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   24-JAN-2024, entry version 149.
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   GlyCosmos; Q921V5; 2 sites, No reported glycans.
DR   GlyGen; Q921V5; 2 sites.
DR   PhosphoSitePlus; Q921V5; -.
DR   EPD; Q921V5; -.
DR   MaxQB; Q921V5; -.
DR   PaxDb; 10090-ENSMUSP00000057905; -.
DR   ProteomicsDB; 295563; -.
DR   Pumba; Q921V5; -.
DR   Antibodypedia; 10266; 172 antibodies from 23 providers.
DR   DNASU; 217664; -.
DR   Ensembl; ENSMUST00000060579.10; ENSMUSP00000057905.9; ENSMUSG00000043998.11.
DR   GeneID; 217664; -.
DR   KEGG; mmu:217664; -.
DR   UCSC; uc011ymy.1; mouse.
DR   AGR; MGI:2384966; -.
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; 3676111at2759; -.
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 78 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 267 other cell types or tissues.
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: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; IBA:GO_Central.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:MGI.
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.
DR   Genevisible; Q921V5; MM.
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
//