ID A0A1Y3BC50_EURMA Unreviewed; 238 AA.
AC A0A1Y3BC50;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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};
GN ORFNames=BLA29_002979 {ECO:0000313|EMBL:OTF77488.1};
OS Euroglyphus maynei (Mayne's house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF77488.1, ECO:0000313|Proteomes:UP000194236};
RN [1] {ECO:0000313|EMBL:OTF77488.1, ECO:0000313|Proteomes:UP000194236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF77488.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:OTF77488.1};
RA Arlian L.G., Morgan M.S., Rider S.D.;
RT "Genome Survey of Euroglyphus maynei.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTF77488.1}.
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DR EMBL; MUJZ01032309; OTF77488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3BC50; -.
DR OrthoDB; 3676111at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000194236; Unassembled WGS sequence.
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:InterPro.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000194236};
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 238 AA; 28635 MW; 1F5656C8F13F17F6 CRC64;
MEHLPQTRKH HGDFLFIEED HYVSPDLIHH WKLMKLAQKD LKESDTAIDI LTMGNYEFNV
QQKSIDNMQT EMTKLNLTNW FSSKHNMAFT IDRSLWSRIK SCQFAFCTFD DYNWDWSLQH
TIDECLKRKL RTLVTVVPRV FHTGTCGGLH HKQKHCDENS ETNKLKKFLA QNQEYQFIDQ
VRIEKHFGQY RKGIKNNGGW NDRRDHQLCQ QYQLPFLQIF HQNEHFYPLL KNDFLSEN
//
