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Protein

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

Gene

ALG3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc(2)-PP-Dol. Sensitive to H.mrakii HM-1 killer toxin.2 Publications

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.1 Publication

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

  • alpha-1,3-mannosyltransferase activity Source: SGD
  • dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity Source: SGD

GO - Biological processi

  • mannosylation Source: GOC
  • oligosaccharide-lipid intermediate biosynthetic process Source: SGD
  • protein glycosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7188.
YEAST:YBL082C-MONOMER.
BRENDAi2.4.1.258. 984.
ReactomeiR-SCE-446193. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT58. Glycosyltransferase Family 58.

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 3
Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase
HM-1 killer toxin resistance protein
Gene namesi
Name:ALG3
Synonyms:RHK1
Ordered Locus Names:YBL082C
ORF Names:YBL0720
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL082C.
SGDiS000000178. ALG3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4141LumenalSequence analysisAdd
BLAST
Transmembranei42 – 6221HelicalSequence analysisAdd
BLAST
Topological domaini63 – 9533CytoplasmicSequence analysisAdd
BLAST
Transmembranei96 – 11621HelicalSequence analysisAdd
BLAST
Topological domaini117 – 13721LumenalSequence analysisAdd
BLAST
Transmembranei138 – 15821HelicalSequence analysisAdd
BLAST
Topological domaini159 – 17113CytoplasmicSequence analysisAdd
BLAST
Transmembranei172 – 19221HelicalSequence analysisAdd
BLAST
Topological domaini193 – 21624LumenalSequence analysisAdd
BLAST
Transmembranei217 – 23721HelicalSequence analysisAdd
BLAST
Topological domaini238 – 2425CytoplasmicSequence analysis
Transmembranei243 – 26321HelicalSequence analysisAdd
BLAST
Topological domaini264 – 30239LumenalSequence analysisAdd
BLAST
Transmembranei303 – 32321HelicalSequence analysisAdd
BLAST
Topological domaini324 – 34522CytoplasmicSequence analysisAdd
BLAST
Transmembranei346 – 36621HelicalSequence analysisAdd
BLAST
Topological domaini367 – 38115LumenalSequence analysisAdd
BLAST
Transmembranei382 – 40221HelicalSequence analysisAdd
BLAST
Topological domaini403 – 41513CytoplasmicSequence analysisAdd
BLAST
Transmembranei416 – 43621HelicalSequence analysisAdd
BLAST
Topological domaini437 – 45822LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi275 – 2751A → V in ALG3-1; leads to an underglycosylation of secretory proteins.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferasePRO_0000080565Add
BLAST

Proteomic databases

MaxQBiP38179.
PeptideAtlasiP38179.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RPB9P279994EBI-2463,EBI-15798

Protein-protein interaction databases

BioGridi32621. 86 interactions.
DIPiDIP-4854N.
MINTiMINT-489474.

Structurei

3D structure databases

ProteinModelPortaliP38179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 58 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000013904.
HOGENOMiHOG000237555.
InParanoidiP38179.
KOiK03845.
OMAiLECRTIL.
OrthoDBiEOG76MKJK.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P38179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGEQSPQGE KSLQRKQFVR PPLDLWQDLK DGVRYVIFDC RANLIVMPLL
60 70 80 90 100
ILFESMLCKI IIKKVAYTEI DYKAYMEQIE MIQLDGMLDY SQVSGGTGPL
110 120 130 140 150
VYPAGHVLIY KMMYWLTEGM DHVERGQVFF RYLYLLTLAL QMACYYLLHL
160 170 180 190 200
PPWCVVLACL SKRLHSIYVL RLFNDCFTTL FMVVTVLGAI VASRCHQRPK
210 220 230 240 250
LKKSLALVIS ATYSMAVSIK MNALLYFPAM MISLFILNDA NVILTLLDLV
260 270 280 290 300
AMIAWQVAVA VPFLRSFPQQ YLHCAFNFGR KFMYQWSINW QMMDEEAFND
310 320 330 340 350
KRFHLALLIS HLIALTTLFV TRYPRILPDL WSSLCHPLRK NAVLNANPAK
360 370 380 390 400
TIPFVLIASN FIGVLFSRSL HYQFLSWYHW TLPILIFWSG MPFFVGPIWY
410 420 430 440 450
VLHEWCWNSY PPNSQASTLL LALNTVLLLL LALTQLSGSV ALAKSHLRTT

