MGT5B_MOUSE
ID MGT5B_MOUSE Reviewed; 792 AA.
AC Q765H6; Q8C7T8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B;
DE EC=2.4.1.-;
DE EC=2.4.1.155 {ECO:0000250|UniProtKB:Q3V5L5};
DE AltName: Full=Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase B;
DE AltName: Full=GlcNAc-T Vb;
DE Short=GNT-Vb {ECO:0000303|PubMed:14623122};
DE AltName: Full=Mannoside acetylglucosaminyltransferase 5B;
DE AltName: Full=N-acetylglucosaminyl-transferase Vb;
DE AltName: Full=N-acetylglucosaminyltransferase IX;
DE Short=GNT-IX {ECO:0000303|PubMed:16413118};
GN Name=Mgat5b;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14623122; DOI=10.1016/s0014-5793(03)01234-1;
RA Kaneko M., Alvarez-Manilla G., Kamar M., Lee I., Lee J.-K., Troupe K.,
RA Zhang W., Osawa M., Pierce M.;
RT "A novel beta(1,6)-N-acetylglucosaminyltransferase V (GnT-VB).";
RL FEBS Lett. 554:515-519(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=16413118; DOI=10.1016/j.bbagen.2005.11.019;
RA Inamori K., Mita S., Gu J., Mizuno-Horikawa Y., Miyoshi E., Dennis J.W.,
RA Taniguchi N.;
RT "Demonstration of the expression and the enzymatic activity of N-
RT acetylglucosaminyltransferase IX in the mouse brain.";
RL Biochim. Biophys. Acta 1760:678-684(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=22715095; DOI=10.1074/jbc.m112.367565;
RA Lee J.K., Matthews R.T., Lim J.M., Swanier K., Wells L., Pierce J.M.;
RT "Developmental expression of the neuron-specific N-
RT acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in
RT vivo glycan products in comparison with those of its paralog, GnT-V.";
RL J. Biol. Chem. 287:28526-28536(2012).
CC -!- FUNCTION: Glycosyltransferase that acts on alpha-linked mannose of N-
CC glycans and O-mannosyl glycans. Catalyzes the transfer of N-
CC acetylglucosamine (GlcNAc) to the beta 1-6 linkage of the mannose
CC residue of GlcNAc-beta1,2-Man-alpha on both the alpha1,3- and alpha1,6-
CC linked mannose arms in the core structure of N-glycan (By similarity).
CC Also acts on the GlcNAc-beta1,2-Man-alpha1-Ser/Thr moiety, forming a
CC 2,6-branched structure in brain O-mannosyl glycan (PubMed:22715095).
CC Plays an active role in modulating integrin and laminin-dependent
CC adhesion and migration of neuronal cells via its activity in the O-
CC mannosyl glycan pathway. {ECO:0000250|UniProtKB:Q3V5L5,
CC ECO:0000269|PubMed:22715095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-
CC GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-
CC (1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:16921, Rhea:RHEA-COMP:14374, Rhea:RHEA-COMP:14377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139507, ChEBI:CHEBI:139510; EC=2.4.1.155;
CC Evidence={ECO:0000250|UniProtKB:Q3V5L5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl]-L-
CC seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + O(3)-{N-
CC acetyl-beta-D-glucosaminyl-(1->2)-[N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-alpha-D-mannosyl}-L-seryl-[protein] + UDP;
CC Xref=Rhea:RHEA:56252, Rhea:RHEA-COMP:14438, Rhea:RHEA-COMP:14440,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:140080, ChEBI:CHEBI:140085;
CC Evidence={ECO:0000250|UniProtKB:Q3V5L5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl]-L-
CC threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC O(3)-{N-acetyl-beta-D-glucosaminyl-(1->2)-[N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-alpha-D-mannosyl}-L-threonyl-[protein] + UDP;
CC Xref=Rhea:RHEA:56256, Rhea:RHEA-COMP:14439, Rhea:RHEA-COMP:14441,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:140083, ChEBI:CHEBI:140087;
CC Evidence={ECO:0000250|UniProtKB:Q3V5L5};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q3V5L5};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:22715095}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16413118}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16413118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q765H6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q765H6-2; Sequence=VSP_025736, VSP_025737, VSP_025738;
CC -!- TISSUE SPECIFICITY: Present in brain (at protein level)
CC (PubMed:16413118). Predominantly expressed in hippocampus, superficial
CC layers of the brain cortex, striatum, nucleus accumbens, a subset of
CC nuclei in the thalamus, inferior colliculus, brain stem and cerebellum
CC (PubMed:16413118, PubMed:22715095). {ECO:0000269|PubMed:16413118,
CC ECO:0000269|PubMed:22715095}.
CC -!- DISRUPTION PHENOTYPE: Brains from mutant mice display defective
CC biosynthesis of O-mannosyl glycans (PubMed:22715095). Mutant mice that
CC lack both Mgat5 and Mgat5b display no visible changes in brain anatomy,
CC but their brains display defective biosynthesis of both O-mannosyl
CC glycans and N-linked glycans (PubMed:22715095).
CC {ECO:0000269|PubMed:22715095}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 18 family.
CC {ECO:0000305}.
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DR EMBL; AB116028; BAD08454.1; -; mRNA.
DR EMBL; AB119127; BAC87707.1; -; mRNA.
DR EMBL; AK049266; BAC33645.1; -; mRNA.
