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Database: UniProt
Entry: A0A1I8HL31_9PLAT
LinkDB: A0A1I8HL31_9PLAT
Original site: A0A1I8HL31_9PLAT 
ID   A0A1I8HL31_9PLAT        Unreviewed;       430 AA.
AC   A0A1I8HL31;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00014817};
DE            EC=2.4.1.143 {ECO:0000256|ARBA:ARBA00012613};
DE   AltName: Full=Beta-1,2-N-acetylglucosaminyltransferase II {ECO:0000256|ARBA:ARBA00032915};
DE   AltName: Full=GlcNAc-T II {ECO:0000256|ARBA:ARBA00032552};
DE   AltName: Full=Mannoside acetylglucosaminyltransferase 2 {ECO:0000256|ARBA:ARBA00031203};
DE   AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II {ECO:0000256|ARBA:ARBA00029663};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0006799-snap-gene-0.6-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0006799-snap-gene-0.6-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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:0000256|ARBA:ARBA00000406};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 16 (GT16) protein
CC       family. {ECO:0000256|ARBA:ARBA00011011}.
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DR   AlphaFoldDB; A0A1I8HL31; -.
DR   WBParaSite; maker-uti_cns_0006799-snap-gene-0.6-mRNA-1; maker-uti_cns_0006799-snap-gene-0.6-mRNA-1; maker-uti_cns_0006799-snap-gene-0.6.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IEA:InterPro.
DR   GO; GO:0008455; F:alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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; 2.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   430 AA;  49809 MW;  D10013E37BD207B5 CRC64;
     LTQQLQQPLL LTRTPFNFTP VEDPLPLIYS LQNANATAIL DAMLAINAEH EILNAQFYNG
     PITEVIVVQV HDRIGYLYLL IDSLRRVKDV EDCLLVFSHD VYSSAINALV RSIRFARVLQ
     QLLFILIIDQ LPKLQSLVTL NSPLQIFYPY TKQIYFDRFP GNDPRDCPRD AGLYRARQLG
     CNNAEWPDKY GHYRESKYTQ TKHHWLYKMN RLFERSPVLA NFTGQFVFLE EDHYVVEDLL
     HMLRLMVAAR KDLSQNVEIL TLGTYEKKPD FTRNTAQVVV DKWVSSFHNM GMSFSRAIWD
     QIKPCLPAFC SFDDYNWDWS LNHILTKCTK RPFQTMVIRI SPRVFHIGQC GVHHKNKVCN
     PALLSSKLDR MLANNIAKLY PDQLMFNAKL KIRARALKPN GGWGDLRDRR LCSSFFNSSE
     SPPSGLPYGM
//
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