ID A0A0V1LKT7_9BILA Unreviewed; 500 AA.
AC A0A0V1LKT7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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};
DE Flags: Fragment;
GN Name=MGAT2 {ECO:0000313|EMBL:KRZ60136.1};
GN ORFNames=T02_11193 {ECO:0000313|EMBL:KRZ60136.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60136.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ60136.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60136.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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:KRZ60136.1}.
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DR EMBL; JYDW01000032; KRZ60136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LKT7; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054721; 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: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; 1.
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, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 104..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 500
FT /evidence="ECO:0000313|EMBL:KRZ60136.1"
SQ SEQUENCE 500 AA; 57527 MW; 3CC529C9B597EC85 CRC64;
LVFNVLNISG VGGDCLTFRR CYSVGNIVGT WFGVAGDDGI LLSEACFRML SSRLLIKLLK
LTFTFFVLLV LVLKLKRGRG FNFEYSTTAN ADILFRPSQP PSALSKAGGF TTEQESPVPP
GSGGIEFVEA REPPLSPSVD EIRRIIRDNN VHADVLNENL FGPVENVSFV IVVQVHRRLN
YLRKLVESFE AAPFINRALV IFSHDYYDVE MNEFVRSIRF CRVMQIFYPD NVQISPYKFP
GQDPLDCARD IDKAQAQKEK CLNWDSPDRY GHYREASLTQ IKHHWWWKIN YVFDGIPRLK
NYSDWVLLLE EDHYVSPDFL YTFDYIVRNR DNLCKHCQVI TLGSYNQLNR RNTQPNALSV
MLWFSSHHNM GMAINRSTWN AIRSCGSNFC KYDDYNWDWS LLHVSRQCMN PPLSTIVVST
PRVFHIGDCG IHHKGQLCTV DSSANTVVTR LKDLKPQLFP QNFFLKLSNR RSPKLPAEYG
GWGDKRDHQL CMKNIIAQNV
//
