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Q6BVB2 (ALG11_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:
GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase

EC=2.4.1.131
Alternative name(s):
Alpha-1,2-mannosyltransferase ALG11
Asparagine-linked glycosylation protein 11
Glycolipid 2-alpha-mannosyltransferase
Gene names
Name:ALG11
Ordered Locus Names:DEHA2C03982g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum By similarity.

Catalytic activity

2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = 2 GDP + 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.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Sequence similarities

Belongs to the glycosyltransferase group 1 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionGDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 616616GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
PRO_0000080275

Regions

Transmembrane1 – 2121Helical; Potential
Transmembrane200 – 22021Helical; Potential
Transmembrane235 – 25521Helical; Potential
Transmembrane289 – 30921Helical; Potential

Amino acid modifications

Glycosylation3121N-linked (GlcNAc...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q6BVB2 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 69F8BBC8881DF1DB

FASTA61670,746
        10         20         30         40         50         60 
MGYLVVIGVI ACVAYGILQV VSTVLPRLLL VPSQNWQDKI KKEIEQPMVR YLKVGNKRSS 

        70         80         90        100        110        120 
YRRRLVLASK QPSFYTNFVN NKIKVASVDS QNDEGEFLAE MKKRDVRDPQ RKIIYGFFHP 

       130        140        150        160        170        180 
YANNGGGGER VLWQAVQATL ATSDRNIVAI YTTNYESDPT SILDKVEAKF QISRLDEDRI 

       190        200        210        220        230        240 
VFVYLRKYAR LIDGDYWKRF TLIGQLFGSM VLSWEAMFEL SPDVWIDTIG LPGSYLLVSL 

       250        260        270        280        290        300 
VLKIPIMSYV HYPIIQPEMF NKLKFQGLSQ IRVPKLSEIK TDVFSIGKLI YWSGVFYFYK 

       310        320        330        340        350        360 
YLGSLVNITL ANGSWTFNHI SNIWTINKDE AGYEMDILYP PCGTETLTKN VETLGSRENK 

       370        380        390        400        410        420 
LLFIAQFRPE KRHSLILRQY SKFLVNATSI GTPLKNIPTL VFLGSCRTPD DTKTLHDLKQ 

       430        440        450        460        470        480 
EVDDLELNGY VEFVVDCSYE DIMVWLSKVK FGLNAMWNEH FGIGVVEYMS RGVIPLCHAS 

       490        500        510        520        530        540 
AGPLLDIVTN WDNEPTSVSW YNNTGFFFKD KSDPDFDLSL QSDTASEFLQ FSSRDNKDST 

       550        560        570        580        590        600 
STYPTLARLL DELFITNPDL ISETRLQSMR ENGVKSVLEK FSNGVFTLKW MQYSNQLGDL 

       610 
EKSYREERRS GIEKVY 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382135 Genomic DNA. Translation: CAG85902.2.
RefSeqXP_457857.2. XM_457857.1.

3D structure databases

ProteinModelPortalQ6BVB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4959.Q6BVB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2900656.
KEGGdha:DEHA2C03982g.

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000209670.
KOK03844.
OMAHPYANNG.
OrthoDBEOG7673KQ.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

InterProIPR001296. Glyco_trans_1.
[Graphical view]
PfamPF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALG11_DEBHA
AccessionPrimary (citable) accession number: Q6BVB2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways