Reviewed, UniProtKB/Swiss-Prot Q10469 (MGAT2_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
    EC=2.4.1.143
Alternative name(s):
    Mannoside acetylglucosaminyltransferase 2
    N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
    Beta-1,2-N-acetylglucosaminyltransferase II
    GlcNAc-T II
      Short name=GNT-II

Gene names

Name:

MGAT2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes an essential step in the conversion of oligo-mannose to complex N-glycans.
Catalytic activity	UDP-N-acetyl-D-glucosamine + 6-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Involvement in disease	Defects in MGAT2 are the cause of congenital disorder of glycosylation type 2A (CDG2A) [MIM:212066]; also known as carbohydrate-deficient glycoprotein syndrome type II. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Ref.3 Ref.4

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Disease	Congenital disorder of glycosylation Disease mutation
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oligosaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi stack Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Traceable author statement. Source: ProtInc
Molecular function	alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase		PRO_0000080517
Regions
	Topological domain	1 – 9	9	Cytoplasmic Potential
	Transmembrane	10 – 29	20	Signal-anchor for type II membrane protein Potential
	Topological domain	30 – 447	418	Lumenal Potential
Amino acid modifications
	Glycosylation	69	1	N-linked (GlcNAc...) Potential
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	262	1	H → R in CDG2A. Ref.3		VAR_003415
	Natural variant	290	1	S → F in CDG2A. Ref.3		VAR_003416
	Natural variant	318	1	N → D in CDG2A. Ref.4		VAR_012343

Sequences

	Sequence		Length	Mass (Da)
	Q10469-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 533B76D08BD8A572	FASTA	447	51,550
	10 20 30 40 50 60 MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKNEALAPP LLDAEPARGA GGRGGDHPSV 70 80 90 100 110 120 AVGIRRVSNV SAASLVPAVP QPEADNLTLR YRSLVYQLNF DQTLRNVDKA GTWAPRELVL 130 140 150 160 170 180 VVQVHNRPEY LRLLLDSLRK AQGIDNVLVI FSHDFWSTEI NQLIAGVNFC PVLQVFFPFS 190 200 210 220 230 240 IQLYPNEFPG SDPRDCPRDL PKNAALKLGC INAEYPDSFG HYREAKFSQT KHHWWWKLHF 250 260 270 280 290 300 VWERVKILRD YAGLILFLEE DHYLAPDFYH VFKKMWKLKQ QECPECDVLS LGTYSASRSF 310 320 330 340 350 360 YGMADKVDVK TWKSTEHNMG LALTRNAYQK LIECTDTFCT YDDYNWDWTL QYLTVSCLPK 370 380 390 400 410 420 FWKVLVPQIP RIFHAGDCGM HHKKTCRPST QSAQIESLLN NNKQYMFPET LTISEKFTVV 430 440 AISPPRKNGG WGDIRDHELC KSYRRLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein." Tan J., D'Agostaro A.F., Bendiak B., Reck F., Sarkar M., Squire J.A., Leong P., Schachter H. Eur. J. Biochem. 231:317-328(1995) [PubMed: 7635144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16. Tissue: Leukocyte.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disease with defective brain development." Tan J., Dunn J., Jaeken J., Schachter H. Am. J. Hum. Genet. 59:810-817(1996) [PubMed: 8808595] [Abstract] Cited for: VARIANTS CDG2A ARG-262 AND PHE-290.
[4]	"Congenital disorders of glycosylation IIa cause growth retardation, mental retardation, and facial dysmorphism." Cormier-Daire V., Amiel J., Vuillaumier-Barrot S., Tan J., Durand G., Munnich A., Le Merrer M., Seta N. J. Med. Genet. 37:875-877(2000) [PubMed: 11228641] [Abstract] Cited for: VARIANT CDG2A ASP-318.

Web resources

GeneReviews

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

Cross-references

Sequence databases
EMBLGenBankDDBJ	U15128 Genomic DNA. Translation: AAA86956.1. BC006390 mRNA. Translation: AAH06390.1.
IPI	IPI00025809.
PIR	S66256.
RefSeq	NP_002399.1.
UniGene	Hs.93338
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT16. Glycosyltransferase Family 16.
Proteomic databases
PeptideAtlas	Q10469.
PRIDE	Q10469.
Genome annotation databases
Ensembl	ENSG00000168282. Homo sapiens. [Contig view]
GeneID	4247.
KEGG	hsa:4247.
Organism-specific databases
GeneCards	GC14P049157.
H-InvDB	HIX0037689.
HGNC	HGNC:7045. MGAT2.
MIM	212066. phenotype. 602616. gene.
Orphanet	137. CDG syndrome. 79329. CDG syndrome, type IIa.
PharmGKB	PA30780.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q10469.
HOVERGEN	Q10469.
OMA	Q10469. KVDVKTW.
Enzyme and pathway databases
BRENDA	2.4.1.143. 247.
Gene expression databases
ArrayExpress	Q10469.
Bgee	Q10469.
CleanEx	HS_MGAT2.
GermOnline	ENSG00000168282. Homo sapiens.
Family and domain databases
InterPro	IPR007754. GlcNAc_II. [Graphical view]
PANTHER	PTHR12871. MGAT2. 1 hit.
Pfam	PF05060. MGAT2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	16741.
SOURCE	Search...

Entry information

Entry name

MGAT2_HUMAN

Accession

Primary (citable) accession number: Q10469

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)