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Q6BYY8 (ALG3_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 49. 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:DEHA2A05940g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length481 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 – 481481Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
PRO_0000350926

Regions

Topological domain1 – 4141Lumenal Potential
Transmembrane42 – 6221Helical; Potential
Topological domain63 – 12462Cytoplasmic Potential
Transmembrane125 – 14521Helical; Potential
Topological domain146 – 17227Lumenal Potential
Transmembrane173 – 19321Helical; Potential
Topological domain194 – 1974Cytoplasmic Potential
Transmembrane198 – 21821Helical; Potential
Topological domain219 – 2213Lumenal Potential
Transmembrane222 – 24221Helical; Potential
Topological domain243 – 2464Cytoplasmic Potential
Transmembrane247 – 26721Helical; Potential
Topological domain268 – 30841Lumenal Potential
Transmembrane309 – 32921Helical; Potential
Topological domain330 – 36738Cytoplasmic Potential
Transmembrane368 – 38821Helical; Potential
Topological domain389 – 40214Lumenal Potential
Transmembrane403 – 42321Helical; Potential
Topological domain424 – 43310Cytoplasmic Potential
Transmembrane434 – 45421Helical; Potential
Topological domain455 – 48127Lumenal Potential

Sequences

Sequence LengthMass (Da)Tools
Q6BYY8 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 3C015A3C038664CA

FASTA48155,180
        10         20         30         40         50         60 
MTEQSIKDGQ RPELPPFTLR NVLNDIYNGI LALFTDPFCT RIICPVVIVL TSLLSKAIIY 

        70         80         90        100        110        120 
KVPYTEIDFR TYIQQIQIIN DGELDYSLVQ GDTGQIVYPA GFVQIYQVLN WLTDEGTDIH 

       130        140        150        160        170        180 
AGQTAFGYLL ALTNFLVIIA YTMTPDFQPW PVYCLLLSKR LFSIYVLRLF NDCFTTVCMV 

       190        200        210        220        230        240 
SVTILLQQAA YWYKKGGSSI SFLLTMVAAD LYSIAISIKM NALLYFPGFI IVAYFLCGEN 

       250        260        270        280        290        300 
LLKFGTVLLV IPIVQVLMGW KFLLPFFNDE EASYIRWNYI NQAFNFNRKF LYKWTVNWRF 

       310        320        330        340        350        360 
VSEEFFLSDV FSNGLLIANA SVLIFFIFTR YISPRITCKP VSRLIKDAMV GPFSSTINKN 

       370        380        390        400        410        420 
NLLIDPKCGP KLVMLILGST NIIGILFARS LHYQFLSWYC WQLPFMLYMT GWSLLVCIPL 

       430        440        450        460        470        480 
WVVHEWCWNV FPSTPMSSGL LVSILAIVLF GVWYNTNEWF PKLADNEAAT IDESGESKKD 


K

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR382133 Genomic DNA. Translation: CAG84537.1.
RefSeqXP_456581.1. XM_456581.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ6BYY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2899876.
GenomeReviewsGene locus DEHA2A05940g in contig CR382133_GR.
KEGGdha:DEHA2A05940g.

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_DEBHA
AccessionPrimary (citable) accession number: Q6BYY8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: August 16, 2004
Last modified: December 14, 2011
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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