MGT4C_DANRE
ID MGT4C_DANRE Reviewed; 454 AA.
AC Q5U3T0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C;
DE EC=2.4.1.145;
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVc;
DE Short=GnT-IVc;
DE Short=N-acetylglucosaminyltransferase IVc;
DE AltName: Full=UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVc;
GN Name=mgat4c; ORFNames=zgc:101663;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycosyltransferase that participates in the transfer of N-
CC acetylglucosamine (GlcNAc) to the core mannose residues of N-linked
CC glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the
CC GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-
CC (1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:16057, Rhea:RHEA-COMP:13526,
CC Rhea:RHEA-COMP:14374, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:60651, ChEBI:CHEBI:139507;
CC EC=2.4.1.145;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
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 54 family.
CC {ECO:0000305}.
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DR EMBL; BC085406; AAH85406.1; -; mRNA.
DR RefSeq; NP_001007438.1; NM_001007437.1.
DR RefSeq; XP_005161953.1; XM_005161896.3.
DR AlphaFoldDB; Q5U3T0; -.
DR STRING; 7955.ENSDARP00000101204; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR PaxDb; Q5U3T0; -.
DR Ensembl; ENSDART00000055148; ENSDARP00000055147; ENSDARG00000037852.
DR Ensembl; ENSDART00000114000; ENSDARP00000101204; ENSDARG00000037852.
DR GeneID; 492796; -.
DR KEGG; dre:492796; -.
DR ZFIN; ZDB-GENE-041114-149; zgc:101663.
DR eggNOG; ENOG502SJ9J; Eukaryota.
DR GeneTree; ENSGT00940000167901; -.
DR HOGENOM; CLU_027046_1_0_1; -.
DR InParanoid; Q5U3T0; -.
DR OMA; QDKVIRF; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q5U3T0; -.
DR TreeFam; TF324570; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5U3T0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000037852; Expressed in head kidney and 23 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:0008454; F:alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR006759; Glyco_transf_54.
DR PANTHER; PTHR12062; PTHR12062; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..454
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase C"
FT /id="PRO_0000288601"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..454
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 454 AA; 52254 MW; E22350447B8D300A CRC64;
MRCHLKKWVV VAAGLSILTS LYVYMQRAQS GNLKGSVIWT WDRESWMEGI KSHYLHFNIS
INVLGGVLQP SKKYLTVGLS SVRREKGFYL HDTLQSIFSE SSEEELDQMV VVVLLADFDL
PWIQQTADKI SREFAVQLSK GRLLVIHANK EHYPPLTGLK RNFNDAPDRV SFRSKQNVDY
SFLLHFSSNL SQYYIMLEDD VGCSRNFLSS IQQHIRSMTD SKWVTLEFSK LGYIGKLYQS
KDLPTLARFL YNFYQEMPCD FLLSHFRRLL MQDKVIRFRP SLFQHMGTYS SFRGTYNRLK
DEDFVQELAD NPPADVRTNI QVFQTYVPEK AYSQDVEYFW GVSPIGTESF FLVVFREAVR
ISRVQIHTGS DGKDELASAD VELGRVLVTG EPAVDCSGFK TLGSLQHGQF NEEGVQKLLP
DAVVCLRIRV TAAQPEWVII SRIQVWTVKE DKTI
