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Reviewed, UniProtKB/Swiss-Prot P27115 (MGAT1_RABIT)

Last modified November 25, 2008. Version 63. 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 · 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
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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_0000191387

Regions

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

Secondary structure

...................................................... 447
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27115-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 18AC90994F0EB435

FASTA44751,540
        10         20         30         40         50         60 
MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPVPSRLPSD NALDDDPASL TREVIRLAQD 

        70         80         90        100        110        120 
AEVELERQRG LLQQIREHHA LWSQRWKVPT AAPPAQPHVP VTPPPAVIPI LVIACDRSTV 

       130        140        150        160        170        180 
RRCLDKLLHY RPSAELFPII VSQDCGHEET AQVIASYGSA VTHIRQPDLS NIAVQPDHRK 

       190        200        210        220        230        240 
FQGYYKIARH YRWALGQIFH NFNYPAAVVV EDDLEVAPDF FEYFQATYPL LKADPSLWCV 

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

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

       370        380        390        400        410        420 
LARVYGAPQL QVEKVRTNDR KELGEVRVQY TGRDSFKAFA KALGVMDDLK SGVPRAGYRG 

       430        440 
IVTFLFRGRR VHLAPPQTWD GYDPSWT 

« Hide

References

[1]"Molecular cloning and expression of cDNA encoding the enzyme that controls conversion of high-mannose to hybrid and complex N-glycans: UDP-N-acetylglucosamine: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I."
Sarkar M., Hull E., Nishikawa Y., Simpson R.J., Moritz R.L., Dunn R., Schachter H.
Proc. Natl. Acad. Sci. U.S.A. 88:234-238(1991) [PubMed: 1824724] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

M57301 mRNA. Translation: AAA31493.1.
PIRA38561.
RefSeqNP_001076214.1.
UniGeneOcu.1975

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FO8X-ray1.40A106-447[»]
1FO9X-ray1.50A106-447[»]
1FOAX-ray1.80A106-447[»]
2AM3X-ray1.80A106-447[»]
2AM4X-ray1.70A106-447[»]
2AM5X-ray1.60A106-447[»]
2APCX-ray1.50A106-447[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSOCUG00000006544. Oryctolagus cuniculus. [Contig view]
GeneID100009521.

Phylogenomic databases

HOVERGENP27115.

Family and domain databases

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

Entry information

Entry nameMGAT1_RABIT
AccessionPrimary (citable) accession number: P27115
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 25, 2008
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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