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   24-JAN-2024, entry version 120.
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   STRING; 9823.ENSSSCP00000063762; -.
DR   CAZy; GT16; Glycosyltransferase Family 16.
DR   GlyCosmos; O19071; 2 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000005385; -.
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; 3676111at2759; -.
DR   TreeFam; TF314772; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0005795; C:Golgi stack; IEA:InterPro.
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   InterPro; IPR007754; GlcNAc_II.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR12871:SF0; ALPHA-1,6-MANNOSYL-GLYCOPROTEIN 2-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR12871; BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE II; 1.
DR   Pfam; PF05060; MGAT2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; O19071; SS.
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
//