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A3LTB7 (ALG3_PICST) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
ORF Names:PICST_58095
OrganismScheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) [Complete proteome]
Taxonomic identifier322104 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeScheffersomyces

Protein attributes

Sequence length477 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 – 477477Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
PRO_0000350931

Regions

Topological domain1 – 4848Lumenal Potential
Transmembrane49 – 6921Helical; Potential
Topological domain70 – 13162Cytoplasmic Potential
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 17220Lumenal Potential
Transmembrane173 – 19321Helical; Potential
Topological domain194 – 20310Cytoplasmic Potential
Transmembrane204 – 22421Helical; Potential
Topological domain2251Lumenal Potential
Transmembrane226 – 24318Helical; Potential
Topological domain244 – 2474Cytoplasmic Potential
Transmembrane248 – 27023Helical; Potential
Topological domain271 – 31646Lumenal Potential
Transmembrane317 – 33721Helical; Potential
Topological domain338 – 37134Cytoplasmic Potential
Transmembrane372 – 39221Helical; Potential
Topological domain393 – 40614Lumenal Potential
Transmembrane407 – 42721Helical; Potential
Topological domain428 – 4336Cytoplasmic Potential
Transmembrane434 – 45421Helical; Potential
Topological domain455 – 47723Lumenal Potential

Sequences

Sequence LengthMass (Da)Tools
A3LTB7 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 54DA89F304148739

FASTA47753,790
        10         20         30         40         50         60 
MSEPESSVAN NDGESTQAPQ LAELTLKNVL GDIVNGVHFI IFDPLGNRFV VPVIILLTSI 

        70         80         90        100        110        120 
ITKVIITKVP YTEIDFVTYM QQIQLVNQGE IDYAEISGDT GPIVYPAGFV QIYQWLYSQT 

       130        140        150        160        170        180 
NGGADIATGQ SIFGYLMTAT VVFVCVAYTM SPTTKPWVLF LLLGSKRLYS IYVLRLFNDC 

       190        200        210        220        230        240 
FTTAAMVGVT VFLQQGSYWY STSSFISFLF AIVGADLFSI AISIKMNALL YLPAVVIIAY 

       250        260        270        280        290        300 
FLVGENILLF AIVLAIVPLV QILVGWKFLL PLFDDEAASQ IRWNYINNAF NFGRKFLFKW 

       310        320        330        340        350        360 
TVNWRFIGEE TFLSDKFSIL LMGGHIVVLL FFIFTRFLNS KVTGKSIWQL IKDAFKPSST 

       370        380        390        400        410        420 
ISSNNKLIDY NVGPKLILLI LATTNVIGVL FSRSLHYQFL SWYCWQLPFL LHSTGWNFIV 

       430        440        450        460        470 
CLVLWGAHEW TWNVYPSTVA SSLVLVGILS SVLVGTWRNE AVWFEENNVV DDEKKNE 

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References

[1]"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.
Nat. Biotechnol. 25:319-326(2007) [PubMed: 17334359] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000498 Genomic DNA. Translation: ABN66377.2.
RefSeqXP_001384406.2. XM_001384369.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA3LTB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4838968.
GenomeReviewsGene locus ALG3 in contig CP000498_GR.
KEGGpic:PICST_58095.

Phylogenomic databases

eggNOGfuNOG07998.
HOGENOMHBG525447.
OMAIHRVAYT.
OrthoDBEOG4MPN04.

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_PICST
AccessionPrimary (citable) accession number: A3LTB7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: July 24, 2007
Last modified: November 16, 2011
This is version 37 of the entry and version 2 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