P16661 (ALG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chitobiosyldiphosphodolichol beta-mannosyltransferase
EC=2.4.1.142

Alternative name(s):
Asparagine-linked glycosylation protein 1
Beta-1,4-mannosyltransferase
GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
GDP-mannose-dolichol diphosphochitobiose mannosyltransferase

Gene names

Name:	ALG1
Ordered Locus Names:	YBR110W
ORF Names:	YBR0906

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	449 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man5 intermediate on the cytoplasmic surface of the ER.
Catalytic activity	GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-1,4-D-mannosylchitobiosyldiphosphodolichol.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Homodimer. Interacts with ALG2 and ALG11. Ref.7
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein Potential Ref.5.
Miscellaneous	Present with 1890 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 33 subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	oligosaccharide-lipid intermediate biosynthetic process Inferred from mutant phenotype PubMed 7037780. Source: SGD protein N-linked glycosylation Inferred from mutant phenotype PubMed 6369318. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from physical interaction Ref.7. Source: SGD endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from sequence or structural similarity Ref.1. Source: SGD
Molecular_function	beta-1,4-mannosyltransferase activity Inferred from direct assay PubMed 6368538. Source: SGD chitobiosyldiphosphodolichol beta-mannosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALG11	P53954	2	EBI-2206309,EBI-2497
ALG2	P43636	2	EBI-2206309,EBI-2459

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Chitobiosyldiphosphodolichol beta-mannosyltransferase		PRO_0000080259
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 34	27	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	35 – 449	415	Lumenal Potential
	Region	435 – 449	15	Required for oligomerization
	Motif	21 – 32	12	Dolichol recognition Potential
Amino acid modifications
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	199	1	N-linked (GlcNAc...) Potential
	Glycosylation	425	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	278	1	E → K: Abolishes enzymatic activity. Ref.7
	Mutagenesis	310	1	G → D: Abolishes enzymatic activity. Ref.7
	Mutagenesis	356	1	H → Q: Abolishes enzymatic activity. Ref.7
	Mutagenesis	363	1	D → A: No effect on enzymatic activity. Ref.7
	Mutagenesis	370	1	D → A: No effect on enzymatic activity. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P16661 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 662E0CB1632DED5A	FASTA	449	51,929
	10 20 30 40 50 60 MFLEIPRWLL ALIILYLSIP LVVYYVIPYL FYGNKSTKKR IIIFVLGDVG HSPRICYHAI 70 80 90 100 110 120 SFSKLGWQVE LCGYVEDTLP KIISSDPNIT VHHMSNLKRK GGGTSVIFMV KKVLFQVLSI 130 140 150 160 170 180 FKLLWELRGS DYILVQNPPS IPILPIAVLY KLTGCKLIID WHNLAYSILQ LKFKGNFYHP 190 200 210 220 230 240 LVLISYMVEM IFSKFADYNL TVTEAMRKYL IQSFHLNPKR CAVLYDRPAS QFQPLAGDIS 250 260 270 280 290 300 RQKALTTKAF IKNYIRDDFD TEKGDKIIVT STSFTPDEDI GILLGALKIY ENSYVKFDSS 310 320 330 340 350 360 LPKILCFITG KGPLKEKYMK QVEEYDWKRC QIEFVWLSAE DYPKLLQLCD YGVSLHTSSS 370 380 390 400 410 420 GLDLPMKILD MFGSGLPVIA MNYPVLDELV QHNVNGLKFV DRRELHESLI FAMKDADLYQ 430 440 KLKKNVTQEA ENRWQSNWER TMRDLKLIH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence and transcript heterogeneity of the yeast gene ALG1, an essential mannosyltransferase involved in N-glycosylation." Albright C.F., Robbins P.W. J. Biol. Chem. 265:7042-7049(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of a 70 kb region on the right arm of yeast chromosome II." Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H. Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"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].
[7]	"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: OLIGOMERIZATION, INTERACTION WITH ALG2 AND ALG11, MUTAGENESIS OF GLU-278; GLY-310; HIS-356; ASP-363 AND ASP-370.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05416 Genomic DNA. Translation: AAA66322.1. X78993 Genomic DNA. Translation: CAA55613.1. Z35979 Genomic DNA. Translation: CAA85067.1. BK006936 Genomic DNA. Translation: DAA07229.1.
PIR	A35762.
RefSeq	NP_009668.3. NM_001178458.3.
3D structure databases
ProteinModelPortal	P16661.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-7371N.
IntAct	P16661. 2 interactions.
MINT	MINT-1355815.
STRING	4932.YBR110W.
Protein family/group databases
CAZy	GT33. Glycosyltransferase Family 33.
Proteomic databases
PaxDb	P16661.
PeptideAtlas	P16661.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR110W; YBR110W; YBR110W.
GeneID	852407.
KEGG	sce:YBR110W. sce:YBR112C.
Organism-specific databases
CYGD	YBR110w.
SGD	S000000314. ALG1.
Phylogenomic databases
eggNOG	COG0438.
GeneTree	ENSGT00390000008647.
HOGENOM	HOG000216716.
KO	K03842. K06665.
OMA	KFEAWPE.
OrthoDB	EOG4WWVT5.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-7182.
UniPathway	UPA00378.
Gene expression databases
Genevestigator	P16661.
GermOnline	YBR110W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR026051. ALG1-like. IPR001296. Glyco_trans_1. [Graphical view]
PANTHER	PTHR13036. PTHR13036. 1 hit.
Pfam	PF00534. Glycos_transf_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971252.

Entry information

Entry name

ALG1_YEAST

Accession

Primary (citable) accession number: P16661
Secondary accession number(s): D6VQA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	April 3, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program