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Q751K5 (ALG3_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase

EC=2.4.1.258
Alternative name(s):
Asparagine-linked glycosylation protein 6
Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Gene names
Name:ALG3
Ordered Locus Names:AGL299C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc(2)-PP-Dol By similarity.

Catalytic activity

Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->3)-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 ALG3 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
PRO_0000350919

Regions

Topological domain1 – 124124Lumenal Potential
Transmembrane125 – 14521Helical; Potential
Topological domain146 – 16823Cytoplasmic Potential
Transmembrane169 – 18921Helical; Potential
Topological domain190 – 20617Lumenal Potential
Transmembrane207 – 22721Helical; Potential
Topological domain228 – 2303Cytoplasmic Potential
Transmembrane231 – 25121Helical; Potential
Topological domain252 – 29039Lumenal Potential
Transmembrane291 – 31121Helical; Potential
Topological domain312 – 34332Cytoplasmic Potential
Transmembrane344 – 36421Helical; Potential
Topological domain365 – 37511Lumenal Potential
Transmembrane376 – 39621Helical; Potential
Topological domain397 – 40812Cytoplasmic Potential
Transmembrane409 – 42921Helical; Potential
Topological domain430 – 4323Lumenal Potential

Sequences

Sequence LengthMass (Da)Tools
Q751K5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B462531EC4FC7313

FASTA43248,660
        10         20         30         40         50         60 
MSAAVPTTRA GTPPTLQCGW RSACGKLLDI ANYVIFSPEA SAVVMPVLVA WECVLLKLIV 

        70         80         90        100        110        120 
KHVPYTEIDY LAYMEQIWQI NNGERDYSKI EGGTGPLVYP AGHVLIHRLL ERATDGLQNV 

       130        140        150        160        170        180 
ARGQDIFTWL YLLTLVLQFG VYRMLRLPPW CIVLACLSKR LHSVYVLRLF NDGWTTLMVV 

       190        200        210        220        230        240 
VAVFLLLLAA RHPRLCLPAA LVYSAAVSIK MNALLYLPGV LVALFLLTRG HLLALALCGA 

       250        260        270        280        290        300 
VAVAWQVLVA ADFLSTHPAE YFATAFDFRR QFMYRWSVNW QLVGEQVFSH PTFHRCLLLS 

       310        320        330        340        350        360 
HIAILMLFFF TRYAEPRQPN WFRTAAAALR HPATAVLAAS PPRAHVAYVL LVSNFIGVLF 

       370        380        390        400        410        420 
ARSLHYQFLA WYHWTLPALL HWARMPCLLA LLWYVLHELC WDTYPPSSVA SATLYALNSA 

       430 
LLLLLYINGP PA 

« Hide

References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016820 Genomic DNA. Translation: AAS54192.1.
RefSeqNP_986368.2. NM_211430.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ751K5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4622661.
GenomeReviewsGene locus AGL299C in contig AE016820_GR.
KEGGago:AGOS_AGL299C.
NMPDRfig|33169.1.peg.4013.

Organism-specific databases

AGDAGL299C.

Phylogenomic databases

eggNOGfuNOG07998.
HOGENOMHBG525447.
OMAIHRVAYT.
OrthoDBEOG4MPN04.
PhylomeDBQ751K5.

Family and domain databases

InterProIPR007873. Glycosyltransferase_ALG3.
[Graphical view]
KOK03845.
PANTHERPTHR12646. ALG3. 1 hit.
PfamPF05208. ALG3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALG3_ASHGO
AccessionPrimary (citable) accession number: Q751K5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: July 5, 2004
Last modified: December 14, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families