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P43636 (ALG2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ALG2
Ordered Locus Names:YGL065C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mannosylates Man2GlcNAc(2)-dolichol diphosphate and Man1GlcNAc(2)-dolichol diphosphate to form Man3GlcNAc(2)-dolichol diphosphate. Ref.6

Catalytic activity

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. Ref.6

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. Ref.6

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with ALG1. Ref.8

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.8.

Miscellaneous

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

Sequence similarities

Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ALG1P166612EBI-2459,EBI-2206309

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Alpha-1,3/1,6-mannosyltransferase ALG2
PRO_0000080271

Regions

Transmembrane64 – 8421Helical; Potential
Transmembrane112 – 13221Helical; Potential
Transmembrane443 – 46321Helical; Potential

Amino acid modifications

Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis3351E → A: Severly affects activity, especially the second mannosylation step. Ref.6
Mutagenesis3431E → A: No activity. Ref.6
Sequence conflict81T → S in CAA61199. Ref.1
Sequence conflict237 – 2382KA → NG in CAA61199. Ref.1
Sequence conflict3021T → A in CAA61199. Ref.1
Sequence conflict4571M → I in CAA61199. Ref.1
Sequence conflict470 – 50334FLFMA…PYEEI → SYLWPLLWYYILRTTYGEFT GHLYSLSPTLMKKYNVYLNK QCIPPEEKIIYIGEEISKCK Ref.1

Sequences

Sequence LengthMass (Da)Tools
P43636 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 1200E1C8EA023DD4

FASTA50358,047
        10         20         30         40         50         60 
MIEKDKRTIA FIHPDLGIGG AERLVVDAAL GLQQQGHSVI IYTSHCDKSH CFEEVKNGQL 

        70         80         90        100        110        120 
KVEVYGDFLP TNFLGRFFIV FATIRQLYLV IQLILQKKVN AYQLIIIDQL STCIPLLHIF 

       130        140        150        160        170        180 
SSATLMFYCH FPDQLLAQRA GLLKKIYRLP FDLIEQFSVS AADTVVVNSN FTKNTFHQTF 

       190        200        210        220        230        240 
KYLSNDPDVI YPCVDLSTIE IEDIDKKFFK TVFNEGDRFY LSINRFEKKK DVALAIKAFA 

       250        260        270        280        290        300 
LSEDQINDNV KLVICGGYDE RVAENVEYLK ELQSLADEYE LSHTTIYYQE IKRVSDLESF 

       310        320        330        340        350        360 
KTNNSKIIFL TSISSSLKEL LLERTEMLLY TPAYEHFGIV PLEAMKLGKP VLAVNNGGPL 

       370        380        390        400        410        420 
ETIKSYVAGE NESSATGWLK PAVPIQWATA IDESRKILQN GSVNFERNGP LRVKKYFSRE 

       430        440        450        460        470        480 
AMTQSFEENV EKVIWKEKKY YPWEIFGISF SNFILHMAFI KILPNNPWPF LFMATFMVLY 

       490        500 
FKNYLWGIYW AFVFALSYPY EEI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X87947 Genomic DNA. Translation: CAA61199.1.
Z72587 Genomic DNA. Translation: CAA96768.1.
BK006941 Genomic DNA. Translation: DAA08037.1.
PIRS64069.
RefSeqNP_011450.1. NM_001180930.1.

3D structure databases

ProteinModelPortalP43636.
SMRP43636. Positions 215-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33182. 8 interactions.
DIPDIP-5401N.
IntActP43636. 4 interactions.
MINTMINT-523155.
STRING4932.YGL065C.

Protein family/group databases

CAZyGT4. Glycosyltransferase Family 4.

Proteomic databases

PaxDbP43636.
PeptideAtlasP43636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL065C; YGL065C; YGL065C.
GeneID852815.
KEGGsce:YGL065C.

Organism-specific databases

CYGDYGL065c.
SGDS000003033. ALG2.

Phylogenomic databases

eggNOGCOG0438.
GeneTreeENSGT00550000075033.
HOGENOMHOG000177048.
KOK03843.
OMAAVCAYVR.
OrthoDBEOG7G4QQG.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-7186.
YEAST:YGL065C-MONOMER.
ReactomeREACT_85873. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorP43636.

Family and domain databases

InterProIPR027054. ALG2.
IPR001296. Glyco_trans_1.
[Graphical view]
PANTHERPTHR12526:SF22. PTHR12526:SF22. 1 hit.
PfamPF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972351.
PROP43636.

Entry information

Entry nameALG2_YEAST
AccessionPrimary (citable) accession number: P43636
Secondary accession number(s): D6VU76
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways