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Q5AJD2 (ALG8_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase
Gene names
Name:ALG8
ORF Names:CaO19.1659, CaO19.9228
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the ALG6/ALG8 glucosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
PRO_0000278328

Regions

Topological domain1 – 4141Lumenal Potential
Transmembrane42 – 6221Helical; Potential
Topological domain63 – 13977Cytoplasmic Potential
Transmembrane140 – 16021Helical; Potential
Topological domain161 – 1699Lumenal Potential
Transmembrane170 – 19223Helical; Potential
Topological domain193 – 22028Cytoplasmic Potential
Transmembrane221 – 24121Helical; Potential
Topological domain242 – 27433Lumenal Potential
Transmembrane275 – 29521Helical; Potential
Topological domain296 – 2983Cytoplasmic Potential
Transmembrane299 – 32123Helical; Potential
Topological domain322 – 37857Lumenal Potential
Transmembrane379 – 39921Helical; Potential
Topological domain400 – 41516Cytoplasmic Potential
Transmembrane416 – 43621Helical; Potential
Topological domain437 – 4437Lumenal Potential
Transmembrane444 – 46421Helical; Potential
Topological domain465 – 4662Cytoplasmic Potential
Transmembrane467 – 48721Helical; Potential
Topological domain488 – 51831Lumenal Potential
Transmembrane519 – 53921Helical; Potential
Topological domain540 – 55718Cytoplasmic Potential
Transmembrane558 – 57821Helical; Potential
Topological domain579 – 5879Lumenal Potential
Compositional bias24 – 3916Thr-rich

Sequences

Sequence LengthMass (Da)Tools
Q5AJD2 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 27BF61F4B8F67FEA

FASTA58767,887
        10         20         30         40         50         60 
MAKKKSTGPQ PSLSSSPNGR AKVTAETITT TTTTTTDTTN SYSLLNIWVI SLALKILLFI 

        70         80         90        100        110        120 
GYHSTDFDVH RNWLAITNKL PISQWYIENT SQWTLDYPPF FAYFEYLLSL LVPRFVANDG 

       130        140        150        160        170        180 
CLDIVEIGQY GLPTIYFQRL TVIISELVLF YALQTIVKTS PTLSAKRRMY VATASLALSP 

       190        200        210        220        230        240 
GLILIDHIHF QYNGMMYGIL LLCINSARLQ QYLLCGFWFS VLLCFKHIYL YLAPAVFIFL 

       250        260        270        280        290        300 
LRGYCLKFNW NKRKNFFINI FNFIQWINLF KLGSIVILVF IIAFGPFYNV LPQLISRLFP 

       310        320        330        340        350        360 
FSRGLTHAYW APNIWAVYSF LDRILIQIYK KIPMSKYPLL KIFQFDPNSL NNDQLLKTST 

       370        380        390        400        410        420 
RGIVGDIEFF ILPNITPKLT FLLTLFYQIM ALIPLFIQPT YRRFVGALTL CGYASFLFGW 

       430        440        450        460        470        480 
HVHEKAILLV IFPMTLLVAR DQKLLTPFNL LVSCGYGSLF PLIFTCNEWL IKVVYTYTWY 

       490        500        510        520        530        540 
IIFYFNFRKV VRPSKNNIIG NGIGNGNGKG GGIILDRMVN LYILLFNVVV IITSLFDLFK 

       550        560        570        580 
HKYPVLQNFE FLNLMIYSVY CAIGIISSWN GFCWLYFIDD GIWNQDQ 

« Hide

References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000014 Genomic DNA. Translation: EAL02821.1.
AACQ01000013 Genomic DNA. Translation: EAL02948.1.
RefSeqXP_721617.1. XM_716524.1.
XP_721736.1. XM_716643.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5AJD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3636562.
3636691.
KEGGcal:CaO19.1659.
cal:CaO19.9228.

Organism-specific databases

CGDCAL0000044. ALG8.

Phylogenomic databases

OMAARERRYV.
PhylomeDBQ5AJD2.

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...

Entry information

Entry nameALG8_CANAL
AccessionPrimary (citable) accession number: Q5AJD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families