MGAT2_MOUSE
ID MGAT2_MOUSE Reviewed; 442 AA.
AC Q921V5; Q3U6X4; Q8C3Z6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.143 {ECO:0000250|UniProtKB:Q10469};
DE AltName: Full=Beta-1,2-N-acetylglucosaminyltransferase II;
DE AltName: Full=GlcNAc-T II;
DE Short=GNT-II;
DE AltName: Full=Mannoside acetylglucosaminyltransferase 2;
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II;
GN Name=Mgat2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=11805078; DOI=10.1093/glycob/11.12.1051;
RA Wang Y., Tan J., Sutton-Smith M., Ditto D., Panico M., Campbell R.M.,
RA Varki N.M., Long J.M., Jaeken J., Levinson S.R., Wynshaw-Boris A.,
RA Morris H.R., Le D., Dell A., Schachter H., Marth J.D.;
RT "Modeling human congenital disorder of glycosylation type IIa in the mouse:
RT conservation of asparagine-linked glycan-dependent functions in mammalian
RT physiology and insights into disease pathogenesis.";
RL Glycobiology 11:1051-1070(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, and Testis;
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).
CC -!- FUNCTION: Plays an essential role in protein N-glycosylation. Catalyzes
CC the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal
CC mannose moiety in the core structure of the nascent N-linked glycan
CC chain, giving rise to the second branch in complex glycans.
CC {ECO:0000269|PubMed:11805078}.
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:0000250|UniProtKB:Q10469};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q10469};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q10469}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q10469}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q10469}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q10469}.
CC -!- TISSUE SPECIFICITY: Detected in liver, lung, testis, kidney, brain,
CC spleen, thymus, uterus and intestine. {ECO:0000269|PubMed:11805078}.
CC -!- DISRUPTION PHENOTYPE: Decreased embryonic survival between 9 and 15
CC dpc. Surviving embryos are about 20% smaller than their littermates by
CC 15 dpc. Most of the newborn pups die during the first week after birth,
CC and none live longer than 4 weeks. Pups are about half the size of
CC their littermates 8 days after birth, have dismorphic facial features
CC and severe locomotor deficits. Pups display impaired muscle development
CC and defects in bone development including a hunched spinal column, plus
CC poorly calcified and brittle bones in vertebrae, ribs, femur and skull.
CC Mutant mice have also mild anemia and impaired mucus production in the
CC gastrointestinal system. Outcrossing increases the length of the
CC lifespan, but does not increase the number of pups that survive after
CC the fist week. Surviving males display testicular atrophy and are
CC infertile. About one third of the surviving females produce offspring,
CC but do not nurture their pups. {ECO:0000269|PubMed:11805078}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 16 (GT16) protein
CC family. {ECO:0000305}.
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DR EMBL; AK083370; BAC38888.1; -; mRNA.
DR EMBL; AK152925; BAE31600.1; -; mRNA.
DR EMBL; BC010583; AAH10583.1; -; mRNA.
DR EMBL; BC027169; AAH27169.1; -; mRNA.
DR CCDS; CCDS25947.1; -.
DR RefSeq; NP_666147.1; NM_146035.2.
DR AlphaFoldDB; Q921V5; -.
DR SMR; Q921V5; -.
DR BioGRID; 229940; 2.
DR STRING; 10090.ENSMUSP00000057905; -.
DR BindingDB; Q921V5; -.
DR ChEMBL; CHEMBL2375203; -.
DR CAZy; GT16; Glycosyltransferase Family 16.
DR GlyGen; Q921V5; 2 sites.
DR PhosphoSitePlus; Q921V5; -.
DR EPD; Q921V5; -.
DR MaxQB; Q921V5; -.
DR PaxDb; Q921V5; -.
DR PRIDE; Q921V5; -.
DR ProteomicsDB; 295563; -.
DR Antibodypedia; 10266; 161 antibodies from 23 providers.
DR DNASU; 217664; -.
DR Ensembl; ENSMUST00000060579; ENSMUSP00000057905; ENSMUSG00000043998.
DR GeneID; 217664; -.
DR KEGG; mmu:217664; -.
DR UCSC; uc011ymy.1; mouse.
DR CTD; 4247; -.
DR MGI; MGI:2384966; Mgat2.
DR VEuPathDB; HostDB:ENSMUSG00000043998; -.
DR eggNOG; KOG2791; Eukaryota.
DR GeneTree; ENSGT00390000007341; -.
DR HOGENOM; CLU_032753_2_1_1; -.
DR InParanoid; Q921V5; -.
DR OMA; MHHKKTC; -.
DR OrthoDB; 647764at2759; -.
DR PhylomeDB; Q921V5; -.
DR TreeFam; TF314772; -.
DR Reactome; R-MMU-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 217664; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Mgat2; mouse.
DR PRO; PR:Q921V5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q921V5; protein.
DR Bgee; ENSMUSG00000043998; Expressed in parotid gland and 263 other tissues.
DR Genevisible; Q921V5; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008455; F:alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IMP:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:MGI.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR007754; GlcNAc_II.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12871; PTHR12871; 1.
DR Pfam; PF05060; MGAT2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..442
FT /note="Alpha-1,6-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000080518"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..442
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 118..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 224..228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 369
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 191..205
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 278..281
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 329..352
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 334..435
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 373..381
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT CONFLICT 9
FT /note="K -> E (in Ref. 1; BAC38888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 51030 MW; E32D078C4F209843 CRC64;
MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKSDALGPP LLDAEPVRGA GHLAVSVGIR
RVSNESAAPL VPAVPRPEVD NLTLRYRSLV YQLNFDQMLR NVGNDGTWSP GELVLVVQVH
NRPEYLRLLI DSLRKAQGIQ EVLVIFSHDF WSAEINSLIS RVDFCPVLQV FFPFSIQLYP
NEFPGSDPRD CPRDLKKNAA LKLGCINAEY PDSFGHYREA KFSQTKHHWW WKLHFVWERV
KVLQDYTGLI LFLEEDHYLA PDFYHVFKKM WKLKQQECPG CDVLSLGTYT TIRSFYGIAD
KVDVKTWKST EHNMGLALTR DAYQKLIECT DTFCTYDDYN WDWTLQYLTL ACLPKIWKVL
VPQAPRIFHA GDCGMHHKKT CRPSTQSAQI ESLLNSNKQY LFPETLVIGE KFPMAAISPP
RKNGGWGDIR DHELCKSYRR LQ
