MGT4C_PIG
ID MGT4C_PIG Reviewed; 478 AA.
AC Q6ITT3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.G., Vallet J.L., Nonneman D., Rohrer G.A., Christenson R.K.;
RT "Characterization of porcine UDP-N-acetylglucosamine:a-1,3-D-mannoside
RT beta-1,4-N-acetylglucosaminyltransferase IV-homolog (HGNT-IV-H).";
RL Submitted (MAY-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 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; AY626239; AAT45730.1; -; mRNA.
DR RefSeq; NP_001001859.1; NM_001001859.1.
DR AlphaFoldDB; Q6ITT3; -.
DR SMR; Q6ITT3; -.
DR STRING; 9823.ENSSSCP00000000994; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR PaxDb; Q6ITT3; -.
DR Ensembl; ENSSSCT00005068212; ENSSSCP00005042427; ENSSSCG00005042510.
DR Ensembl; ENSSSCT00015036603; ENSSSCP00015014568; ENSSSCG00015027448.
DR Ensembl; ENSSSCT00025060305; ENSSSCP00025025572; ENSSSCG00025044359.
DR Ensembl; ENSSSCT00030096002; ENSSSCP00030044243; ENSSSCG00030068629.
DR Ensembl; ENSSSCT00045035605; ENSSSCP00045024734; ENSSSCG00045020885.
DR Ensembl; ENSSSCT00055048911; ENSSSCP00055039047; ENSSSCG00055024806.
DR Ensembl; ENSSSCT00060046367; ENSSSCP00060019859; ENSSSCG00060034183.
DR Ensembl; ENSSSCT00065000413; ENSSSCP00065000059; ENSSSCG00065000372.
DR GeneID; 414851; -.
DR KEGG; ssc:414851; -.
DR CTD; 25834; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q6ITT3; -.
DR OrthoDB; 593094at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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..478
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase C"
FT /id="PRO_0000288599"
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"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 478 AA; 56312 MW; AA4DDEF8554ACE25 CRC64;
MFKFHQVKHI FEILDKMRCL RKRFTVSFLG VLVIFLLFMN LYIEDSYVLE GDKQLVRETS
IHQLNPERYV HTFKYLSNFS GTINVTYRYL AVMPFQRKRF LTIGLSSVRR KKGNYLLETI
KSIFEQSSYE ELKEISVVVH LADFNSSWRE VMVQDITQKF AHHIIAGRLM VIHAPEEYYP
VLNGLKRNYN DPEDRVRFRS KQNVDYAFLL NFCANISDYY VMLEDDVRCS KNFLTAIKKV
ITSLQGTYWV TLEFSKLGYI GKLYHSHDLP RLAHFLLMFY QEMPCDWLLT HFRGLLAQKN
VIRFKPSLFQ HMGYYSSYKG TENKLKDDDF EEELIDLPDN PPASLYTNMS VFENYDASKA
YSSVDGYFWG KPPSTGDVFV VVFENPVIIK KIKVSTGTED RQNDILHHGA LDVGGYIRYF
KQNRQCITYI RLGEFKNGNF EVSDVNQKIP FDVHCMRIHV TKTQKEWLII RSISIWTS
