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P27115 (MGAT1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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=GNT-I
Short name=GlcNAc-T I
Gene names
Name:MGAT1
Synonyms:GNT1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
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.

Cofactor

Manganese. The cofactor is mostly bound to the substrate. Ref.3

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 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 447418Lumenal Potential

Sites

Active site2911Proton acceptor Potential
Metal binding2131Manganese
Binding site1171Substrate
Binding site1441Substrate
Binding site1901Substrate
Binding site2121Substrate
Binding site3221Substrate

Amino acid modifications

Disulfide bond115 ↔ 145 Ref.2 Ref.3
Disulfide bond239 ↔ 305 Ref.2 Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P27115 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues."
Gordon R.D., Sivarajah P., Satkunarajah M., Ma D., Tarling C.A., Vizitiu D., Withers S.G., Rini J.M.
J. Mol. Biol. 360:67-79(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 106-447 IN COMPLEX WITH SUBSTRATE ANALOGS, MANGANESE-BINDING SITE, DISULFIDE BONDS.
[3]"X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily."
Unligil U.M., Zhou S., Yuwaraj S., Sarkar M., Schachter H., Rini J.M.
EMBO J. 19:5269-5280(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 106-447 ALONE AND IN COMPLEX WITH UDP-GLCNAC, ACTIVE SITE, COFACTOR, MANGANESE-BINDING SITE, SUBSTRATE-BINDING SITES, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57301 mRNA. Translation: AAA31493.1.
PIRA38561.
RefSeqNP_001076214.1. NM_001082745.1.
UniGeneOcu.1975.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP27115.
SMRP27115. Positions 106-447.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT13. Glycosyltransferase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009521.

Organism-specific databases

CTD100009521.

Phylogenomic databases

HOVERGENHBG052466.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

InterProIPR004139. Glyco_trans_13.
[Graphical view]
PANTHERPTHR10468. PTHR10468. 1 hit.
PfamPF03071. GNT-I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27115.

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: February 19, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways