Reviewed, UniProtKB/Swiss-Prot Q812G0 (MGT4A_MOUSE)

Names and origin

Protein names

Recommended name:
    Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
    EC=2.4.1.145
Alternative name(s):
    UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa
    N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa
      Short name=N-acetylglucosaminyltransferase IVa
      Short name=GlcNAc-T IVa
      Short name=GnT-IVa
Cleaved into the following chain:
    1- Recommended name:
            Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form

Gene names

Name:

Mgat4a

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells. Ref.1
Catalytic activity	UDP-N-acetyl-D-glucosamine + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2,4-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.
Cofactor	Divalent metal cations By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A: Golgi apparatus membrane; Single-pass type II membrane protein By similarity. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form: Secreted By similarity.
Disruption phenotype	Mice display impaired beta cell glucose transport and insulin secretion causing type 2 diabete. This is due to defects in SLC2A2/Glut-2 glycosylation, provoking SLC2A2/Glut-2 endocytosis with redistribution into endosomes and lysosomes. Ref.1
Sequence similarities	Belongs to the glycosyltransferase 54 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Signal-anchor Transmembrane
Ligand	Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q812G0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q812G0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     79-88: SKTALSTISD → N

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 535	535	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A		PRO_0000288585
	Chain	93 – 535	443	Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form By similarity		PRO_0000288586
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Signal-anchor for type II membrane protein Potential
	Topological domain	28 – 535	508	Lumenal Potential
	Coiled coil	28 – 63	36	Potential
Amino acid modifications
	Glycosylation	77	1	N-linked (GlcNAc...) Potential
	Glycosylation	458	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	79 – 88	10	SKTALSTISD → N in isoform 2.		VSP_025715
Experimental info
	Sequence conflict	487	1	F → S in BAE37301. Ref.2
	Sequence conflict	504	1	G → A in BAE37301. Ref.2
	Sequence conflict	522	1	W → R in BAE37301. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D6E0CA37825795C2	FASTA	535	61,480
	10 20 30 40 50 60 MRLRNGTVAT ALVFVTSFLT LSWYTTWQNG KEKLIAYQRE FLALKERLRV AEHRISQRSS 70 80 90 100 110 120 ELNTIVQQFR RAGAETNGSK TALSTISDNT IKLLKELTSK KSLRVPSIYY HLPHLLQNER 130 140 150 160 170 180 SLQPAVQIGS GRTGVSIVMG IPTVKREVKS YLVETLHSLI DNLYPEEKLD CVIVVFIGET 190 200 210 220 230 240 DLDYVHSVVA NLEKEFSREI SSGLLEIISP PESYYPDLTN LKETFGDSKE RVRWRTKQNL 250 260 270 280 290 300 DYCFLMMYAQ EKGIYYIQLE DDIIVKQNYF NTIKNFALQL SSEEWMILEF SQLGFIGKMF 310 320 330 340 350 360 QAPDLALVVE FILMFYKEKP IDWLLDHILW VKVCNPEKDA KHCDRQKANL RIRFRPSLFQ 370 380 390 400 410 420 HVGLHSSLSG KIQKLTDKDY MKPLLLKVHV NPPAEVSTSL KVYQGHTLEK TYMGEDFFWA 430 440 450 460 470 480 ITPTAGDYIL FKFDKPVNVE SYLFHSGNQE HPGDILLNTT VDVLPLKSDS LEISKETKDK 490 500 510 520 530 RLEDGYFRIG KFEYGVAEGI VDPGLNPISA FRLSVIQNSA VWAILNEIHI KKVTS
	Isoform 2. Checksum: 352E5C85E588BA1A	FASTA	526	60,590
	10 20 30 40 50 60 MRLRNGTVAT ALVFVTSFLT LSWYTTWQNG KEKLIAYQRE FLALKERLRV AEHRISQRSS 70 80 90 100 110 120 ELNTIVQQFR RAGAETNGNN TIKLLKELTS KKSLRVPSIY YHLPHLLQNE RSLQPAVQIG 130 140 150 160 170 180 SGRTGVSIVM GIPTVKREVK SYLVETLHSL IDNLYPEEKL DCVIVVFIGE TDLDYVHSVV 190 200 210 220 230 240 ANLEKEFSRE ISSGLLEIIS PPESYYPDLT NLKETFGDSK ERVRWRTKQN LDYCFLMMYA 250 260 270 280 290 300 QEKGIYYIQL EDDIIVKQNY FNTIKNFALQ LSSEEWMILE FSQLGFIGKM FQAPDLALVV 310 320 330 340 350 360 EFILMFYKEK PIDWLLDHIL WVKVCNPEKD AKHCDRQKAN LRIRFRPSLF QHVGLHSSLS 370 380 390 400 410 420 GKIQKLTDKD YMKPLLLKVH VNPPAEVSTS LKVYQGHTLE KTYMGEDFFW AITPTAGDYI 430 440 450 460 470 480 LFKFDKPVNV ESYLFHSGNQ EHPGDILLNT TVDVLPLKSD SLEISKETKD KRLEDGYFRI 490 500 510 520 GKFEYGVAEG IVDPGLNPIS AFRLSVIQNS AVWAILNEIH IKKVTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes." Ohtsubo K., Takamatsu S., Minowa M.T., Yoshida A., Takeuchi M., Marth J.D. Cell 123:1307-1321(2005) [PubMed: 16377570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE. Strain: 129/SvJ.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Egg.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB053217 mRNA. Translation: BAC55018.1. AB053225 Genomic DNA. Translation: BAC55085.1. AK163327 mRNA. Translation: BAE37301.1.
IPI	IPI00330055. IPI00850878.
RefSeq	NP_776295.1.
UniGene	Mm.25861 Mm.447744
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT54. Glycosyltransferase Family 54.
Proteomic databases
PRIDE	Q812G0.
Genome annotation databases
Ensembl	ENSMUSG00000026110. Mus musculus. [Contig view]
GeneID	269181.
KEGG	mmu:269181.
Organism-specific databases
MGI	MGI:2662992. Mgat4a.
Phylogenomic databases
HOGENOM	Q812G0.
HOVERGEN	Q812G0.
OMA	Q812G0. SSEDWMI.
Enzyme and pathway databases
BRENDA	2.4.1.145. 244.
Gene expression databases
ArrayExpress	Q812G0.
Bgee	Q812G0.
Family and domain databases
InterPro	IPR006759. Glyco_transf_54. [Graphical view]
PANTHER	PTHR12062. Glyco_transf_54. 1 hit.
Pfam	PF04666. Glyco_transf_54. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	392721.
SOURCE	Search...

Entry information

Entry name

MGT4A_MOUSE

Accession

Primary (citable) accession number: Q812G0
Secondary accession number(s): Q3TQT1, Q80UI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)