     GVVGFTREQF RLINGASNLY FGWGGEDDDL RNRAVHMKLP LLRKTLAHGL YDMVSHVEAG
     WNVNPHSKGA HSLYDMLNKA LGVQAGWNVH PNSKWPLRLF DSVNHAPAEG AGWNVNPDRF
     KIYSTSRQRQ HVDGINSLVY NVTWYRTSPL YTWVGVGFNK TVITNSIPED LRIGPEADNT
     YLTGNFTIIS