MGAT1_RAT
ID MGAT1_RAT Reviewed; 447 AA.
AC Q09325;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=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=Mgat1; Synonyms=Gnt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7764514; DOI=10.1271/bbb.58.200;
RA Fukada T., Iida K., Kioka N., Sakai H., Komano T.;
RT "Cloning of a cDNA encoding N-acetylglucosaminyltransferase I from rat
RT liver and analysis of its expression in rat tissues.";
RL Biosci. Biotechnol. Biochem. 58:200-201(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Initiates complex N-linked carbohydrate formation. Essential
CC for the conversion of high-mannose to hybrid and complex N-glycans.
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 -!- SUBUNIT: Interacts with MGAT4D. Interacts with BRI3 (By similarity).
CC {ECO:0000250|UniProtKB:P26572, ECO:0000250|UniProtKB:P27808}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P26572}. Note=Co-localizes with BRI3 at the
CC perinuclear region. {ECO:0000250|UniProtKB:P26572}.
CC -!- TISSUE SPECIFICITY: Appears to be present in all tissues.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC {ECO:0000305}.
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DR EMBL; D16302; BAA03807.1; -; mRNA.
DR EMBL; BC074010; AAH74010.1; -; mRNA.
DR PIR; JC2076; JC2076.
DR RefSeq; NP_110488.1; NM_030861.1.
DR RefSeq; XP_006246244.1; XM_006246182.3.
DR RefSeq; XP_006246245.1; XM_006246183.3.
DR RefSeq; XP_006246246.1; XM_006246184.3.
DR RefSeq; XP_006246247.1; XM_006246185.3.
DR RefSeq; XP_008765937.1; XM_008767715.2.
DR AlphaFoldDB; Q09325; -.
DR SMR; Q09325; -.
DR IntAct; Q09325; 1.
DR STRING; 10116.ENSRNOP00000044560; -.
DR CAZy; GT13; Glycosyltransferase Family 13.
DR iPTMnet; Q09325; -.
DR PhosphoSitePlus; Q09325; -.
DR jPOST; Q09325; -.
DR PaxDb; Q09325; -.
DR PRIDE; Q09325; -.
DR Ensembl; ENSRNOT00000052360; ENSRNOP00000044560; ENSRNOG00000068826.
DR Ensembl; ENSRNOT00000093956; ENSRNOP00000081587; ENSRNOG00000068826.
DR Ensembl; ENSRNOT00000100116; ENSRNOP00000083147; ENSRNOG00000068826.
DR Ensembl; ENSRNOT00000101283; ENSRNOP00000081858; ENSRNOG00000068826.
DR Ensembl; ENSRNOT00000106126; ENSRNOP00000090215; ENSRNOG00000068826.
DR Ensembl; ENSRNOT00000113892; ENSRNOP00000079270; ENSRNOG00000068826.
DR Ensembl; ENSRNOT00000116725; ENSRNOP00000082878; ENSRNOG00000068826.
DR GeneID; 81519; -.
DR KEGG; rno:81519; -.
DR UCSC; RGD:620097; rat.
DR CTD; 4245; -.
DR RGD; 620097; Mgat1.
DR eggNOG; KOG1413; Eukaryota.
DR GeneTree; ENSGT00530000063632; -.
DR HOGENOM; CLU_022150_0_0_1; -.
DR InParanoid; Q09325; -.
DR OMA; KGYDLSW; -.
DR OrthoDB; 1324622at2759; -.
DR PhylomeDB; Q09325; -.
DR TreeFam; TF320555; -.
DR Reactome; R-RNO-964739; N-glycan trimming and elongation in the cis-Golgi.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q09325; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000031208; Expressed in thymus and 19 other tissues.
DR Genevisible; Q09325; RN.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; ISO:RGD.
DR GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; ISO:RGD.
DR GO; GO:0030145; F:manganese ion binding; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:RGD.
DR GO; GO:0006049; P:UDP-N-acetylglucosamine catabolic process; ISO:RGD.
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; Glycosyltransferase; Golgi apparatus; Manganese;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..447
FT /note="Alpha-1,3-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000191386"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..447
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 291
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 115..145
FT /evidence="ECO:0000250"
FT DISULFID 239..305
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 51586 MW; 1AB54107072C53A2 CRC64;
MLKKQSAGLV LWGAIIFVGW NALLLLFFWT RPAPGRLPSD SALGDDPASL TREVIHLAED
AEAELERQRG LLQQIKEHYS LWRQRWRVPT VAPPAWPRVP GTPSPAVIPI LVIACDRSTV
RRCLDKLLHY RPSAEHFPII VSQDCGHEET AQVIASYGTA VTHIRQPDLS NIAVQPDHRK
FQGYYKIARH YRWALGQIFN KFKFPAAVVV EDDLEVAPDF FEYFQATYPL LKADPSLWCV
SAWNDNGKEQ MVDSSKPELL YRTDFFPGLG WLLLADLWAE LEPKWPKAFW DDWMRRPEQR
KGRACIRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY LQREAYDRDF
LAQVYGAPQL QVEKVRTNDR KELGEVRVQY TSRDSFKAFA KALGVMDDLK SGVPRAGYRG
IVTFQFRGRR VHLAPPETWN GYDPSWN