DR EMBL; AL627205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094604; AAH94604.1; -; mRNA.
DR CCDS; CCDS25682.1; -. [Q765H6-1]
DR RefSeq; NP_766536.2; NM_172948.3. [Q765H6-1]
DR AlphaFoldDB; Q765H6; -.
DR SMR; Q765H6; -.
DR BioGRID; 234512; 3.
DR STRING; 10090.ENSMUSP00000099316; -.
DR CAZy; GT18; Glycosyltransferase Family 18.
DR GlyConnect; 2120; 1 N-Linked glycan (1 site).
DR GlyGen; Q765H6; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q765H6; -.
DR PhosphoSitePlus; Q765H6; -.
DR MaxQB; Q765H6; -.
DR PaxDb; Q765H6; -.
DR PRIDE; Q765H6; -.
DR ProteomicsDB; 290229; -. [Q765H6-1]
DR ProteomicsDB; 290230; -. [Q765H6-2]
DR Antibodypedia; 46175; 61 antibodies from 18 providers.
DR DNASU; 268510; -.
DR Ensembl; ENSMUST00000103027; ENSMUSP00000099316; ENSMUSG00000043857. [Q765H6-1]
DR GeneID; 268510; -.
DR KEGG; mmu:268510; -.
DR UCSC; uc007mmu.1; mouse. [Q765H6-1]
DR UCSC; uc007mmv.1; mouse. [Q765H6-2]
DR CTD; 146664; -.
DR MGI; MGI:3606200; Mgat5b.
DR VEuPathDB; HostDB:ENSMUSG00000043857; -.
DR eggNOG; ENOG502QWJG; Eukaryota.
DR GeneTree; ENSGT00940000153470; -.
DR HOGENOM; CLU_016749_0_0_1; -.
DR InParanoid; Q765H6; -.
DR OMA; ASIWKFQ; -.
DR OrthoDB; 179031at2759; -.
DR PhylomeDB; Q765H6; -.
DR TreeFam; TF313714; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 268510; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mgat5b; mouse.
DR PRO; PR:Q765H6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q765H6; protein.
DR Bgee; ENSMUSG00000043857; Expressed in embryonic brain and 79 other tissues.
DR ExpressionAtlas; Q765H6; baseline and differential.
DR Genevisible; Q765H6; MM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
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:0030144; F:alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity; IDA:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:MGI.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISO:MGI.
DR InterPro; IPR026116; GlyclTrfase_18.
DR Pfam; PF15024; Glyco_transf_18; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..792
FT /note="Alpha-1,6-mannosylglycoprotein 6-beta-N-
FT acetylglucosaminyltransferase B"
FT /id="PRO_0000288612"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..792
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..195
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 168..208
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 184..353
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 387..644
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 700..775
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 704..777
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 711..764
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 732..753
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT DISULFID 788..791
FT /evidence="ECO:0000250|UniProtKB:Q09328"
FT VAR_SEQ 1..377
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025736"
FT VAR_SEQ 378..431
FT /note="MGLSFKKYRCRIRVIDTFGTEPAYNHEEYATLHGYRTNWGYWNLNPKQFMTM
FT FP -> MALGVPCSELQASPPMGALPTRSAETPGRGISREQASAWTFDNLFFPLCGRAV
FT A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025737"
FT VAR_SEQ 475..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025738"
SQ SEQUENCE 792 AA; 89473 MW; C063E2614AB240B1 CRC64;
MITVNPDGKI MVRRCLVTLR PFRLFVLGIG FFTLCFLMTS LGGQFSARRL GDSPFTIRTE
VPGSPESRGA LRKMSDLLEL MVKRMDMLAR LENSSELHRT ASVAHLAADR LTPGASLIER
IQAIAQNVSD IAVKVDQILR HSLILHSKVS EGRRDQCEAP SDPKFPDCSG KVEWMRARWT
SDPCYAFFGV DGTECSFLIY LSEVEWFCPP LPWRNQTAAR TAPKSLPRVQ AVFRSNLSHL
LELMGSGKES LIFMKKRTRR FTAQWTKAAK YLAQKLGDIR RDQKQILVHI GFLTEESGDV
FSPRVLKGGP LGEMVQWADI LAALYVLGHS LRITVSLKEL QSNLGVPPGR GNCPLTVPLP
FDLIYTDYHG LQQMKQHMGL SFKKYRCRIR VIDTFGTEPA YNHEEYATLH GYRTNWGYWN
LNPKQFMTMF PHTPDNSFMG FVSEELNETE KQLIKDGKAS NMAVVYGKEA SIWKLQGKEK
FLAVLNKYME IHGTVYYESQ RPPEVPAFVK NHGLLPQPEF QQLLRKAKLF IGFGFPYEGP
APLEAIANGC IFLQSRFSPP HSSLNHEFFR GKPTSREVFS QHPYAENFIG KPHVWTVDYN
NSDEFETAIK AIMNTQVDPY LPYEYTCAGM LERINAYIQH QDFCVGPSPL PPGASTAQSP
FVLAPNATHL EWAQNISSVP GAWPPTHSLR AWLAAPGRAC TDACLDHGLI CEPSFFPFLN
SQNSFLKLQV PCDSTEWEMH HLYPAFAQPG QECYLQKEPL LFSCAGASTK YQRLCPCRDF
RKGQVALCQG CL
