Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase

Gene

ALG8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • oligosaccharide-lipid intermediate biosynthetic process Source: SGD
  • protein N-linked glycosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7192.
YEAST:YOR067C-MONOMER.
BRENDAi2.4.1.265. 984.
ReactomeiR-SCE-446193. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT57. Glycosyltransferase Family 57.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ALG8
Ordered Locus Names:YOR067C
ORF Names:YOR29-18
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR067C.
SGDiS000005593. ALG8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4242LumenalSequence analysisAdd
BLAST
Transmembranei43 – 6321HelicalSequence analysisAdd
BLAST
Topological domaini64 – 9229CytoplasmicSequence analysisAdd
BLAST
Transmembranei93 – 11321HelicalSequence analysisAdd
BLAST
Topological domaini114 – 13926LumenalSequence analysisAdd
BLAST
Transmembranei140 – 16021HelicalSequence analysisAdd
BLAST
Topological domaini161 – 1688CytoplasmicSequence analysis
Transmembranei169 – 18921HelicalSequence analysisAdd
BLAST
Topological domaini190 – 21930LumenalSequence analysisAdd
BLAST
Transmembranei220 – 24021HelicalSequence analysisAdd
BLAST
Topological domaini241 – 26626CytoplasmicSequence analysisAdd
BLAST
Transmembranei267 – 28721HelicalSequence analysisAdd
BLAST
Topological domaini288 – 30720LumenalSequence analysisAdd
BLAST
Transmembranei308 – 32821HelicalSequence analysisAdd
BLAST
Topological domaini329 – 38254CytoplasmicSequence analysisAdd
BLAST
Transmembranei383 – 40321HelicalSequence analysisAdd
BLAST
Topological domaini404 – 41916LumenalSequence analysisAdd
BLAST
Transmembranei420 – 44021HelicalSequence analysisAdd
BLAST
Topological domaini441 – 4477CytoplasmicSequence analysis
Transmembranei448 – 46821HelicalSequence analysisAdd
BLAST
Topological domaini469 – 4702LumenalSequence analysis
Transmembranei471 – 49121HelicalSequence analysisAdd
BLAST
Topological domaini492 – 50413CytoplasmicSequence analysisAdd
BLAST
Transmembranei505 – 52521HelicalSequence analysisAdd
BLAST
Topological domaini526 – 54318LumenalSequence analysisAdd
BLAST
Transmembranei544 – 56421HelicalSequence analysisAdd
BLAST
Topological domaini565 – 57713CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferasePRO_0000174168Add
BLAST

Proteomic databases

MaxQBiP40351.

Interactioni

Protein-protein interaction databases

BioGridi34466. 143 interactions.
DIPiDIP-7542N.

Structurei

3D structure databases

ProteinModelPortaliP40351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000074967.
HOGENOMiHOG000168174.
InParanoidiP40351.
KOiK03849.
OMAiWKLKYPF.
OrthoDBiEOG7DZ8VC.

Family and domain databases

InterProiIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
PANTHERiPTHR12413. PTHR12413. 2 hits.
PfamiPF03155. Alg6_Alg8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40351-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGDRSRQNM AVTKKAKLKK NDEPKKVLKT AATEKGEGSK RYSLWNFWIS
60 70 80 90 100
TLFLKLLLIP DYFSTDFDVH RNWLAITNKL PISEWYYEHT SQWTLDYPPF
110 120 130 140 150
FAYFEWFLSQ FVPKSVRDDG CLDIVEIGKF GLPTIVFQRL TVIFSEILLF
160 170 180 190 200
VILQIYINTT KLSERSQSFV VASSIVLSPG FLIIDHIHFQ YNGFLFAILI
210 220 230 240 250
GSIVAAKNKR YILCAVLYTT AICFKHIFLY LAPCYFVFLL RAYVLNVNNF
260 270 280 290 300
KFKSYKDFLF LIRWANLLKL ATVVVGIFTI CFLPFAHQMP QVLSRLFPFS
310 320 330 340 350
RGLTHAYWAP NFWALYSFMD KILTTVMLKL PYVHTFATKF IKPPLIPQNI
360 370 380 390 400
KEINERLAAN NNGSKGLVQD VFFVILPQIP PKLTFILTIF YQVLAVLPLL
410 420 430 440 450
FDPSFKRFVG SLTLCGLASF LFGWHVHEKA IMLVIIPFTF LVGFDRRLLV
460 470 480 490 500
PFMLVASAGY VSLYPLLYKG QDFFIKTLYT YVWCIIYFAA FRKTTKISSS
510 520 530 540 550
VERRIFFLDR LALTYIFSLL PIVTVLQILD EVKWRYSFLQ KFEFLGLMIY
560 570
SVYCSLGIIS SWFALSWLYN FDELLWQ
Length:577
Mass (Da):67,385
Last modified:February 1, 1995 - v1
Checksum:iA59716F526B7B5A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75929 Genomic DNA. Translation: CAA53533.1.
Z74975 Genomic DNA. Translation: CAA99260.1.
Z70678 Genomic DNA. Translation: CAA94552.1.
BK006948 Genomic DNA. Translation: DAA10846.1.
PIRiS47961.
RefSeqiNP_014710.1. NM_001183486.1.

Genome annotation databases

EnsemblFungiiYOR067C; YOR067C; YOR067C.
GeneIDi854233.
KEGGisce:YOR067C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75929 Genomic DNA. Translation: CAA53533.1.
Z74975 Genomic DNA. Translation: CAA99260.1.
Z70678 Genomic DNA. Translation: CAA94552.1.
BK006948 Genomic DNA. Translation: DAA10846.1.
PIRiS47961.
RefSeqiNP_014710.1. NM_001183486.1.

3D structure databases

ProteinModelPortaliP40351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34466. 143 interactions.
DIPiDIP-7542N.

Protein family/group databases

CAZyiGT57. Glycosyltransferase Family 57.

Proteomic databases

MaxQBiP40351.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR067C; YOR067C; YOR067C.
GeneIDi854233.
KEGGisce:YOR067C.

Organism-specific databases

EuPathDBiFungiDB:YOR067C.
SGDiS000005593. ALG8.

Phylogenomic databases

GeneTreeiENSGT00550000074967.
HOGENOMiHOG000168174.
InParanoidiP40351.
KOiK03849.
OMAiWKLKYPF.
OrthoDBiEOG7DZ8VC.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:MONOMER-7192.
YEAST:YOR067C-MONOMER.
BRENDAi2.4.1.265. 984.
ReactomeiR-SCE-446193. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

PROiP40351.

Family and domain databases

InterProiIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
PANTHERiPTHR12413. PTHR12413. 2 hits.
PfamiPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiALG8_YEAST
AccessioniPrimary (citable) accession number: P40351
Secondary accession number(s): D6W2D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.