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Protein

Alpha-1,3/1,6-mannosyltransferase ALG2

Gene

ALG2

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

Mannosylates Man2GlcNAc(2)-dolichol diphosphate and Man1GlcNAc(2)-dolichol diphosphate to form Man3GlcNAc(2)-dolichol diphosphate.1 Publication

Catalytic activityi

GDP-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol.1 Publication
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol.1 Publication

Pathwayi

GO - Molecular functioni

  1. GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity Source: SGD
  2. glycolipid 6-alpha-mannosyltransferase activity Source: SGD

GO - Biological processi

  1. mannosylation Source: GOC
  2. oligosaccharide-lipid intermediate biosynthetic process Source: SGD
  3. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7186.
YEAST:YGL065C-MONOMER.
ReactomeiREACT_250523. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1,3/1,6-mannosyltransferase ALG2 (EC:2.4.1.132, EC:2.4.1.257)
Alternative name(s):
Asparagine-linked glycosylation protein 2
GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase
GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
Gene namesi
Name:ALG2
Ordered Locus Names:YGL065C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL065c.
SGDiS000003033. ALG2.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei64 – 8421HelicalSequence AnalysisAdd
BLAST
Transmembranei112 – 13221HelicalSequence AnalysisAdd
BLAST
Transmembranei443 – 46321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. endoplasmic reticulum membrane Source: Reactome
  3. 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
Mutagenesisi335 – 3351E → A: Severly affects activity, especially the second mannosylation step. 1 Publication
Mutagenesisi343 – 3431E → A: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Alpha-1,3/1,6-mannosyltransferase ALG2PRO_0000080271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP43636.
PaxDbiP43636.
PeptideAtlasiP43636.

Expressioni

Gene expression databases

GenevestigatoriP43636.

Interactioni

Subunit structurei

Interacts with ALG1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ALG1P166612EBI-2459,EBI-2206309

Protein-protein interaction databases

BioGridi33182. 8 interactions.
DIPiDIP-5401N.
IntActiP43636. 4 interactions.
MINTiMINT-523155.
STRINGi4932.YGL065C.

Structurei

3D structure databases

ProteinModelPortaliP43636.
SMRiP43636. Positions 219-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00550000075033.
HOGENOMiHOG000177048.
InParanoidiP43636.
KOiK03843.
OMAiGETGWLR.
OrthoDBiEOG7G4QQG.

Family and domain databases

InterProiIPR027054. ALG2.
IPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4_N.
[Graphical view]
PANTHERiPTHR12526:SF221. PTHR12526:SF221. 1 hit.
PfamiPF13439. Glyco_transf_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43636-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIEKDKRTIA FIHPDLGIGG AERLVVDAAL GLQQQGHSVI IYTSHCDKSH
60 70 80 90 100
CFEEVKNGQL KVEVYGDFLP TNFLGRFFIV FATIRQLYLV IQLILQKKVN
110 120 130 140 150
AYQLIIIDQL STCIPLLHIF SSATLMFYCH FPDQLLAQRA GLLKKIYRLP
160 170 180 190 200
FDLIEQFSVS AADTVVVNSN FTKNTFHQTF KYLSNDPDVI YPCVDLSTIE
210 220 230 240 250
IEDIDKKFFK TVFNEGDRFY LSINRFEKKK DVALAIKAFA LSEDQINDNV
260 270 280 290 300
KLVICGGYDE RVAENVEYLK ELQSLADEYE LSHTTIYYQE IKRVSDLESF
310 320 330 340 350
KTNNSKIIFL TSISSSLKEL LLERTEMLLY TPAYEHFGIV PLEAMKLGKP
360 370 380 390 400
VLAVNNGGPL ETIKSYVAGE NESSATGWLK PAVPIQWATA IDESRKILQN
410 420 430 440 450
GSVNFERNGP LRVKKYFSRE AMTQSFEENV EKVIWKEKKY YPWEIFGISF
460 470 480 490 500
SNFILHMAFI KILPNNPWPF LFMATFMVLY FKNYLWGIYW AFVFALSYPY

