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A5DJQ5 (ALG3_PICGU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. 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:PGUG_03506
OrganismMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) [Complete proteome]
Taxonomic identifier294746 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Meyerozyma

Protein attributes

Sequence length475 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 – 475475Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
PRO_0000350930

Regions

Topological domain1 – 5656Lumenal Potential
Transmembrane57 – 7923Helical; Potential
Topological domain80 – 9819Cytoplasmic Potential
Transmembrane99 – 12123Helical; Potential
Topological domain122 – 13918Lumenal Potential
Transmembrane140 – 16021Helical; Potential
Topological domain161 – 18727Cytoplasmic Potential
Transmembrane188 – 20821Helical; Potential
Topological domain209 – 2102Lumenal Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 2365Cytoplasmic Potential
Transmembrane237 – 25721Helical; Potential
Topological domain258 – 2614Lumenal Potential
Transmembrane262 – 28221Helical; Potential
Topological domain283 – 32240Cytoplasmic Potential
Transmembrane323 – 34321Helical; Potential
Topological domain344 – 38441Lumenal Potential
Transmembrane385 – 40420Helical; Potential
Topological domain405 – 41511Cytoplasmic Potential
Transmembrane416 – 43621Helical; Potential
Topological domain437 – 4459Lumenal Potential
Transmembrane446 – 46621Helical; Potential
Topological domain467 – 4759Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
A5DJQ5 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 599B22AB461CEBB5

FASTA47554,217
        10         20         30         40         50         60 
MEETHEPKKH SEKEEIEDGL SSKTEAPHLP EFTFKNVCND IINGVIALFM DPFCNAIVVP 

        70         80         90        100        110        120 
ILVVFTSIAC KIVIANVKYT EIDFKTYMQQ IDMINDGELD YSLIAGDTGP IVYPAGFVQI 

       130        140        150        160        170        180 
YQWLSWLSSG GEDIPVVQSV FGYLHTLTVL LTCCTYSLVG DVQPWAYMLI VASKRLMSIY 

       190        200        210        220        230        240 
VLRLFNDCFT TACMVGVTLV LQAASYWFDT LGSTLVFLLT LVAADLYSMA ISIKMNALLF 

       250        260        270        280        290        300 
MPAFLIVVYF LCMENILKLL AVILVMVLVQ VMVGWKFLLV LFHDEDANYL RMTYLQRAFD 

       310        320        330        340        350        360 
FKRSFLYEWT VNWRFVPEEY FTSKLFANFL LVCHISVLIF FVISRFFSSK ITGKSLVTLV 

       370        380        390        400        410        420 
KDGFKPFNTI ASTNLYVNKK QGPKLILLTF ATTNTIGVLL SRSLHYQFLS WYCWHMPFLL 

       430        440        450        460        470 
YSTGWGPIIS GAMWAVHEWC WLTFPSTIQS SAILVTILSF TLATVWHRGE NWYGS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH408158 Genomic DNA. Translation: EDK39408.2.
RefSeqXP_001484125.1. XM_001484075.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5DJQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5126391.
KEGGpgu:PGUG_03506.

Phylogenomic databases

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_PICGU
AccessionPrimary (citable) accession number: A5DJQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: July 22, 2008
Last modified: December 14, 2011
This is version 33 of the entry and version 2 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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