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Q2U6A4 (ALG3_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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
ORF Names:AO090120000319
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length413 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

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontransferase activity, transferring hexosyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
PRO_0000350923

Regions

Topological domain1 – 1818Lumenal Potential
Transmembrane19 – 3921Helical; Potential
Topological domain40 – 9556Cytoplasmic Potential
Transmembrane96 – 11621Helical; Potential
Topological domain117 – 13923Lumenal Potential
Transmembrane140 – 16021Helical; Potential
Topological domain161 – 18121Cytoplasmic Potential
Transmembrane182 – 20221Helical; Potential
Topological domain203 – 2075Lumenal Potential
Transmembrane208 – 22821Helical; Potential
Topological domain229 – 26133Cytoplasmic Potential
Transmembrane262 – 28221Helical; Potential
Topological domain283 – 30422Lumenal Potential
Transmembrane305 – 32521Helical; Potential
Topological domain326 – 37247Cytoplasmic Potential
Transmembrane373 – 39321Helical; Potential
Topological domain394 – 41320Lumenal Potential

Sequences

Sequence LengthMass (Da)Tools
Q2U6A4 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: D73845A54C5E4F76

FASTA41346,649
        10         20         30         40         50         60 
MELKHFIHEL CLNPRHTKWI APLLVIGDAF LCALIIWKIP YTEIDWTTYM QQIALYISGE 

        70         80         90        100        110        120 
RDYTLIKGST GPLVYPAAHV YSYMALYHLT DEGRDILFGQ ILFAVLYLVT LAVVMVCYRQ 

       130        140        150        160        170        180 
SGAPPYLFPL LVLSKRLHSV FVLRLFNDGL AVCAMWIAIL LFQNKKWTAG VTAWTVGVGI 

       190        200        210        220        230        240 
KMTLLLLAPA IAVVTVLSLS LVPSIRLGIL ALLIQVLLAI PFLQGNPIGY VARAFELTRQ 

       250        260        270        280        290        300 
FMFKWTVNWR FVGEDLFLSK QFSLALLGLH IFLLGLFVTT GWLRPSGSNV PDFLRSLLQG 

       310        320        330        340        350        360 
RQRTVVLSKS FIMTVMLTSL AIGLLCARSL HYQFFAYLSW ATPCLLWRAR LHPILIYAIW 

       370        380        390        400        410 
ALQEWAWNVY PSTNASSSVV VFSLAVQVFG VLLNSRNALS DAPPRRKGKE HIQ

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP007166 Genomic DNA. Translation: BAE62911.1.
RefSeqXP_001824044.1. XM_001823992.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2U6A4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00011459; CADAORAP00011226; CADAORAG00011459.
GeneID5996303.
GenomeReviewsGene locus alg3 in contig AP007166_GR.
KEGGaor:AOR_1_556094.

Phylogenomic databases

GeneTreeEFGT00050000003598.
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_ASPOR
AccessionPrimary (citable) accession number: Q2U6A4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 39 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

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