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P40351 (ALG8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
EC=2.4.1.265
Alternative name(s):
Asparagine-linked glycosylation protein 8
Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase
Gene names
Name:ALG8
Ordered Locus Names:YOR067C
ORF Names:YOR29-18
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 length577 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adds the second 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 Glc1Man9GlcNAc(2)-PP-Dol. Ref.5

Catalytic activity

Dolichyl beta-D-glucosyl phosphate + 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->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.

Sequence similarities

Belongs to the ALG6/ALG8 glucosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
PRO_0000174168

Regions

Topological domain1 – 4242Lumenal Potential
Transmembrane43 – 6321Helical; Potential
Topological domain64 – 9229Cytoplasmic Potential
Transmembrane93 – 11321Helical; Potential
Topological domain114 – 13926Lumenal Potential
Transmembrane140 – 16021Helical; Potential
Topological domain161 – 1688Cytoplasmic Potential
Transmembrane169 – 18921Helical; Potential
Topological domain190 – 21930Lumenal Potential
Transmembrane220 – 24021Helical; Potential
Topological domain241 – 26626Cytoplasmic Potential
Transmembrane267 – 28721Helical; Potential
Topological domain288 – 30720Lumenal Potential
Transmembrane308 – 32821Helical; Potential
Topological domain329 – 38254Cytoplasmic Potential
Transmembrane383 – 40321Helical; Potential
Topological domain404 – 41916Lumenal Potential
Transmembrane420 – 44021Helical; Potential
Topological domain441 – 4477Cytoplasmic Potential
Transmembrane448 – 46821Helical; Potential
Topological domain469 – 4702Lumenal Potential
Transmembrane471 – 49121Helical; Potential
Topological domain492 – 50413Cytoplasmic Potential
Transmembrane505 – 52521Helical; Potential
Topological domain526 – 54318Lumenal Potential
Transmembrane544 – 56421Helical; Potential
Topological domain565 – 57713Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
P40351 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: A59716F526B7B5A6

FASTA57767,385
        10         20         30         40         50         60 
MKGDRSRQNM AVTKKAKLKK NDEPKKVLKT AATEKGEGSK RYSLWNFWIS TLFLKLLLIP 

        70         80         90        100        110        120 
DYFSTDFDVH RNWLAITNKL PISEWYYEHT SQWTLDYPPF FAYFEWFLSQ FVPKSVRDDG 

       130        140        150        160        170        180 
CLDIVEIGKF GLPTIVFQRL TVIFSEILLF VILQIYINTT KLSERSQSFV VASSIVLSPG 

       190        200        210        220        230        240 
FLIIDHIHFQ YNGFLFAILI GSIVAAKNKR YILCAVLYTT AICFKHIFLY LAPCYFVFLL 

       250        260        270        280        290        300 
RAYVLNVNNF KFKSYKDFLF LIRWANLLKL ATVVVGIFTI CFLPFAHQMP QVLSRLFPFS 

       310        320        330        340        350        360 
RGLTHAYWAP NFWALYSFMD KILTTVMLKL PYVHTFATKF IKPPLIPQNI KEINERLAAN 

       370        380        390        400        410        420 
NNGSKGLVQD VFFVILPQIP PKLTFILTIF YQVLAVLPLL FDPSFKRFVG SLTLCGLASF 

       430        440        450        460        470        480 
LFGWHVHEKA IMLVIIPFTF LVGFDRRLLV PFMLVASAGY VSLYPLLYKG QDFFIKTLYT 

       490        500        510        520        530        540 
YVWCIIYFAA FRKTTKISSS VERRIFFLDR LALTYIFSLL PIVTVLQILD EVKWRYSFLQ 

       550        560        570 
KFEFLGLMIY SVYCSLGIIS SWFALSWLYN FDELLWQ

« Hide

References

« Hide 'large scale' references
[1]"New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus."
Stagjar I., Te Heesen S., Aebi M.
Proc. Natl. Acad. Sci. U.S.A. 91:5977-5981(1994) [PubMed: 8016100] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the presence of two tRNAs and 24 new open reading frames."
Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.
Yeast 13:379-390(1997) [PubMed: 9133743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues."
Runge K.W., Robbins P.W.
J. Biol. Chem. 261:15582-15590(1986) [PubMed: 3536907] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[6]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X75929 Genomic DNA. Translation: CAA53533.1.
Z74975 Genomic DNA. Translation: CAA99260.1.
Z70678 Genomic DNA. Translation: CAA94552.1.
BK006948 Genomic DNA. Translation: DAA10846.1.
PIRS47961.
RefSeqNP_014710.1. NM_001183486.1.

3D structure databases

ProteinModelPortalP40351.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-7542N.
STRINGP40351.

Protein family/group databases

CAZyGT57. Glycosyltransferase Family 57.

Proteomic databases

PeptideAtlasP40351.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR067C; YOR067C; YOR067C.
GeneID854233.
KEGGsce:YOR067C.
NMPDRfig|4932.3.peg.5810.

Organism-specific databases

CYGDYOR067c.
SGDS000005593. ALG8.

Phylogenomic databases

eggNOGfuNOG05442.
GeneTreeEFGT00050000004500.
HOGENOMHBG560959.
OMAHNLNYSS.
OrthoDBEOG4J40RC.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-7192.

Gene expression databases

ArrayExpressP40351.
GenevestigatorP40351.
GermOnlineYOR067C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
KOK03849.
PANTHERPTHR12413. Alg6_Alg8. 1 hit.
PfamPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976121.

Entry information

Entry nameALG8_YEAST
AccessionPrimary (citable) accession number: P40351
Secondary accession number(s): D6W2D0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 14, 2011
This is version 90 of the entry and version 1 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

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