MGAT1_CAEEL
ID MGAT1_CAEEL Reviewed; 449 AA.
AC Q11068; O76776;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.101;
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I;
DE Short=GNT-I;
DE Short=GlcNAc-T I;
GN Name=gly-13; ORFNames=B0416.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9867843; DOI=10.1074/jbc.274.1.288;
RA Chen S., Zhou S., Sarkar M., Spence A.M., Schachter H.;
RT "Expression of three Caenorhabditis elegans N-acetylglucosaminyltransferase
RT I genes during development.";
RL J. Biol. Chem. 274:288-297(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Initiates complex N-linked carbohydrate formation. Essential
CC for the conversion of high-mannose to hybrid and complex N-glycans (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC 5A1,2) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-
CC GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:11456,
CC Rhea:RHEA-COMP:14367, Rhea:RHEA-COMP:14368, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:59087,
CC ChEBI:CHEBI:60625; EC=2.4.1.101;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=The cofactor is mostly bound to the substrate. {ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P26572}; Single-pass type II membrane protein
CC {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P26572}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:9867843}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC {ECO:0000305}.
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DR EMBL; AF082010; AAD03022.1; -; mRNA.
DR EMBL; FO080200; CCD61925.1; -; Genomic_DNA.
DR PIR; T43340; T43340.
DR RefSeq; NP_509566.1; NM_077165.5.
DR AlphaFoldDB; Q11068; -.
DR SMR; Q11068; -.
DR BioGRID; 46076; 7.
DR STRING; 6239.B0416.6; -.
DR CAZy; GT13; Glycosyltransferase Family 13.
DR EPD; Q11068; -.
DR PaxDb; Q11068; -.
DR PeptideAtlas; Q11068; -.
DR PRIDE; Q11068; -.
DR EnsemblMetazoa; B0416.6.1; B0416.6.1; WBGene00001638.
DR GeneID; 181160; -.
DR KEGG; cel:CELE_B0416.6; -.
DR UCSC; B0416.6; c. elegans.
DR CTD; 181160; -.
DR WormBase; B0416.6; CE26434; WBGene00001638; gly-13.
DR eggNOG; KOG1413; Eukaryota.
DR GeneTree; ENSGT00530000063632; -.
DR HOGENOM; CLU_022150_0_1_1; -.
DR InParanoid; Q11068; -.
DR OMA; KGYDLSW; -.
DR OrthoDB; 1324622at2759; -.
DR PhylomeDB; Q11068; -.
DR BRENDA; 2.4.1.101; 1045.
DR Reactome; R-CEL-964739; N-glycan trimming and elongation in the cis-Golgi.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q11068; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001638; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005797; C:Golgi medial cisterna; ISS:WormBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; ISS:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:WormBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004139; Glyco_trans_13.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF03071; GNT-I; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..449
FT /note="Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000191388"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..449
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..131
FT /evidence="ECO:0000250"
FT DISULFID 227..293
FT /evidence="ECO:0000250"
SQ SEQUENCE 449 AA; 52151 MW; 8448210B2A78FC88 CRC64;
MHAVTKIFII FIFVFILWTL YVENDITNRT RNTDNIDDLL ESANRLERLL KFEAKKIAAL
AEDVHKIRAN RKGKHVIMEE MVSQDLKQWK DPIPVLVFSC NRAMAVRDHV EKLIRYRPSQ
EKFPIIVTQD CDNENVKNEV KKFGDKVEYI KHLAGDKANI TIPPSHRQYT AYYRIARHYK
LALNHVFVDK GYSSVIITED DLDISPDFFS YFSSTRYLLE NDEKLWCVTA WNDNGKQENI
DMTAASTLYR SDFFAGLGWM MSSKTWHELE PIWPVGFWDD WMRDPARRKD RQCIRPEISR
TGMMSYGKEG ASKGQFFSKH LAKIKVNDKY INFGKIDLDY LLPANFAKKT NLEVMKEAVE
LSIDNVASFV LSSENKGKSV RVMYDGNIDY IRKADKLHIM HDFKAGVPRT AYDGIVTCFI
NGIRIYLVPD RTKVSAYNPD WSVPPSFGE
