MGT4C_MACFA
ID MGT4C_MACFA Reviewed; 478 AA.
AC Q4R4A8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=QtsA-11376;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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 Essential for the production of tri- and tetra-antennary N-linked sugar
CC chains. Does not catalyze the transfer of GlcNAc to the Manalpha1-6 arm
CC to form GlcNAcBeta1-4Manalpha1-6 linkage ('GnT-VI' activity) (By
CC 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; AB179007; BAE02058.1; -; mRNA.
DR RefSeq; NP_001270014.1; NM_001283085.1.
DR RefSeq; XP_015286134.1; XM_015430648.1.
DR RefSeq; XP_015286135.1; XM_015430649.1.
DR RefSeq; XP_015286136.1; XM_015430650.1.
DR RefSeq; XP_015286137.1; XM_015430651.1.
DR RefSeq; XP_015286138.1; XM_015430652.1.
DR RefSeq; XP_015286139.1; XM_015430653.1.
DR AlphaFoldDB; Q4R4A8; -.
DR STRING; 9541.XP_005571726.1; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR Ensembl; ENSMFAT00000034156; ENSMFAP00000026001; ENSMFAG00000044473.
DR GeneID; 101866242; -.
DR KEGG; mcf:101866242; -.
DR CTD; 25834; -.
DR VEuPathDB; HostDB:ENSMFAG00000044473; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155352; -.
DR OMA; RQCTTYL; -.
DR OrthoDB; 593094at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000233100; Chromosome 11.
DR Bgee; ENSMFAG00000044473; Expressed in frontal cortex and 3 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: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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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..478
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase C"
FT /id="PRO_0000288597"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..478
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 478 AA; 56089 MW; 7E0AA1B8686800C6 CRC64;
MFKFHQMKHI FEILDKMRCL RKRSTVSFLG VLVIFLLFMN LYIEDSYVLE GDKQLIRETS
THQLNSERYV HTFKDLSNFS GAINVTYRYL AATPLQRKRY LTIGLSSVKR KKGNYLLETI
KSIFEQSSYE ELKEISVVVH LADFNSSWRD AMVQDITQKF AHHIIAGRLM VIHAPEEYYP
ILDGLKRNYN DPEDRVKFRS KQNVDYAFLL NFCANTSDYY VMLEDDVRCS KNFLTAIKKV
IASLEGTYWV TLEFSKLGYI GKLYHSHDLP RLAHFLLMFY QEMPCDWLLT HFRGLLAQKN
VIRFKPSLFQ HMGYYSSYKG TENKLKDDDF EEESFDIPDN PPASLYTNMN VFENYEASKA
YSSVDEYFWG KPPSTGDVFV IVFENPIIIK KIKVNTGTED RQNDILHHGA LDVGENVMPS
KRRRQCSTYL RLGEFKNGNF EMSGVNQKIP FDIHCMRIYV TKTQKEWLII RSISIWTS
