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Q6CMF1 (ALG3_KLULA) 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:KLLA0E20823g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length462 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 – 462462Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
PRO_0000350927

Regions

Topological domain1 – 144144Lumenal Potential
Transmembrane145 – 16521Helical; Potential
Topological domain166 – 17611Cytoplasmic Potential
Transmembrane177 – 19721Helical; Potential
Topological domain198 – 21720Lumenal Potential
Transmembrane218 – 23821Helical; Potential
Topological domain239 – 2435Cytoplasmic Potential
Transmembrane244 – 26421Helical; Potential
Topological domain265 – 30642Lumenal Potential
Transmembrane307 – 32721Helical; Potential
Topological domain328 – 35629Cytoplasmic Potential
Transmembrane357 – 37721Helical; Potential
Topological domain378 – 39013Lumenal Potential
Transmembrane391 – 41121Helical; Potential
Topological domain412 – 46251Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
Q6CMF1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 25B8027AA8A961D6

FASTA46253,252
        10         20         30         40         50         60 
MVEEGANKTV GAPTVGDDQQ PKEFVRPPFT PFQDILDAFN YLMWNPEANA IAMPVLILLE 

        70         80         90        100        110        120 
SIAMKFIQNK VSYTEIDYTA YMEQIWMIQN GERDYSQIKG GTGPLVYPAG HVFIYKIFEW 

       130        140        150        160        170        180 
VSDGLENISE AQDLFRYLYV ITLMIQFMCF GLLNIPPGYA IFAILSKRLH SVYVLRLFND 

       190        200        210        220        230        240 
CFTTLFMSLA VLVMILCAKY KIRGFLVLIG SSFYSMAVSI KMNALLYLPG VLLTIYLLER 

       250        260        270        280        290        300 
CNTFKIVLNL AVMVIWQVII AIPFWKEYPW EYLQSAFNFS RQFMYKWSVN WQMVDEEVFL 

       310        320        330        340        350        360 
DPLFHRSLLI SHVIVLVVFL FYKLIPTNMN TPAGLLKIGK ANLLHPFTDA VFSAMRVNAE 

       370        380        390        400        410        420 
QIAYILLVTN YIGVLFARSL HYQFLSWYHW TLPVLLNWAN VPYPLCVLWY LTHEWCWNSY 

       430        440        450        460 
PPNATASTLL HACNTSLLLA VFLRGPANSK SGDNETTHEK AE

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR382125 Genomic DNA. Translation: CAG99975.1.
RefSeqXP_454888.1. XM_454888.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ6CMF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2894493.
GenomeReviewsGene locus KLLA0E20823g in contig CR382125_GR.
KEGGkla:KLLA0E20747g.

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_KLULA
AccessionPrimary (citable) accession number: Q6CMF1
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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