Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P27808 (MGAT1_MOUSE)

Last modified January 19, 2010. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
    EC=2.4.1.101
Alternative name(s):
    N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
      Short name=GlcNAc-T I
      Short name=GNT-I
Gene names
Name: Mgat1
Synonyms: Gnt1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.

Catalytic activity

UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(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.

Tissue specificity

Appears to be present in all tissues.

Sequence similarities

Belongs to the glycosyltransferase 13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
PRO_0000191385

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Signal-anchor for type II membrane protein Potential
Topological domain30 – 447418Lumenal Potential

Sequences

Sequence LengthMass (Da)Tools
P27808-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: E7C65EA8C8B34E6A

FASTA44751,690
        10         20         30         40         50         60 
MLKKQTAGLV LWGAIIFVGW NALLLLFFWT RPAPGRLPSD SALGDDPASL TREVIHLAED 

        70         80         90        100        110        120 
AEAELERQRG LLQQIKEHYA LWRQRWRVPT VAPPAWPRVP VTPSPVQIPI LVIACDRSTV 

       130        140        150        160        170        180 
RRCLDKLLHY RPSAERFPII VSQDCGHEET AQVIASYGTA VTHIRQPDLS NIAVQPDHRK 

       190        200        210        220        230        240 
FQGYYKIARH YRWALGQIFN KFKFPAAVVV EDDLEVAPDF FEYFQATYPL LRTDPSLWCV 

       250        260        270        280        290        300 
SAWNDNGKEQ MVDSSKPELL YRTDFFPGLG WLLLADLWAE LEPKWPKAFW DDWMRRPEQR 

       310        320        330        340        350        360 
KGRACIRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY LQQEAYDRDF 

       370        380        390        400        410        420 
LAQVYGAPQL QVEKVRTNDQ KELGEVRVQY TSRDSFKAFA KALGVMDDLK SGVPRAGYRG 

       430        440 
IVTFQFRGRR VHLAPPQTWT GYDPSWN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the mouse UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I gene."
Pownall S., Kozak C.A., Schappert K.T., Sarkar M., Hull E., Schachter H., Math J.D.
Genomics 12:699-704(1992) [PubMed: 1533386] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and expression of the murine gene and chromosomal location of the human gene encoding N-acetylglucosaminyltransferase I."
Kumar R., Yang J., Eddy R.L., Byers M.G., Shows T.B., Stanley P.
Glycobiology 2:383-393(1992) [PubMed: 1421759] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: NOD.
Tissue: Thymus.
[4]"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 gland.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

alpha-1,3-mannosyl-glycoprotein beta 1,2-GlcNAc T I (Mgat1)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73491 Genomic DNA. Translation: AAA37698.1.
L07037 mRNA. Translation: AAA40478.1.
AK087959 mRNA. Translation: BAC40058.1.
BC006629 mRNA. Translation: AAH06629.1.
IPIIPI00120839.
PIRA42500.
RefSeqNP_001103618.1.
NP_001103619.1.
NP_001103620.1.
NP_034924.3.
UniGeneMm.196933

3D structure databases

SMRP27808. Positions 108-446.
ModBaseSearch...

Protein-protein interaction databases

STRINGP27808.

Protein family/group databases

CAZyGT13. Glycosyltransferase Family 13.

PTM databases

PhosphoSiteP27808.

Proteomic databases

PRIDEP27808.

Genome annotation databases

EnsemblENSMUST00000081794; ENSMUSP00000080484; ENSMUSG00000020346; Mus musculus. [Genome view]
ENSMUST00000101293; ENSMUSP00000098851; ENSMUSG00000020346; Mus musculus. [Genome view]
ENSMUST00000109194; ENSMUSP00000104817; ENSMUSG00000020346; Mus musculus. [Genome view]
GeneID17308.
KEGGmmu:17308.
UCSCuc007iqc.1. mouse.

Organism-specific databases

CTD17308.
MGIMGI:96973. Mgat1.

Phylogenomic databases

eggNOGroNOG11145.
HOGENOMHBG717617.
HOVERGENP27808.
InParanoidP27808.
OMAPPDHRKF.
OrthoDBEOG9S7N92.
PhylomeDBP27808.

Enzyme and pathway databases

BRENDA2.4.1.101. 244.

Gene expression databases

ArrayExpressP27808.
BgeeP27808.
CleanExMM_MGAT1.
GenevestigatorP27808.
GermOnlineENSMUSG00000020346. Mus musculus.

Family and domain databases

InterProIPR004139. Glyco_trans_13.
[Graphical view]
PANTHERPTHR10468. Glyco_trans_13. 1 hit.
PfamPF03071. GNT-I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio291856.
SOURCESearch...

Entry information

Entry nameMGAT1_MOUSE
AccessionPrimary (citable) accession number: P27808
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 19, 2010
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents