GCNT1_BOVIN
ID GCNT1_BOVIN Reviewed; 427 AA.
AC Q92180;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase;
DE EC=2.4.1.102 {ECO:0000305|PubMed:9490652};
DE AltName: Full=Core 2 beta-1,6-N-acetylglucosaminyltransferase {ECO:0000250|UniProtKB:Q09324};
DE Short=C2GlcNAcT {ECO:0000250|UniProtKB:Q09324};
DE AltName: Full=Core 2-branching enzyme;
DE AltName: Full=Core2-GlcNAc-transferase;
DE Short=C2GNT;
DE Short=Core 2 GNT;
DE AltName: Full=Leukocyte type core 2 beta-1,6-N-acetylglucosaminyltransferase {ECO:0000250|UniProtKB:Q09324};
DE Short=C2GnT-L {ECO:0000250|UniProtKB:Q09324};
GN Name=GCNT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9490652; DOI=10.1165/ajrcmb.18.3.2593;
RA Li C.-M., Adler K.B., Cheng P.W.;
RT "Mucin biosynthesis: molecular cloning and expression of bovine lung mucin
RT core 2 N-acetylglucosaminyltransferase cDNA.";
RL Am. J. Respir. Cell Mol. Biol. 18:343-352(1998).
CC -!- FUNCTION: Glycosyltransferase that catalyzes the transfer of an N-
CC acetylglucosamine (GlcNAc) moiety in beta1-6 linkage from UDP-GlcNAc
CC onto mucin-type core 1 O-glycan to form the branched mucin-type core 2
CC O-glycan. The catalysis is metal ion-independent and occurs with
CC inversion of the anomeric configuration of sugar donor (PubMed:9490652)
CC (By similarity). Selectively involved in synthesis of mucin-type core 2
CC O-glycans that serve as scaffolds for the display of selectin ligand
CC sialyl Lewis X epitope by myeloid cells, with an impact on homeostasis
CC and recruitment to inflammatory sites (By similarity). Can also act on
CC glycolipid substrates. Transfers GlcNAc moiety to GalGb4Cer globosides
CC in a reaction step to the synthesis of stage-specific embryonic antigen
CC 1 (SSEA-1) determinant (By similarity). Can use Galbeta1-
CC 3GalNAcalpha1- and Galbeta1-3GalNAcbeta1- oligosaccharide derivatives
CC as acceptor substrates (By similarity). {ECO:0000250|UniProtKB:Q09324,
CC ECO:0000269|PubMed:9490652}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine
CC = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13922, Rhea:RHEA-
CC COMP:14419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:137949, ChEBI:CHEBI:139605; EC=2.4.1.102;
CC Evidence={ECO:0000305|PubMed:9490652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56213;
CC Evidence={ECO:0000305|PubMed:9490652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:56216, Rhea:RHEA-COMP:13923,
CC Rhea:RHEA-COMP:14420, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:137950, ChEBI:CHEBI:139607;
CC EC=2.4.1.102; Evidence={ECO:0000305|PubMed:9490652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56217;
CC Evidence={ECO:0000305|PubMed:9490652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside GalGb4Cer + UDP-N-acetyl-alpha-D-glucosamine =
CC globoside GlcNAc-(beta1->6)-GalGb4Cer + H(+) + UDP;
CC Xref=Rhea:RHEA:56900, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:140691, ChEBI:CHEBI:140702;
CC Evidence={ECO:0000250|UniProtKB:Q09324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56901;
CC Evidence={ECO:0000250|UniProtKB:Q09324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GA1 + UDP-N-acetyl-alpha-D-glucosamine =
CC ganglioside beta-DGlcNAc-(1->6)-GA1 + H(+) + UDP;
CC Xref=Rhea:RHEA:69691, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:88069, ChEBI:CHEBI:187897;
CC Evidence={ECO:0000250|UniProtKB:Q09324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69692;
CC Evidence={ECO:0000250|UniProtKB:Q09324};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q02742}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:Q09324}.
CC -!- SUBUNIT: Interacts with GOLPH3; may control GCNT1 retention in the
CC Golgi. {ECO:0000250|UniProtKB:Q02742}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q02742}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q02742}. Note=Also detected in the trans-Golgi
CC network. {ECO:0000250|UniProtKB:Q02742}.
CC -!- TISSUE SPECIFICITY: Expressed in tracheal submucosal glands and
CC epithelium (at protein level). {ECO:0000269|PubMed:9490652}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC {ECO:0000305}.
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DR EMBL; U41320; AAA83244.1; -; mRNA.
DR AlphaFoldDB; Q92180; -.
DR SMR; Q92180; -.
DR STRING; 9913.ENSBTAP00000044098; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PaxDb; Q92180; -.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; Q92180; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0003829; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0060352; P:cell adhesion molecule production; ISS:UniProtKB.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISS:UniProtKB.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0016268; P:O-glycan processing, core 2; ISS:UniProtKB.
DR InterPro; IPR003406; Glyco_trans_14.
DR Pfam; PF02485; Branch; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..427
FT /note="Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-
FT 1,6-N-acetylglucosaminyltransferase"
FT /id="PRO_0000191394"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..427
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 5..9
FT /note="Mediates interaction with GOLPH3 and is necessary
FT and sufficient for localization to the Golgi"
FT /evidence="ECO:0000250|UniProtKB:Q02742"
FT REGION 33..121
FT /note="Stem region"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT REGION 122..427
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 128..130
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 155..157
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 187
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 243
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 251
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 254
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 320
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 341
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 358
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 377
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 400
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..412
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT DISULFID 100..172
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT DISULFID 151..199
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT DISULFID 372..380
FT /evidence="ECO:0000250|UniProtKB:Q09324"
SQ SEQUENCE 427 AA; 49734 MW; 41B9CBFD948D4196 CRC64;
MLRKLWRRKL FSFPTKYYFL FLAFSVVTFT VLRIHQKTEF VNFGHLELFE ENPSSNINCT
KILQGDVDEI QKVKLESLTV KFKKRARWTN YDYINMTGDC ASFIKKRKYI TEPLSKEEAG
FPIAYSIVVH HKIEMLDRLL RAIYMPQNFY CIHVDAKSEK SFLAAAVGIA SCFSNVFVAS
QLESVVYASW SRVQADLNCM QDLYQMNAGW KYLINLCGMD FPIKTNLEIV RKLKLLMGEN
NLETEKMPSH KKERWKKHYE VVNGKLTNMG TDKIHPPLET PLFSGSAHFV VSREYVEYVL
QNQNIQKFME WAKDTYSPDE YLWATIQRIP EVPGSLSLSY KYDTSDMQAI ARFVKWQYFE
GDVSKGAPYP PCSVHVRSVC VFGAGDLNWL LHVHHLFANK FDTDIDLFAI QCLDEHLRHK
ALETLKP
