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Q921V5 (MGAT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 16, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
EC=2.4.1.143
Alternative name(s):
Beta-1,2-N-acetylglucosaminyltransferase II
GlcNAc-T II
Short name=GNT-II
Mannoside acetylglucosaminyltransferase 2
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
Gene names
Name:Mgat2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 442442Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
PRO_0000080518

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 2920Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 442413Lumenal Potential

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict91K → E in BAC38888. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q921V5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E32D078C4F209843

FASTA44251,030
        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

« Hide

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. expand/collapse author list , 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

EMBL
GenBank
DDBJ		AK083370 mRNA. Translation: BAC38888.1.
AK152925 mRNA. Translation: BAE31600.1.
BC010583 mRNA. Translation: AAH10583.1.
BC027169 mRNA. Translation: AAH27169.1.
IPIIPI00122285.
RefSeqNP_666147.1. NM_146035.2.
UniGeneMm.206642.
Mm.398746.
Mm.483133.

3D structure databases

ProteinModelPortalQ921V5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ921V5.

Protein family/group databases

CAZyGT16. Glycosyltransferase Family 16.

Proteomic databases

PRIDEQ921V5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060579; ENSMUSP00000057905; ENSMUSG00000043998.
ENSMUST00000164921; ENSMUSP00000132931; ENSMUSG00000043998.
GeneID217664.
KEGGmmu:217664.
UCSCuc011ymy.1. mouse.

Organism-specific databases

CTD4247.
MGIMGI:2384966. Mgat2.

Phylogenomic databases

eggNOGNOG239633.
GeneTreeENSGT00390000007341.
HOGENOMHOG000261661.
HOVERGENHBG052467.
InParanoidQ921V5.
KOK00736.
OMAGDCGMHH.
OrthoDBEOG4VX255.

Gene expression databases

ArrayExpressQ921V5.
BgeeQ921V5.
CleanExMM_MGAT2.
GenevestigatorQ921V5.
GermOnlineENSMUSG00000043998. Mus musculus.

Family and domain databases

InterProIPR007754. GlcNAc_II.
[Graphical view]
PANTHERPTHR12871. MGAT2. 1 hit.
PfamPF05060. MGAT2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio375938.
SOURCESearch...

Entry information

Entry nameMGAT2_MOUSE
AccessionPrimary (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: May 16, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents