MGT4A_PONAB
ID MGT4A_PONAB Reviewed; 535 AA.
AC Q5REP8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A {ECO:0000250|UniProtKB:Q9UM21};
DE EC=2.4.1.145 {ECO:0000250|UniProtKB:O77836};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa;
DE Short=GlcNAc-T IVa;
DE Short=GnT-IVa;
DE Short=N-acetylglucosaminyltransferase IVa;
DE AltName: Full=UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa;
DE Contains:
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form;
GN Name=MGAT4A {ECO:0000250|UniProtKB:Q9UM21};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from
CC UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of
CC N-linked glycans through a beta1-4 linkage and participates in the
CC production of tri- and tetra-antennary N-linked sugar chains (By
CC similarity). Involved in glucose transport by mediating SLC2A2/GLUT2
CC glycosylation, thereby controlling cell-surface expression of SLC2A2 in
CC pancreatic beta cells (By similarity). {ECO:0000250|UniProtKB:O77836,
CC ECO:0000250|UniProtKB:Q812G0}.
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; Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-
CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69615,
CC Rhea:RHEA-COMP:14369, Rhea:RHEA-COMP:17732, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC ChEBI:CHEBI:187873; Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69616;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-
CC GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69619, Rhea:RHEA-COMP:17733, Rhea:RHEA-COMP:17734,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187874, ChEBI:CHEBI:187875;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69620;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-D-Fuc-(1->6)]-
CC beta-D-GlcNAc}-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)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-[alpha-D-Fuc-(1->6)]-beta-D-GlcNAc}-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:69623, Rhea:RHEA-COMP:17735,
CC Rhea:RHEA-COMP:17736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:187876, ChEBI:CHEBI:187877;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69624;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-Gal-(1->4)-beta-D-
CC GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-
CC GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69627, Rhea:RHEA-COMP:17737, Rhea:RHEA-COMP:17738,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187878, ChEBI:CHEBI:187879;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69628;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man-
CC (1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69631,
CC Rhea:RHEA-COMP:17739, Rhea:RHEA-COMP:17740, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187880,
CC ChEBI:CHEBI:187881; Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69632;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-
CC [beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69635, Rhea:RHEA-COMP:17741, Rhea:RHEA-COMP:17742,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187882, ChEBI:CHEBI:187883;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69636;
CC Evidence={ECO:0000250|UniProtKB:Q9UM21};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:O77836};
CC -!- ACTIVITY REGULATION: Inhibited by UDP. {ECO:0000250|UniProtKB:O77836}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:O77836}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9D4R2}.
CC -!- SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
CC acetylglucosaminyltransferase A soluble form]: Secreted
CC {ECO:0000250|UniProtKB:O77836}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O77836}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
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DR EMBL; CR857472; CAH89759.1; -; mRNA.
DR RefSeq; NP_001128986.1; NM_001135514.1.
DR AlphaFoldDB; Q5REP8; -.
DR SMR; Q5REP8; -.
DR STRING; 9601.ENSPPYP00000013476; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GeneID; 100190826; -.
DR KEGG; pon:100190826; -.
DR CTD; 11320; -.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR InParanoid; Q5REP8; -.
DR OrthoDB; 593094at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0008454; F:alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0046487; P:glyoxylate metabolic process; ISS:UniProtKB.
DR GO; GO:0006491; P:N-glycan processing; ISS:UniProtKB.
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 Coiled coil; Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..535
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase A"
FT /id="PRO_0000288587"
FT CHAIN 93..535
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase A soluble form"
FT /evidence="ECO:0000250|UniProtKB:O77836"
FT /id="PRO_0000288588"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..535
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 28..63
FT /evidence="ECO:0000255"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UM21"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 535 AA; 61525 MW; 6ECC0A0923BA8877 CRC64;
MRLRNGTVAT ALAFITSFLT LSWYTTWQNG KEKLIAYQRE FLALKERLRI AEHRISQRSS
ELNTIVQQFK RVGAETNGSK DALNKFSDNT LKLLKELTSK KSLQVPSIYY HLPHLLKNEG
SLQPAVQIGN GRTGVSIVMG IPTVKREVKS YLIETLHSLI DNLYPEEKLD CVIVVFIGET
DIDYVHGVVA NLEKEFSKEI SSGLVEVISP PESYYPDLTN LKETFGDSKE RVRWRTKQNL
DYCFLMMYAQ EKGIYYIQLE DDIIVKQNYF NTIKNFALQL SSEEWMILEF SQLGFIGKMF
QAPDLTLIVE FIFMFYKEKP IDWLLDHILW VKVCNPEKDA KHCDRQKANL RIHFRPSLFQ
HVGLHSSLSG KIQKLTDKDY MKPLLLKIHV NPPAEVSTSL KVYQGHTLEK TYMGEDFFWA
ITPIAGDYIL FKFDKPVNVE SYLFHSGNQE HPGDILLNTT VEVLPFKSEG LEISKETKDK
RLEDGYFRIG KFENGVAEGM VDPSLNPISA FRLSVIQNSA VWAILNEIHI KKATN
