GCNT4_MOUSE
ID GCNT4_MOUSE Reviewed; 455 AA.
AC E9Q649;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4;
DE EC=2.4.1.102 {ECO:0000250|UniProtKB:Q9P109};
DE AltName: Full=Core 2-branching enzyme 3;
DE AltName: Full=Core2-GlcNAc-transferase 3;
DE Short=C2GnT3;
GN Name=Gcnt4;
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 [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: Glycosyltransferase that mediates core 2 O-glycan branching,
CC an important step in mucin-type biosynthesis. Does not have core 4 O-
CC glycan or I-branching enzyme activity. {ECO:0000250|UniProtKB:Q9P109}.
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:0000250|UniProtKB:Q9P109};
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:0000250|UniProtKB:Q9P109};
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 14 family.
CC {ECO:0000305}.
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DR EMBL; AC174082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49336.1; -.
DR RefSeq; NP_001159537.1; NM_001166065.1.
DR RefSeq; XP_006517659.1; XM_006517596.3.
DR RefSeq; XP_006517660.1; XM_006517597.2.
DR RefSeq; XP_006517661.1; XM_006517598.2.
DR RefSeq; XP_006517662.1; XM_006517599.2.
DR RefSeq; XP_006517663.1; XM_006517600.2.
DR RefSeq; XP_006517664.1; XM_006517601.3.
DR AlphaFoldDB; E9Q649; -.
DR SMR; E9Q649; -.
DR BioGRID; 230036; 1.
DR STRING; 10090.ENSMUSP00000130496; -.
DR GlyGen; E9Q649; 3 sites.
DR PhosphoSitePlus; E9Q649; -.
DR PaxDb; E9Q649; -.
DR PRIDE; E9Q649; -.
DR ProteomicsDB; 273429; -.
DR Antibodypedia; 24369; 78 antibodies from 21 providers.
DR Ensembl; ENSMUST00000171324; ENSMUSP00000130496; ENSMUSG00000091387.
DR GeneID; 218476; -.
DR KEGG; mmu:218476; -.
DR UCSC; uc007rno.2; mouse.
DR CTD; 51301; -.
DR MGI; MGI:2684919; Gcnt4.
DR VEuPathDB; HostDB:ENSMUSG00000091387; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000159721; -.
DR HOGENOM; CLU_032341_1_2_1; -.
DR InParanoid; E9Q649; -.
DR OMA; YVKLPVR; -.
DR OrthoDB; 868849at2759; -.
DR PhylomeDB; E9Q649; -.
DR TreeFam; TF315534; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 218476; 1 hit in 71 CRISPR screens.
DR PRO; PR:E9Q649; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; E9Q649; protein.
DR Bgee; ENSMUSG00000091387; Expressed in secondary oocyte and 38 other tissues.
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; IEA:UniProtKB-EC.
DR GO; GO:0002121; P:inter-male aggressive behavior; IMP:MGI.
DR GO; GO:0060993; P:kidney morphogenesis; IGI:MGI.
DR GO; GO:0001780; P:neutrophil homeostasis; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0042403; P:thyroid hormone metabolic process; IMP:MGI.
DR GO; GO:0048729; P:tissue morphogenesis; IMP:MGI.
DR InterPro; IPR003406; Glyco_trans_14.
DR Pfam; PF02485; Branch; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..455
FT /note="Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-
FT 1,6-N-acetylglucosaminyltransferase 4"
FT /id="PRO_0000415825"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..455
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..228
FT /evidence="ECO:0000250"
FT DISULFID 162..383
FT /evidence="ECO:0000250"
FT DISULFID 183..210
FT /evidence="ECO:0000250"
FT DISULFID 392..424
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 52832 MW; EB0F6734CCC898B2 CRC64;
MKIFRCCFKY TLQQKLFILL LTLWLFSLLK LLNVGRLLFP QRDIYLVEYS LSTSPFVRNR
FPESGDAARD NVNCSGVYEH EPLEIGKSLE IRRRSIIDLE DGDVVAMTSD CDVYQTLRQY
HEKLVSREEE DFPIAYSLVV HKDAIMVERL IRAIYNQHNL YCIHYDLKSP DTFKAAMNNL
AKCFPNIFIA SKLETVEYAH ISRLQADWNC LSDLLKSSVQ WKYVINLCGQ DFPLKSNFEL
VTELKSLQGR NMLETVRPPS AKTERFTYHH ELRQVPYDYM KLPVKTNVSK GAPPHNIQVF
VGSAYFVLSR AFVKYIFNSS LVEDFFAWSK DTYSPDEHFW ATLIRIPGIP GGISSSSQDV
SDLQSKTRLV KWFYYEGFLY PNCTGSHLRS VCIYGAAELR WLLNEGHWFA NKFDSKVDPI
LMKCLAEKLE EQQRKLIALS SEKFMTEGTR QSHTL