SSMEKKLN
Length:458
Mass (Da):52,861
Last modified:October 1, 1994 - v1
Checksum:i1C2FEAD6D459C249
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861G → R in AAA75352 (PubMed:7754714).Curated
Sequence conflicti187 – 19812LGAIV…RCHQR → FRGYRGQQVPSA in AAA75352 (PubMed:7754714).CuratedAdd
BLAST
Sequence conflicti266 – 2661S → Q in AAA75352 (PubMed:7754714).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79489 Genomic DNA. Translation: CAA56024.1.
Z35844 Genomic DNA. Translation: CAA84904.1.
M89908 Genomic DNA. Translation: AAA75352.1.
BK006936 Genomic DNA. Translation: DAA07041.1.
PIRiS45424.
RefSeqiNP_009471.1. NM_001178322.1.

Genome annotation databases

EnsemblFungiiYBL082C; YBL082C; YBL082C.
GeneIDi852196.
KEGGisce:YBL082C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79489 Genomic DNA. Translation: CAA56024.1.
Z35844 Genomic DNA. Translation: CAA84904.1.
M89908 Genomic DNA. Translation: AAA75352.1.
BK006936 Genomic DNA. Translation: DAA07041.1.
PIRiS45424.
RefSeqiNP_009471.1. NM_001178322.1.

3D structure databases

ProteinModelPortaliP38179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32621. 86 interactions.
DIPiDIP-4854N.
MINTiMINT-489474.

Protein family/group databases

CAZyiGT58. Glycosyltransferase Family 58.

Proteomic databases

MaxQBiP38179.
PeptideAtlasiP38179.

Protocols and materials databases

DNASUi852196.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL082C; YBL082C; YBL082C.
GeneIDi852196.
KEGGisce:YBL082C.

Organism-specific databases

EuPathDBiFungiDB:YBL082C.
SGDiS000000178. ALG3.

Phylogenomic databases

GeneTreeiENSGT00390000013904.
HOGENOMiHOG000237555.
InParanoidiP38179.
KOiK03845.
OMAiLECRTIL.
OrthoDBiEOG76MKJK.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:MONOMER-7188.
YEAST:YBL082C-MONOMER.
BRENDAi2.4.1.258. 984.
ReactomeiR-SCE-446193. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

NextBioi970682.
PROiP38179.

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. "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II."
    Obermaier B., Gassenhuber J., Piravandi E., Domdey H.
    Yeast 11:1103-1112(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Sequence of a segment of yeast chromosome II shows two novel genes, one almost entirely hydrophobic and the other extremely asparagine-serine rich."
    Cusick M.E.
    Yeast 10:1251-1256(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-406.
  5. "A novel yeast gene, RHK1, is involved in the synthesis of the cell wall receptor for the HM-1 killer toxin that inhibits beta-1,3-glucan synthesis."
    Kimura T., Kitamoto N., Kito Y., Iimura Y., Shirai T., Komiyama T., Furuichi Y., Sakka K., Ohmiya K.
    Mol. Gen. Genet. 254:139-147(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Cloning and characterization of the ALG3 gene of Saccharomyces cerevisiae."
    Aebi M., Gassenhuber J., Domdey H., Te Heesen S.
    Glycobiology 6:439-444(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, VARIANT ALG3-1.
  7. "Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase."
    Sharma C.B., Knauer R., Lehle L.
    Biol. Chem. 382:321-328(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiALG3_YEAST
AccessioniPrimary (citable) accession number: P38179
Secondary accession number(s): D6VPS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 11, 2016
This is version 135 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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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.