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Protein

Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase

Gene

ALG3

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc(2)-PP-Dol.By similarity

Catalytic activityi

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.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ALG3
Ordered Locus Names:AGL299C
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
Proteomesi
  • UP000000591 Componenti: Chromosome VII

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 124124LumenalSequence analysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Topological domaini146 – 16823CytoplasmicSequence analysisAdd
BLAST
Transmembranei169 – 18921HelicalSequence analysisAdd
BLAST
Topological domaini190 – 20617LumenalSequence analysisAdd
BLAST
Transmembranei207 – 22721HelicalSequence analysisAdd
BLAST
Topological domaini228 – 2303CytoplasmicSequence analysis
Transmembranei231 – 25121HelicalSequence analysisAdd
BLAST
Topological domaini252 – 29039LumenalSequence analysisAdd
BLAST
Transmembranei291 – 31121HelicalSequence analysisAdd
BLAST
Topological domaini312 – 34332CytoplasmicSequence analysisAdd
BLAST
Transmembranei344 – 36421HelicalSequence analysisAdd
BLAST
Topological domaini365 – 37511LumenalSequence analysisAdd
BLAST
Transmembranei376 – 39621HelicalSequence analysisAdd
BLAST
Topological domaini397 – 40812CytoplasmicSequence analysisAdd
BLAST
Transmembranei409 – 42921HelicalSequence analysisAdd
BLAST
Topological domaini430 – 4323LumenalSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferasePRO_0000350919Add
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the ALG3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000237555.
InParanoidiQ751K5.
KOiK03845.
OMAiDWKAYMD.
OrthoDBiEOG76MKJK.

Family and domain databases

InterProiIPR007873. Glycosyltransferase_ALG3.
[Graphical view]
PANTHERiPTHR12646. PTHR12646. 1 hit.
PfamiPF05208. ALG3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q751K5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAAVPTTRA GTPPTLQCGW RSACGKLLDI ANYVIFSPEA SAVVMPVLVA
60 70 80 90 100
WECVLLKLIV KHVPYTEIDY LAYMEQIWQI NNGERDYSKI EGGTGPLVYP
110 120 130 140 150
AGHVLIHRLL ERATDGLQNV ARGQDIFTWL YLLTLVLQFG VYRMLRLPPW
160 170 180 190 200
CIVLACLSKR LHSVYVLRLF NDGWTTLMMV VAVFLLLLAA RHPRLCLPAA
210 220 230 240 250
LVYSAAVSIK MNALLYLPGV LVALFLLTRG HLLALALCGA VAVAWQVLVA
260 270 280 290 300
ADFLSTHPAE YFATAFDFRR QFMYRWSVNW QLVGEQVFSH PTFHRCLLLS
310 320 330 340 350
HIAILMLFFF TRYAAPRQPN WFRTAAAALR HPATAVLAAS PPRAHVAYVL
360 370 380 390 400
LVSNFIGVLF ARSLHYQFLA WYHWTLPALL HWARMPCLLA LLWYVLHELC
410 420 430
WDTYPPSSVA SATLYALNSA LLLLLYINGP PA
Length:432
Mass (Da):48,634
Last modified:January 9, 2013 - v2
Checksum:i146BB41AC4F9D865
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016820 Genomic DNA. Translation: AAS54192.2.
RefSeqiNP_986368.2. NM_211430.2.

Genome annotation databases

EnsemblFungiiAAS54192; AAS54192; AGOS_AGL299C.
GeneIDi4622661.
KEGGiago:AGOS_AGL299C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016820 Genomic DNA. Translation: AAS54192.2.
RefSeqiNP_986368.2. NM_211430.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAS54192; AAS54192; AGOS_AGL299C.
GeneIDi4622661.
KEGGiago:AGOS_AGL299C.

Phylogenomic databases

HOGENOMiHOG000237555.
InParanoidiQ751K5.
KOiK03845.
OMAiDWKAYMD.
OrthoDBiEOG76MKJK.

Enzyme and pathway databases

UniPathwayiUPA00378.

Family and domain databases

InterProiIPR007873. Glycosyltransferase_ALG3.
[Graphical view]
PANTHERiPTHR12646. PTHR12646. 1 hit.
PfamiPF05208. ALG3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
    Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
    Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
  2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
    Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
    G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 179.
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Entry informationi

Entry nameiALG3_ASHGO
AccessioniPrimary (citable) accession number: Q751K5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 9, 2013
Last modified: June 8, 2016
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.