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Q12001 (ALG6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 87. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
EC=2.4.1.267
Alternative name(s):
Asparagine-linked glycosylation protein 6
Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
Gene names
Name:ALG6
Ordered Locus Names:YOR002W
ORF Names:UNA544
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 length544 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adds the first 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 Man9GlcNAc(2)-PP-Dol. Ref.5

Catalytic activity

Dolichyl beta-D-glucosyl phosphate + 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-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 – 544544Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
PRO_0000174161

Regions

Topological domain1 – 3535Cytoplasmic Potential
Transmembrane36 – 5621Helical; Potential
Topological domain57 – 10448Lumenal Potential
Transmembrane105 – 12521Helical; Potential
Topological domain126 – 14520Cytoplasmic Potential
Transmembrane146 – 16621Helical; Potential
Topological domain167 – 1715Lumenal Potential
Transmembrane172 – 19221Helical; Potential
Topological domain193 – 22331Cytoplasmic Potential
Transmembrane224 – 24421Helical; Potential
Topological domain245 – 26319Lumenal Potential
Transmembrane264 – 28421Helical; Potential
Topological domain285 – 33248Cytoplasmic Potential
Transmembrane333 – 35321Helical; Potential
Topological domain354 – 3563Lumenal Potential
Transmembrane357 – 37721Helical; Potential
Topological domain378 – 39821Cytoplasmic Potential
Transmembrane399 – 41921Helical; Potential
Topological domain420 – 4256Lumenal Potential
Transmembrane426 – 44621Helical; Potential
Topological domain447 – 48135Cytoplasmic Potential
Transmembrane482 – 50221Helical; Potential
Topological domain503 – 5086Lumenal Potential
Transmembrane509 – 52921Helical; Potential
Topological domain530 – 54415Cytoplasmic Potential

Experimental info

Sequence conflict2031M → V in AAT92914. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q12001 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 64BFA11A1F6D02B7

FASTA54462,783
        10         20         30         40         50         60 
MAIGKRLLVN KPAEESFYAS PMYDFLYPFR PVGNQWLPEY IIFVCAVILR CTIGLGPYSG 

        70         80         90        100        110        120 
KGSPPLYGDF EAQRHWMEIT QHLPLSKWYW YDLQYWGLDY PPLTAFHSYL LGLIGSFFNP 

       130        140        150        160        170        180 
SWFALEKSRG FESPDNGLKT YMRSTVIISD ILFYFPAVIY FTKWLGRYRN QSPIGQSIAA 

       190        200        210        220        230        240 
SAILFQPSLM LIDHGHFQYN SVMLGLTAYA INNLLDEYYA MAAVCFVLSI CFKQMALYYA 

       250        260        270        280        290        300 
PIFFAYLLSR SLLFPKFNIA RLTVIAFATL ATFAIIFAPL YFLGGGLKNI HQCIHRIFPF 

       310        320        330        340        350        360 
ARGIFEDKVA NFWCVTNVFV KYKERFTIQQ LQLYSLIATV IGFLPAMIMT LLHPKKHLLP 

       370        380        390        400        410        420 
YVLIACSMSF FLFSFQVHEK TILIPLLPIT LLYSSTDWNV LSLVSWINNV ALFTLWPLLK 

       430        440        450        460        470        480 
KDGLHLQYAV SFLLSNWLIG NFSFITPRFL PKSLTPGPSI SSINSDYRRR SLLPYNVVWK 

       490        500        510        520        530        540 
SFIIGTYIAM GFYHFLDQFV APPSKYPDLW VLLNCAVGFI CFSIFWLWSY YKIFTSGSKS 


MKDL

« Hide

References

« Hide 'large scale' references
[1]"The sequence of a 30 kb fragment on the left arm of chromosome XV from Saccharomyces cerevisiae reveals 15 open reading frames, five of which correspond to previously identified genes."
Sterky F., Holmberg A., Pettersson B., Uhlen M.
Yeast 12:1091-1095(1996) [PubMed: 8896276] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway."
Reiss G., te Heesen S., Zimmerman J., Robbins P.W., Aebi M.
Glycobiology 6:493-498(1996) [PubMed: 8877369] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION.
[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		U43491 Genomic DNA. Translation: AAC49481.1.
Z74910 Genomic DNA. Translation: CAA99190.1.
AY692895 Genomic DNA. Translation: AAT92914.1.
BK006948 Genomic DNA. Translation: DAA10784.1.
PIRS61985.
RefSeqNP_014644.1. NM_001183421.1.

3D structure databases

ProteinModelPortalQ12001.
ModBaseSearch...

Protein-protein interaction databases

IntActQ12001. 5 interactions.
STRINGQ12001.

Protein family/group databases

CAZyGT57. Glycosyltransferase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR002W; YOR002W; YOR002W.
GeneID854163.
KEGGsce:YOR002W.
NMPDRfig|4932.3.peg.5739.

Organism-specific databases

CYGDYOR002w.
SGDS000005528. ALG6.

Phylogenomic databases

eggNOGfuNOG06801.
HOGENOMHBG621987.
OMAFLISVIT.
OrthoDBEOG4936SH.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-7191.

Gene expression databases

ArrayExpressQ12001.
GenevestigatorQ12001.
GermOnlineYOR002W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
KOK03848.
PANTHERPTHR12413. Alg6_Alg8. 1 hit.
PfamPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975941.

Entry information

Entry nameALG6_YEAST
AccessionPrimary (citable) accession number: Q12001
Secondary accession number(s): D6W268, E9P8Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 87 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents