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Reviewed, UniProtKB/Swiss-Prot Q751K5 (ALG3_ASHGO)

Last modified November 3, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
    EC=2.4.1.130
Alternative name(s):
    Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
    Asparagine-linked glycosylation protein 6
Gene names
Name: ALG3
Ordered Locus Names: AGL299C
OrganismAshbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

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Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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

Transfers an alpha-D-mannosyl residue from dolichyl-phosphate D-mannose into membrane lipid-linked oligosaccharide.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Sequence similarities

Belongs to the ALG3 family.

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Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
PRO_0000350919

Regions

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

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Sequences

Sequence LengthMass (Da)Tools
Q751K5-1 [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

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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 / NRRL Y-1056 / CBS 109.51.

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Cross-references

Sequence databases

AE016820 Genomic DNA. Translation: AAS54192.1.
RefSeqNP_986368.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ751K5.

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

HOGENOMQ751K5.
OMALRLFNDC.

Family and domain databases

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

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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: November 3, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents