MGT4A_BOVIN
ID MGT4A_BOVIN Reviewed; 535 AA.
AC O77836;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A {ECO:0000250|UniProtKB:Q9UM21};
DE EC=2.4.1.145 {ECO:0000269|PubMed:9278430, ECO:0000269|PubMed:9565571};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 93-96; 161-168; 183-194;
RP 198-222; 230-251; 261-266; 326-331; 379-382; 387-425; 427-432; 434-448;
RP 454-463; 467-475 AND 484-491, GLYCOSYLATION AT ASN-458, MUTAGENESIS OF
RP SER-79 AND THR-460, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC TISSUE=Small intestine;
RX PubMed=9565571; DOI=10.1074/jbc.273.19.11556;
RA Minowa M.T., Oguri S., Yoshida A., Hara T., Iwamatsu A., Ikenaga H.,
RA Takeuchi M.;
RT "cDNA cloning and expression of bovine UDP-N-acetylglucosamine: alpha1, 3-
RT D-mannoside beta1,4-N-acetylglucosaminyltransferase IV.";
RL J. Biol. Chem. 273:11556-11562(1998).
RN [2]
RP IDENTIFICATION, COFACTOR, CATALYTIC ACTIVITY, FUNCTION, PATHWAY,
RP GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=9278430; DOI=10.1074/jbc.272.36.22721;
RA Oguri S., Minowa M.T., Ihara Y., Taniguchi N., Ikenaga H., Takeuchi M.;
RT "Purification and characterization of UDP-N-acetylglucosamine: alpha1,3-D-
RT mannoside beta1,4-N-acetylglucosaminyltransferase (N-
RT acetylglucosaminyltransferase-IV) from bovine small intestine.";
RL J. Biol. Chem. 272:22721-22727(1997).
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
CC (PubMed:9278430, PubMed:9565571). Involved in glucose transport by
CC mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface
CC expression of SLC2A2 in pancreatic beta cells (By similarity).
CC {ECO:0000250|UniProtKB:Q812G0, ECO:0000269|PubMed:9278430,
CC ECO:0000269|PubMed:9565571}.
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:0000269|PubMed:9278430,
CC ECO:0000269|PubMed:9565571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058;
CC Evidence={ECO:0000269|PubMed:9278430, ECO:0000305|PubMed:9565571};
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:0000269|PubMed:9278430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69616;
CC Evidence={ECO:0000269|PubMed:9278430};
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:0000269|PubMed:9278430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69620;
CC Evidence={ECO:0000269|PubMed:9278430};
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:0000269|PubMed:9278430};
CC -!- ACTIVITY REGULATION: Inhibited by UDP. {ECO:0000269|PubMed:9278430}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.73 mM for Gn2(2',2)core-PA {ECO:0000269|PubMed:9278430};
CC KM=0.13 mM for Gn2(29,2)core-PAGn3(6',2',2)core-PA
CC {ECO:0000269|PubMed:9278430};
CC KM=0.22 mM for UDP-N-acetyl-alpha-D-glucosamine (with 0.8 mM
CC Gn2(2',2)core-PA as an acceptor) {ECO:0000269|PubMed:9278430};
CC pH dependence:
CC Optimum pH is 7.3. {ECO:0000269|PubMed:9278430};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:9278430, ECO:0000269|PubMed:9565571}.
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:0000305|PubMed:9565571}.
CC -!- TISSUE SPECIFICITY: Highly expressed in small intestine, kidney, lung
CC and spleen. Weakly expressed in brain, heart and liver.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9278430}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
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DR EMBL; AB000628; BAA31162.1; -; mRNA.
DR RefSeq; NP_803486.1; NM_177520.3.
DR AlphaFoldDB; O77836; -.
DR SMR; O77836; -.
DR STRING; 9913.ENSBTAP00000013715; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR iPTMnet; O77836; -.
DR PaxDb; O77836; -.
DR Ensembl; ENSBTAT00000013715; ENSBTAP00000013715; ENSBTAG00000010388.
DR GeneID; 282276; -.
DR KEGG; bta:282276; -.
DR CTD; 11320; -.
DR VEuPathDB; HostDB:ENSBTAG00000010388; -.
DR VGNC; VGNC:96699; MGAT4A.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR GeneTree; ENSGT00940000159177; -.
DR InParanoid; O77836; -.
DR OMA; ERIRWRT; -.
DR OrthoDB; 593094at2759; -.
DR BRENDA; 2.4.1.145; 908.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000010388; Expressed in spiral colon and 110 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
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; IDA: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; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR006759; Glyco_transf_54.
DR PANTHER; PTHR12062; PTHR12062; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..535
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase A"
FT /id="PRO_0000288579"
FT CHAIN 93..535
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase A soluble form"
FT /evidence="ECO:0000269|PubMed:9565571"
FT /id="PRO_0000288580"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..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 31..57
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:0000269|PubMed:9565571"
FT MUTAGEN 79
FT /note="S->A: Does not abolish enzyme activity."
FT /evidence="ECO:0000269|PubMed:9565571"
FT MUTAGEN 460
FT /note="T->A: Does not abolish enzyme activity."
FT /evidence="ECO:0000269|PubMed:9565571"
SQ SEQUENCE 535 AA; 61618 MW; 614C1AA3B536BB5D CRC64;
MRLRNGTVAT VLAFITSFLT LSWYTTWQNG KEKVIAYQRE FLALKERLRI AEHRISQRSS
ELSAIVQQFK RVEAETNRSK DPVNKFSDDT LKILKELTSK KSLQVPSIYY HLPHLLQNEG
SLQPAVQIGN GRTGVSIVMG IPTVKREVKS YLIETLHSLI DNLYPEEKLD CVIVVFIGET
DTDYVNGVVA NLEKEFSKEI SSGLVEIISP PESYYPDLTN LKETFGDSKE RVRWRTKQNL
DYCFLMMYAQ EKGTYYIQLE DDIIVKQNYF NTIKNFALQL SSEEWMILEF SQLGFIGKMF
QAPDLTLIVE FIFMFYKEKP IDWLLDHILW VKVCNPEKDA KHCDRQKANL RIRFRPSLFQ
HVGLHSSLTG KIQKLTDKDY MKPLLLKIHV NPPAEVSTSL KVYQGHTLEK TYMGEDFFWA
ITPVAGDYIL FKFDKPVNVE SYLFHSGNQD HPGDILLNTT VEVLPLKSEG LDISKETKDK
RLEDGYFRIG KFENGVAEGM VDPSLNPISA FRLSVIQNSA VWAILNEIHI KKVTN
