MGAT2_RAT
ID MGAT2_RAT Reviewed; 442 AA.
AC Q09326;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.143 {ECO:0000269|PubMed:7797505};
DE AltName: Full=Beta-1,2-N-acetylglucosaminyltransferase II {ECO:0000303|PubMed:7797505};
DE AltName: Full=GlcNAc-T II;
DE Short=GNT-II;
DE AltName: Full=Mannoside acetylglucosaminyltransferase 2;
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II;
GN Name=Mgat2; Synonyms=Gnt2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7797505; DOI=10.1074/jbc.270.25.15211;
RA D'Agostaro G.A.F., Zingoni A., Moritz R.L., Simpson R.J., Schachter H.,
RA Bendiak B.;
RT "Molecular cloning and expression of cDNA encoding the rat UDP-N-
RT acetylglucosamine:alpha-6-D-mannoside beta-1,2-N-
RT acetylglucosaminyltransferase II.";
RL J. Biol. Chem. 270:15211-15221(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plays an essential role in protein N-glycosylation. Catalyzes
CC the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal
CC mannose moiety in the core structure of the nascent N-linked glycan
CC chain, giving rise to the second branch in complex glycans.
CC {ECO:0000269|PubMed:7797505}.
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)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-
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:12941,
CC Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC ChEBI:CHEBI:60651; EC=2.4.1.143;
CC Evidence={ECO:0000269|PubMed:7797505};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q10469};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:7797505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q10469}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q10469}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q10469}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Detected in
CC liver, brain, thymus and spleen. {ECO:0000269|PubMed:7797505}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 16 (GT16) protein
CC family. {ECO:0000305}.
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DR EMBL; U21662; AAA86721.1; -; mRNA.
DR EMBL; BC081754; AAH81754.1; -; mRNA.
DR PIR; A57044; A57044.
DR RefSeq; NP_446056.1; NM_053604.2.
DR AlphaFoldDB; Q09326; -.
DR SMR; Q09326; -.
DR STRING; 10116.ENSRNOP00000005608; -.
DR CAZy; GT16; Glycosyltransferase Family 16.
DR GlyGen; Q09326; 2 sites.
DR PaxDb; Q09326; -.
DR PRIDE; Q09326; -.
DR Ensembl; ENSRNOT00000005608; ENSRNOP00000005608; ENSRNOG00000004234.
DR GeneID; 94273; -.
DR KEGG; rno:94273; -.
DR UCSC; RGD:620098; rat.
DR CTD; 4247; -.
DR RGD; 620098; Mgat2.
DR eggNOG; KOG2791; Eukaryota.
DR GeneTree; ENSGT00390000007341; -.
DR HOGENOM; CLU_032753_2_1_1; -.
DR InParanoid; Q09326; -.
DR OMA; MHHKKTC; -.
DR OrthoDB; 647764at2759; -.
DR PhylomeDB; Q09326; -.
DR TreeFam; TF314772; -.
DR BRENDA; 2.4.1.143; 5301.
DR Reactome; R-RNO-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q09326; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004234; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q09326; RN.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008455; F:alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IPI:RGD.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:RGD.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR007754; GlcNAc_II.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12871; PTHR12871; 1.
DR Pfam; PF05060; MGAT2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..442
FT /note="Alpha-1,6-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000080520"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..442
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 118..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 224..228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 369
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 191..205
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 278..281
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 329..352
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 334..435
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 373..381
FT /evidence="ECO:0000250|UniProtKB:Q10469"
SQ SEQUENCE 442 AA; 51110 MW; 86A9C8210AA8B7C4 CRC64;
MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKNDALAPP LLDSEPLRGA GHFAASVGIR
RVSNDSAAPL VPAVPRPEVD NLTLRYRSLV YQLNFDQMLR NVDKDGTWSP GELVLVVQVH
NRPEYLRLLI DSLRKAQGIR EVLVIFSHDF WSAEINSLIS SVDFCPVLQV FFPFSIQLYP
SEFPGSDPRD CPRDLKKNAA LKLGCINAEY PDSFGHYREA KFSQTKHHWW WKLHFVWERV
KVLQDYTGLI LFLEEDHYLA PDFYHVFKKM WKLKQQECPG CDVLSLGTYT TIRSFYGIAD
KVDVKTWKST EHNMGLALTR DAYQKLIECT DTFCTYDDYN WDWTLQYLTL ACLPKVWKVL
VPQAPRIFHA GDCGMHHKKT CRPSTQSAQI ESLLNNNKQY LFPETLVIGE KFPMAAISPP
RKNGGWGDIR DHELCKSYRR LQ