EEI
Length:503
Mass (Da):58,047
Last modified:October 1, 1996 - v2
Checksum:i1200E1C8EA023DD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81T → S in CAA61199. (PubMed:8400550)Curated
Sequence conflicti237 – 2382KA → NG in CAA61199. (PubMed:8400550)Curated
Sequence conflicti302 – 3021T → A in CAA61199. (PubMed:8400550)Curated
Sequence conflicti457 – 4571M → I in CAA61199. (PubMed:8400550)Curated
Sequence conflicti470 – 50334FLFMA…PYEEI → SYLWPLLWYYILRTTYGEFT GHLYSLSPTLMKKYNVYLNK QCIPPEEKIIYIGEEISKCK(PubMed:8400550)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87947 Genomic DNA. Translation: CAA61199.1.
Z72587 Genomic DNA. Translation: CAA96768.1.
BK006941 Genomic DNA. Translation: DAA08037.1.
PIRiS64069.
RefSeqiNP_011450.1. NM_001180930.1.

Genome annotation databases

EnsemblFungiiYGL065C; YGL065C; YGL065C.
GeneIDi852815.
KEGGisce:YGL065C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87947 Genomic DNA. Translation: CAA61199.1.
Z72587 Genomic DNA. Translation: CAA96768.1.
BK006941 Genomic DNA. Translation: DAA08037.1.
PIRiS64069.
RefSeqiNP_011450.1. NM_001180930.1.

3D structure databases

ProteinModelPortaliP43636.
SMRiP43636. Positions 219-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33182. 8 interactions.
DIPiDIP-5401N.
IntActiP43636. 4 interactions.
MINTiMINT-523155.
STRINGi4932.YGL065C.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Proteomic databases

MaxQBiP43636.
PaxDbiP43636.
PeptideAtlasiP43636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL065C; YGL065C; YGL065C.
GeneIDi852815.
KEGGisce:YGL065C.

Organism-specific databases

CYGDiYGL065c.
SGDiS000003033. ALG2.

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00550000075033.
HOGENOMiHOG000177048.
InParanoidiP43636.
KOiK03843.
OMAiGETGWLR.
OrthoDBiEOG7G4QQG.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:MONOMER-7186.
YEAST:YGL065C-MONOMER.
ReactomeiREACT_250523. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

NextBioi972351.
PROiP43636.

Gene expression databases

GenevestigatoriP43636.

Family and domain databases

InterProiIPR027054. ALG2.
IPR001296. Glyco_trans_1.
IPR028098. Glyco_trans_4_N.
[Graphical view]
PANTHERiPTHR12526:SF221. PTHR12526:SF221. 1 hit.
PfamiPF13439. Glyco_transf_4. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Biosynthesis of asparagine-linked oligosaccharides in Saccharomyces cerevisiae: the alg2 mutation."
    Jackson B.J., Kukuruzinska M.A., Robbins P.
    Glycobiology 3:357-364(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
    Feuermann M., de Montigny J., Potier S., Souciet J.-L.
    Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis."
    O'Reilly M.K., Zhang G., Imperiali B.
    Biochemistry 45:9593-9603(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, MUTAGENESIS OF GLU-335 AND GLU-343.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum."
    Gao X.-D., Nishikawa A., Dean N.
    Glycobiology 14:559-570(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALG1, SUBCELLULAR LOCATION.
  9. "A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis."
    Thiel C., Schwarz M., Peng J., Grzmil M., Hasilik M., Braulke T., Kohlschuetter A., von Figura K., Lehle L., Koerner C.
    J. Biol. Chem. 278:22498-22505(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiALG2_YEAST
AccessioniPrimary (citable) accession number: P43636
Secondary accession number(s): D6VU76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1840 molecules/cell in log phase SD medium.1 Publication

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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.