Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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: -Protein inferred from homologyi

Functioni

Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man5GlcNAc2-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: 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

Keywordsi

Molecular functionGlycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378

Protein family/group databases

CAZyiGT4 Glycosyltransferase Family 4

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
Proteomesi
  • UP000000591 Componenti: Chromosome IV

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 33Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini34 – 582LumenalSequence analysisAdd BLAST549

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000802721 – 582GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferaseAdd BLAST582

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi314N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi331N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi499N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi33169.AAS51685

Structurei

3D structure databases

ProteinModelPortaliQ75B12
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi139 – 142Poly-Gly4

Sequence similaritiesi

Belongs to the glycosyltransferase group 1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000209670
InParanoidiQ75B12
KOiK03844
OMAiTLPIFRY
OrthoDBiEOG092C21XK

Family and domain databases

CDDicd03806 GT1_ALG11_like, 1 hit
InterProiView protein in InterPro
IPR038013 ALG11
IPR031814 ALG11_N
IPR001296 Glyco_trans_1
PfamiView protein in Pfam
PF15924 ALG11_N, 1 hit
PF00534 Glycos_transf_1, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiALG11_ASHGO
AccessioniPrimary (citable) accession number: Q75B12
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: July 5, 2004
Last modified: March 28, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health