MGAT2_PIG
ID MGAT2_PIG Reviewed; 446 AA.
AC O19071;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.143 {ECO:0000250|UniProtKB:Q10469};
DE AltName: Full=Beta-1,2-N-acetylglucosaminyltransferase II;
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 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 [GENOMIC DNA].
RC TISSUE=Brain, and Liver;
RX PubMed=9367162; DOI=10.1016/s0304-4165(97)00072-x;
RA Leeb T., Kriegesmann B., Baumgartner B., Klett C., Yerle M., Hameister H.,
RA Brenig B.;
RT "Molecular cloning of the porcine beta-1,2-N-acetylglucosaminyltransferase
RT II gene and assignment to chromosome 1q23-q27.";
RL Biochim. Biophys. Acta 1336:361-366(1997).
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:0000250|UniProtKB:Q10469}.
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:0000250|UniProtKB:Q10469};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q10469};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q10469}.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 16 (GT16) protein
CC family. {ECO:0000305}.
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DR EMBL; Y09537; CAA70732.1; -; Genomic_DNA.
DR RefSeq; NP_001121954.1; NM_001128482.1.
DR AlphaFoldDB; O19071; -.
DR SMR; O19071; -.
DR CAZy; GT16; Glycosyltransferase Family 16.
DR PaxDb; O19071; -.
DR PRIDE; O19071; -.
DR GeneID; 100151745; -.
DR KEGG; ssc:100151745; -.
DR CTD; 4247; -.
DR eggNOG; KOG2791; Eukaryota.
DR HOGENOM; CLU_032753_2_1_1; -.
DR InParanoid; O19071; -.
DR OrthoDB; 647764at2759; -.
DR TreeFam; TF314772; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; O19071; SS.
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; ISS:UniProtKB.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..446
FT /note="Alpha-1,6-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000080519"
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..446
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 123..127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 229..233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 261
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 374
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 196..210
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 283..286
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 334..357
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 339..439
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 378..386
FT /evidence="ECO:0000250|UniProtKB:Q10469"
SQ SEQUENCE 446 AA; 51527 MW; 9B03F1C20778D897 CRC64;
MRFRIYKRKV LILTFVVAAC GFVLWSSNGR QRKNEALAPP LLDAEPVRGA GARAGDHPAI
SVGIRRGSND SAAPLVAAAP QPEVDNLTLR YRSLVYQLNF DQTLRNVDKV SSWVPRELVL
VVQVHNRAEY LKLLLDSLRK AQGIDNVLVI FSHDFWSTEI NQLIAGVDFC PVLQVFFPFS
IQLYPNEFPG TDPRDCPRDL EKNAALKMGC INAEYPDSFG HYREAKFSQT KHHWWWKLHF
VWERVKVLRD YAGLILFLEE DHYVAPDFYH VFKKMWNLKQ QECPECDVLS LGTYTTVRSF
RDVADKVDVK TWKSTEHNMG LALTRDAYQK LIECTDTFCT YDDYNWDWTL QYLTVSCLPK
FWKVLVPQVP RIFHAGDCGM HHKKTCRPST QSAQIESLLN SNKQYMFPET LTISEKLTAA
LSPPRKNGGW GDIRDHELCK SYRRLQ
