Reviewed, UniProtKB/Swiss-Prot Q921V5 (MGAT2_MOUSE)

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

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	442 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes an essential step in the conversion of oligo-mannose to complex N-glycans By similarity.
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 By similarity.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	oligosaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro protein amino acid N-linked glycosylation via asparagine Inferred from mutant phenotype. Source: MGI
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
Molecular function	alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 442	442	Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase		PRO_0000080518
Regions
	Topological domain	1 – 9	9	Cytoplasmic Potential
	Transmembrane	10 – 29	20	Signal-anchor for type II membrane protein Potential
	Topological domain	30 – 442	413	Lumenal Potential
Amino acid modifications
	Glycosylation	64	1	N-linked (GlcNAc...) Potential
	Glycosylation	81	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	9	1	K → E in BAC38888. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q921V5-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E32D078C4F209843	FASTA	442	51,030
	10 20 30 40 50 60 MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKSDALGPP LLDAEPVRGA GHLAVSVGIR 70 80 90 100 110 120 RVSNESAAPL VPAVPRPEVD NLTLRYRSLV YQLNFDQMLR NVGNDGTWSP GELVLVVQVH 130 140 150 160 170 180 NRPEYLRLLI DSLRKAQGIQ EVLVIFSHDF WSAEINSLIS RVDFCPVLQV FFPFSIQLYP 190 200 210 220 230 240 NEFPGSDPRD CPRDLKKNAA LKLGCINAEY PDSFGHYREA KFSQTKHHWW WKLHFVWERV 250 260 270 280 290 300 KVLQDYTGLI LFLEEDHYLA PDFYHVFKKM WKLKQQECPG CDVLSLGTYT TIRSFYGIAD 310 320 330 340 350 360 KVDVKTWKST EHNMGLALTR DAYQKLIECT DTFCTYDDYN WDWTLQYLTL ACLPKIWKVL 370 380 390 400 410 420 VPQAPRIFHA GDCGMHHKKT CRPSTQSAQI ESLLNSNKQY LFPETLVIGE KFPMAAISPP 430 440 RKNGGWGDIR DHELCKSYRR LQ

References

[1]	"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]. Strain: C57BL/6J. Tissue: Bone marrow.
[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]. Strain: FVB/N. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK083370 mRNA. Translation: BAC38888.1. AK152925 mRNA. Translation: BAE31600.1. BC010583 mRNA. Translation: AAH10583.1. BC027169 mRNA. Translation: AAH27169.1.
IPI	IPI00122285.
RefSeq	NP_666147.1.
UniGene	Mm.206642 Mm.398746 Mm.475966
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT16. Glycosyltransferase Family 16.
Proteomic databases
PRIDE	Q921V5.
Genome annotation databases
Ensembl	ENSMUSG00000043998. Mus musculus. [Contig view]
GeneID	217664.
KEGG	mmu:217664.
Organism-specific databases
MGI	MGI:2384966. Mgat2.
Phylogenomic databases
HOGENOM	Q921V5.
HOVERGEN	Q921V5.
OMA	Q921V5. KVDVKTW.
Enzyme and pathway databases
BRENDA	2.4.1.143. 244.
Gene expression databases
ArrayExpress	Q921V5.
Bgee	Q921V5.
CleanEx	MM_MGAT2.
GermOnline	ENSMUSG00000043998. Mus musculus.
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	375938.
SOURCE	Search...

Entry information

Entry name

MGAT2_MOUSE

Accession

Primary (citable) accession number: Q921V5
Secondary accession number(s): Q3U6X4, Q8C3Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)