General information | DisProt: | DP00618 | Name: | Alpha-1,2-mannosyltransferase ALG11 | Synonym(s): | ALG11_YEAST
Asparagine-linked glycosylation protein 11
Alg11
| First appeared in release: | Release 5.2 (08/07/2010) | UniProt: | P53954 | UniGene: | | SwissProt: | ALG11_YEAST | TrEMBL: | | NCBI (GI): | 1730730 | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | Sequence length: | 548 | Percent disordered: | 3% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MGSAWTNYNF EEVKSHFGFK KYVVSSLVLV YGLIKVLTWI FRQWVYSSLN PFSKKSSLLN - 60 RAVASCGEKN VKVFGFFHPY CNAGGGGEKV LWKAVDITLR KDAKNVIVIY SGDFVNGENV - 120 TPENILNNVK AKFDYDLDSD RIFFISLKLR YLVDSSTWKH FTLIGQAIGS MILAFESIIQ - 180 CPPDIWIDTM GYPFSYPIIA RFLRRIPIVT YTHYPIMSKD MLNKLFKMPK KGIKVYGKIL - 240 YWKVFMLIYQ SIGSKIDIVI TNSTWTNNHI KQIWQSNTCK IIYPPCSTEK LVDWKQKFGT - 300 AKGERLNQAI VLAQFRPEKR HKLIIESFAT FLKNLPDSVS PIKLIMAGST RSKQDENYVK - 360 SLQDWSENVL KIPKHLISFE KNLPFDKIEI LLNKSTFGVN AMWNEHFGIA VVEYMASGLI - 420 PIVHASAGPL LDIVTPWDAN GNIGKAPPQW ELQKKYFAKL EDDGETTGFF FKEPSDPDYN - 480 TTKDPLRYPN LSDLFLQITK LDYDCLRVMG ARNQQYSLYK FSDLKFDKDW ENFVLNPICK - 540 LLEEEERG
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Functional narrative |
Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | G-loop | Location: | 79 - 92 | Length: | 14 | Region sequence: |
PYCNAGGGGEKVLW | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Substrate/ligand binding
| Detection methods:
- Immunochemistry (298 K; KCl (buffer) 0.5 M)
| References:
- Absmanner B, Schmeiser V, Kampf M, Lehle L. "Biochemical characterization, membrane association and identification of amino acids essential for function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase, catalyzing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide." Biochem J. 2010; 426(2): 205-17. PubMed: 19929855
- Breton C, Snajdrová L, Jeanneau C, Koca J, Imberty A. "Structures and mechanisms of glycosyltransferases." Glycobiology. 2005; 16(2): 29R-37R. PubMed: 16037492
- Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S. "Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases." Proc. Natl. Acad. Sci. U.S.A.. 2003; 100(3): 845-9. PubMed: 12538870
- Qasba PK, Ramakrishnan B, Boeggeman E. "Substrate-induced conformational changes in glycosyltransferases." Trends Biochem. Sci.. 2005; 30(1): 53-62. PubMed: 15653326
- Wrabl JO, Grishin NV. "Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily." J. Mol. Biol.. 2001; 314(3): 365-74. PubMed: 11846551
| Comments:Absmanner, et al. (2010), found that replacement of glycine residues G84, G85 and G87 with alanine, there was no loss of function. When these residues were replaced with proline, G85 and G87 were found to be critical to function, but G84 was not.
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References |
- Absmanner B, Schmeiser V, Kampf M, Lehle L. "Biochemical characterization, membrane association and identification of amino acids essential for function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase, catalyzing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide." Biochem J. 2010; 426(2): 205-17. PubMed: 19929855
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Comments |
AV (7-7-2010) PubMed: 15653326
[ PMID 19929855]
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