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Q6FXS2 (ALG3_CANGA) 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:CAGL0A04587g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length442 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 – 442442Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
PRO_0000350924

Regions

Topological domain1 – 4242Lumenal Potential
Transmembrane43 – 6321Helical; Potential
Topological domain64 – 8724Cytoplasmic Potential
Transmembrane88 – 10821Helical; Potential
Topological domain109 – 16456Lumenal Potential
Transmembrane165 – 18521Helical; Potential
Topological domain186 – 20015Cytoplasmic Potential
Transmembrane201 – 22323Helical; Potential
Topological domain224 – 23613Lumenal Potential
Transmembrane237 – 25721Helical; Potential
Topological domain258 – 29740Cytoplasmic Potential
Transmembrane298 – 31821Helical; Potential
Topological domain319 – 33618Lumenal Potential
Transmembrane337 – 35721Helical; Potential
Topological domain358 – 37518Cytoplasmic Potential
Transmembrane376 – 39621Helical; Potential
Topological domain397 – 40913Lumenal Potential
Transmembrane410 – 43021Helical; Potential
Topological domain431 – 44212Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
Q6FXS2 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 910EC4CB4277E949

FASTA44251,651
        10         20         30         40         50         60 
MQTVRSEDNP PKKEEFKRPP IDLLQDLKDG INHVVYNPLG NKIVMPLMFL LESVLLKYVI 

        70         80         90        100        110        120 
AAIPYTEIDY KAYMEQVEMI YEEGNYNYLE ITGGTGPLVY PAGHVLIFRV LNYFTEGMNH 

       130        140        150        160        170        180 
IEVGQKIFRY LYLITLLMQY TCYYQLRLPP WCVVLASLSK RLHSIYVLRL FNDCFTTFFM 

       190        200        210        220        230        240 
VLFVLLYTLR SNNSTKMSMV ISTFGSLVYS MAISVKMNAL LYLPGYLVST YLINEGKLIN 

       250        260        270        280        290        300 
CLISASVILF WQVIVSLRFL RSYPVEYLAG AFDFSRQFMF KWSVNWQFLD EDAFQDRVFH 

       310        320        330        340        350        360 
TTLLGSQFVA VVAMTLCLYP RLPLDAWKSL KAPFTQVVIA DLRFIVPFLL MTSNFIGVLF 

       370        380        390        400        410        420 
SRSLHYQFLS WYHWTLPCLI YWSKLPMPLG FIWYICHEYC WNSYPPNEKA SILLFTLNAS 

       430        440 
LLCLLAINCM RPVIVNIKRK QQ

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR380947 Genomic DNA. Translation: CAG57860.1.
RefSeqXP_444967.1. XM_444967.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2886386.
GenomeReviewsGene locus CAGL0A04587g in contig CR380947_GR.
KEGGcgr:CAGL0A04587g.

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_CANGA
AccessionPrimary (citable) accession number: Q6FXS2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: July 19, 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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