MGAT1_MOUSE
ID MGAT1_MOUSE Reviewed; 447 AA.
AC P27808;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.101 {ECO:0000269|PubMed:1421759};
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1533386; DOI=10.1016/0888-7543(92)90297-6;
RA Pownall S., Kozak C.A., Schappert K.T., Sarkar M., Hull E., Schachter H.,
RA Math J.D.;
RT "Molecular cloning and characterization of the mouse UDP-N-
RT acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-
RT acetylglucosaminyltransferase I gene.";
RL Genomics 12:699-704(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=1421759; DOI=10.1093/glycob/2.4.383;
RA Kumar R., Yang J., Eddy R.L., Byers M.G., Shows T.B., Stanley P.;
RT "Cloning and expression of the murine gene and chromosomal location of the
RT human gene encoding N-acetylglucosaminyltransferase I.";
RL Glycobiology 2:383-393(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH MGAT4D.
RX PubMed=20805325; DOI=10.1083/jcb.201004102;
RA Huang H.H., Stanley P.;
RT "A testis-specific regulator of complex and hybrid N-glycan synthesis.";
RL J. Cell Biol. 190:893-910(2010).
CC -!- FUNCTION: Initiates complex N-linked carbohydrate formation. Essential
CC for the conversion of high-mannose to hybrid and complex N-glycans.
CC {ECO:0000269|PubMed:1421759}.
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 Evidence={ECO:0000269|PubMed:1421759};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P26572};
CC Note=The cofactor is mostly bound to the substrate.
CC {ECO:0000250|UniProtKB:P27115};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:1421759}.
CC -!- SUBUNIT: Interacts with MGAT4D. Interacts with BRI3 (By similarity).
CC {ECO:0000250|UniProtKB:P26572, ECO:0000269|PubMed:20805325}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P26572}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P26572}. 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: Detected in kidney, liver and brain.
CC {ECO:0000269|PubMed:1533386}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=alpha-
CC 1,3-mannosyl-glycoprotein beta 1,2-GlcNAc T I (Mgat1);
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_583";
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DR EMBL; M73491; AAA37698.1; -; Genomic_DNA.
DR EMBL; L07037; AAA40478.1; -; mRNA.
DR EMBL; AK087959; BAC40058.1; -; mRNA.
DR EMBL; BC006629; AAH06629.1; -; mRNA.
DR CCDS; CCDS24602.1; -.
DR PIR; A42500; A42500.
DR RefSeq; NP_001103618.1; NM_001110148.1.
DR RefSeq; NP_001103619.1; NM_001110149.1.
DR RefSeq; NP_001103620.1; NM_001110150.1.
DR RefSeq; NP_034924.3; NM_010794.3.
DR RefSeq; XP_006532460.1; XM_006532397.3.
DR RefSeq; XP_006532461.1; XM_006532398.3.
DR RefSeq; XP_006532462.1; XM_006532399.2.
DR RefSeq; XP_006532463.1; XM_006532400.3.
DR RefSeq; XP_017169803.1; XM_017314314.1.
DR AlphaFoldDB; P27808; -.
DR SMR; P27808; -.
DR BioGRID; 201410; 3.
DR STRING; 10090.ENSMUSP00000080484; -.
DR ChEMBL; CHEMBL4524036; -.
DR CAZy; GT13; Glycosyltransferase Family 13.
DR iPTMnet; P27808; -.
DR PhosphoSitePlus; P27808; -.
DR EPD; P27808; -.
DR PaxDb; P27808; -.
DR PeptideAtlas; P27808; -.
DR PRIDE; P27808; -.
DR ProteomicsDB; 292316; -.
DR Antibodypedia; 17878; 281 antibodies from 32 providers.
DR DNASU; 17308; -.
DR Ensembl; ENSMUST00000081794; ENSMUSP00000080484; ENSMUSG00000020346.
DR Ensembl; ENSMUST00000101293; ENSMUSP00000098851; ENSMUSG00000020346.
DR Ensembl; ENSMUST00000109194; ENSMUSP00000104817; ENSMUSG00000020346.
DR Ensembl; ENSMUST00000167400; ENSMUSP00000126303; ENSMUSG00000020346.
DR GeneID; 17308; -.
DR KEGG; mmu:17308; -.
DR UCSC; uc007iqb.2; mouse.
DR CTD; 4245; -.
DR MGI; MGI:96973; Mgat1.
DR VEuPathDB; HostDB:ENSMUSG00000020346; -.
DR eggNOG; KOG1413; Eukaryota.
DR GeneTree; ENSGT00530000063632; -.
DR HOGENOM; CLU_022150_0_0_1; -.
DR InParanoid; P27808; -.
DR OMA; KGYDLSW; -.
DR OrthoDB; 1324622at2759; -.
DR PhylomeDB; P27808; -.
DR TreeFam; TF320555; -.
DR Reactome; R-MMU-964739; N-glycan trimming and elongation in the cis-Golgi.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 17308; 23 hits in 69 CRISPR screens.
DR ChiTaRS; Mgat1; mouse.
DR PRO; PR:P27808; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P27808; protein.
DR Bgee; ENSMUSG00000020346; Expressed in retinal neural layer and 247 other tissues.
DR ExpressionAtlas; P27808; baseline and differential.
DR Genevisible; P27808; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
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; IDA:MGI.
DR GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
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; ISS:UniProtKB.
DR GO; GO:0006049; P:UDP-N-acetylglucosamine catabolic process; IDA:MGI.
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 1: Evidence at protein 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_0000191385"
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|UniProtKB:P27115"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT DISULFID 115..145
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT DISULFID 239..305
FT /evidence="ECO:0000250|UniProtKB:P27115"
SQ SEQUENCE 447 AA; 51690 MW; E7C65EA8C8B34E6A CRC64;
MLKKQTAGLV LWGAIIFVGW NALLLLFFWT RPAPGRLPSD SALGDDPASL TREVIHLAED
AEAELERQRG LLQQIKEHYA LWRQRWRVPT VAPPAWPRVP VTPSPVQIPI LVIACDRSTV
RRCLDKLLHY RPSAERFPII VSQDCGHEET AQVIASYGTA VTHIRQPDLS NIAVQPDHRK
FQGYYKIARH YRWALGQIFN KFKFPAAVVV EDDLEVAPDF FEYFQATYPL LRTDPSLWCV
SAWNDNGKEQ MVDSSKPELL YRTDFFPGLG WLLLADLWAE LEPKWPKAFW DDWMRRPEQR
KGRACIRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY LQQEAYDRDF
LAQVYGAPQL QVEKVRTNDQ KELGEVRVQY TSRDSFKAFA KALGVMDDLK SGVPRAGYRG
IVTFQFRGRR VHLAPPQTWT GYDPSWN
