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Protein

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

Gene

ALG11

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

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).By similarity

Catalytic activityi

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.

Pathwayi

GO - Molecular functioni

  1. GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. oligosaccharide-lipid intermediate biosynthetic process Source: EnsemblFungi
  2. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ALG11
Ordered Locus Names:ADL235W
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
ProteomesiUP000000591: Chromosome IV

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini34 – 582549LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 582582GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferasePRO_0000080272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi33169.AGOS_ADL235W.

Structurei

3D structure databases

ProteinModelPortaliQ75B12.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi139 – 1424Poly-Gly

Sequence similaritiesi

Belongs to the glycosyltransferase group 1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0438.
HOGENOMiHOG000209670.
InParanoidiQ75B12.
KOiK03844.
OMAiYGFFHPY.
OrthoDBiEOG7673KQ.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q75B12-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESCWLTMES YQAALVVCIV SGLILAVAGY GNVRRLACEF LLKPPKRFRD
60 70 80 90 100
DICEALLRGP ENDQKPVLVD FGWRHGAVRR QMLLASAKAS AYSNERHGSK
110 120 130 140 150
IHISPDDIAR GRSFADALDV HRRSGRILFG FFHPFCNAGG GGEKVLWKAV
160 170 180 190 200
ETTLKQSLNN IVVVYTGDCD TTGARILSNV EHRFGSQLDS ERIVFIFLRH
210 220 230 240 250
RKWVESRTWP RMTLLGQALG SIVLSIEAAL CCPPDVWCDT MGYPFGYPFV
260 270 280 290 300
SWLCRIPIIT YTHYPVVSID MLDKLRMMPE FRNSPTLWAK FLYWRIFMRC
310 320 330 340 350
YTFAGSFVDL AVTNSTWTYN HINAIWSRTG NVSIIYPPCS TENLVIENAH
360 370 380 390 400
DMWDRKHQAV VIAQFRPEKR HALILRSFSN FVKKTGSNMK LLMLGSTRGQ
410 420 430 440 450
EDRDYVKKLE QLAYSELAIP KESLEFITDC KYEKMKKYLQ ESSFGINAMW
460 470 480 490 500
NEHFGIAVVE YAASGLITLA HASAGPLLDI IVPWDIEGDK QLERGSDKNR
510 520 530 540 550
TGFFFKDRSD PDFCKITAEF PTLEELFVRA DQLTDEERLA ISQRAKRCVL
560 570 580
HKFSDLKFSE DWAQVVDRTI QLLHTLRNDK VE
Length:582
Mass (Da):66,635
Last modified:July 5, 2004 - v1
Checksum:iBE8C12857524068E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016817 Genomic DNA. Translation: AAS51685.1.
RefSeqiNP_983861.1. NM_209214.1.

Genome annotation databases

EnsemblFungiiAAS51685; AAS51685; AGOS_ADL235W.
GeneIDi4619996.
KEGGiago:AGOS_ADL235W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016817 Genomic DNA. Translation: AAS51685.1.
RefSeqiNP_983861.1. NM_209214.1.

3D structure databases

ProteinModelPortaliQ75B12.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi33169.AGOS_ADL235W.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAS51685; AAS51685; AGOS_ADL235W.
GeneIDi4619996.
KEGGiago:AGOS_ADL235W.

Phylogenomic databases

eggNOGiCOG0438.
HOGENOMiHOG000209670.
InParanoidiQ75B12.
KOiK03844.
OMAiYGFFHPY.
OrthoDBiEOG7673KQ.

Enzyme and pathway databases

UniPathwayiUPA00378.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 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.
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Entry informationi

Entry nameiALG11_ASHGO
AccessioniPrimary (citable) accession number: Q75B12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: July 5, 2004
Last modified: January 7, 2015
This is version 74 of the entry and version 1 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

External Data

Dasty 3

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 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.