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P50076 (ALG10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
EC=2.4.1.256
Alternative name(s):
Alpha-1,2-glucosyltransferase ALG10-A
Alpha-2-glucosyltransferase ALG10
Asparagine-linked glycosylation protein 10
Dolichyl-phosphoglucose-dependent glucosyltransferase ALG10
Gene names
Name:DIE2
Synonyms:ALG10
Ordered Locus Names:YGR227W
ORF Names:G8547
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc2Man9GlcNAc(2)-PP-Dol. Ref.5

Catalytic activity

Dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->2)-D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate. Ref.5

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.5.

Sequence similarities

Belongs to the ALG10 glucosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 525525Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
PRO_0000215463

Regions

Transmembrane36 – 5621Helical; Potential
Transmembrane95 – 11521Helical; Potential
Transmembrane128 – 14821Helical; Potential
Transmembrane151 – 17121Helical; Potential
Transmembrane188 – 20821Helical; Potential
Transmembrane214 – 23421Helical; Potential
Transmembrane257 – 27721Helical; Potential
Transmembrane295 – 31521Helical; Potential
Transmembrane334 – 35421Helical; Potential
Transmembrane376 – 39621Helical; Potential
Transmembrane424 – 44421Helical; Potential
Transmembrane448 – 46821Helical; Potential
Transmembrane493 – 51321Helical; Potential

Amino acid modifications

Glycosylation311N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2661I → K in CAA61176. Ref.2
Sequence conflict2661I → K in CAA97255. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P50076 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: CCA51CE249A4AB6E

FASTA52561,793
        10         20         30         40         50         60 
MDAKKNTGEA NNDVLEEEAA IQLIAPGIAR NLTQEVITGI FCNVVIYPLL LIYFVLTFRY 

        70         80         90        100        110        120 
MTTNIVPYEF IDEKFHVGQT LTYLKGKWTQ WDPKITTPPG IYILGLINYY CIKPIFKSWS 

       130        140        150        160        170        180 
TLTILRLVNL LGGIIVFPIL VLRPIFLFNA LGFWPVSLMS FPLMTTYYYL FYTDVWSTIL 

       190        200        210        220        230        240 
ILQSLSCVLT LPFGPVKSIW LSAFFAGVSC LFRQTNIIWT GFIMILAVER PAILQKQFNT 

       250        260        270        280        290        300 
HTFNNYLKLF IHAIDDFSNL VLPYMINFVL FFIYLIWNRS ITLGDKSSHS AGLHIVQIFY 

       310        320        330        340        350        360 
CFTFITVFSL PIWISRNFMK LYKLRIKRKP VQTFFEFIGI MLIIRYFTKV HPFLLADNRH 

       370        380        390        400        410        420 
YTFYLFRRLI GNKSRLIKYF FMTPIYHFST FAYLEVMRPN QLTFHPITPL PIKEPVHLPI 

       430        440        450        460        470        480 
QLTHVSWTAL ITCTMVTIVP SPLFEPRYYI LPYFFWRIFI TCSCEPLIKD LKPAKEGENP 

       490        500        510        520 
ITISSTKRLF MEFLWFMLFN VVTLVIFSKV SFPWTTEPYL QRIIW

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of genes that promote the expression of inositol transporter gene ITR1 in Saccharomyces cerevisiae."
Nikawa J., Hosaka K.
Mol. Microbiol. 16:301-308(1995) [PubMed: 7565092] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the right arm of Saccharomyces cerevisiae chromosome VII."
van der Aart Q.J.M., Kleine K., Steensma H.Y.
Yeast 12:385-390(1996) [PubMed: 8701610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 266.
Strain: ATCC 204508 / S288c.
[5]"The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation."
Burda P., Aebi M.
Glycobiology 8:455-462(1998) [PubMed: 9597543] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D38049 Genomic DNA. Translation: BAA07239.1.
X87941 Genomic DNA. Translation: CAA61176.1.
Z73012 Genomic DNA. Translation: CAA97255.1.
BK006941 Genomic DNA. Translation: DAA08319.2.
PIRS57691.
RefSeqNP_011743.2. NM_001181356.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP50076.

Protein family/group databases

CAZyGT59. Glycosyltransferase Family 59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID853142.
KEGGsce:YGR227W.
NMPDRfig|4932.3.peg.2871.

Organism-specific databases

CYGDYGR227w.
SGDS000003459. DIE2.

Phylogenomic databases

eggNOGfuNOG05358.
GeneTreeEFGT00050000003395.
HOGENOMHBG714502.
OMATHESAIM.
OrthoDBEOG47WRXP.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-7193.

Gene expression databases

ArrayExpressP50076.
GenevestigatorP50076.
GermOnlineYGR227W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016900. Alpha1_2_glucosyltferase_Alg10.
IPR007006. Glycosyltransferase_ALG10.
[Graphical view]
KOK03850.
PANTHERPTHR12989. DIE2_ALG10. 1 hit.
PfamPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNetSearch...

Other

NextBio973213.

Entry information

Entry nameALG10_YEAST
AccessionPrimary (citable) accession number: P50076
Secondary accession number(s): D6VV08
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 21, 2011
Last modified: January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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