P43636 (ALG2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ALG2
Ordered Locus Names:	YGL065C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	oligosaccharide-lipid intermediate biosynthetic process Inferred from direct assay Ref.6. Source: SGD protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD
Molecular_function	GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity Inferred from direct assay Ref.6. Source: SGD glycolipid 6-alpha-mannosyltransferase activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALG1	P16661	2	EBI-2459,EBI-2206309

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 503	503	Alpha-1,3/1,6-mannosyltransferase ALG2		PRO_0000080271
Regions
	Transmembrane	64 – 84	21	Helical; Potential
	Transmembrane	112 – 132	21	Helical; Potential
	Transmembrane	443 – 463	21	Helical; Potential
Amino acid modifications
	Modified residue	302	1	Phosphothreonine Ref.10
	Glycosylation	170	1	N-linked (GlcNAc...) Potential
	Glycosylation	303	1	N-linked (GlcNAc...) Potential
	Glycosylation	371	1	N-linked (GlcNAc...) Potential
	Glycosylation	400	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	335	1	E → A: Severly affects activity, especially the second mannosylation step. Ref.6
	Mutagenesis	343	1	E → A: No activity. Ref.6
	Sequence conflict	8	1	T → S in CAA61199. Ref.1
	Sequence conflict	237 – 238	2	KA → NG in CAA61199. Ref.1
	Sequence conflict	302	1	T → A in CAA61199. Ref.1
	Sequence conflict	457	1	M → I in CAA61199. Ref.1
	Sequence conflict	470 – 503	34	FLFMA…PYEEI → SYLWPLLWYYILRTTYGEFT GHLYSLSPTLMKKYNVYLNK QCIPPEEKIIYIGEEISKCK Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P43636 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 1200E1C8EA023DD4	FASTA	503	58,047
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[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.
[10]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, MASS SPECTROMETRY.
+	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.
PIR	S64069.
RefSeq	NP_011450.1. NM_001180930.1.
3D structure databases
ProteinModelPortal	P43636.
SMR	P43636. Positions 219-363.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5401N.
IntAct	P43636. 4 interactions.
MINT	MINT-523155.
STRING	4932.YGL065C.
Protein family/group databases
CAZy	GT4. Glycosyltransferase Family 4.
Proteomic databases
PaxDb	P43636.
PeptideAtlas	P43636.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL065C; YGL065C; YGL065C.
GeneID	852815.
KEGG	sce:YGL065C.
Organism-specific databases
CYGD	YGL065c.
SGD	S000003033. ALG2.
Phylogenomic databases
eggNOG	COG0438.
GeneTree	ENSGT00550000075033.
HOGENOM	HOG000177048.
KO	K03843.
OMA	KIWTAHY.
OrthoDB	EOG47DDQK.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-7186.
Reactome	REACT_85873. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
Genevestigator	P43636.
GermOnline	YGL065C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR027054. ALG2. IPR001296. Glyco_trans_1. [Graphical view]
PANTHER	PTHR12526:SF22. PTHR12526:SF22. 1 hit.
Pfam	PF00534. Glycos_transf_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972351.

Entry information

Entry name

ALG2_YEAST

Accession

Primary (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:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program