Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32906 (MNS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
EC=3.2.1.113

Alternative name(s):
ER alpha-1,2-mannosidase
Man(9)-alpha-mannosidase

Gene names

Name:	MNS1
Ordered Locus Names:	YJR131W
ORF Names:	J2110

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	549 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in glycoprotein quality control as it is important for the targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man₉GlcNAc₂ to produce Man₈GlcNAc₂, but at high enzyme concentrations it further trims the carbohydrates to Man₅GlcNAc₂. Ref.4
Catalytic activity	Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man₉(GlcNAc)₂. Ref.4
Cofactor	Calcium.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Disruption phenotype	No visible phenotype. Ref.1
Miscellaneous	Present with 8260 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype PubMed 8905927. Source: SGD protein deglycosylation involved in glycoprotein catabolic process Inferred from mutant phenotype PubMed 9732283. Source: SGD protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	endoplasmic reticulum Inferred from direct assay PubMed 8864657. Source: SGD endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YBR296C-A	Q8TGU5	1	EBI-11094,EBI-2042814

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 549

549

Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase

PRO_0000210319

Regions

Topological domain

1 – 4

Cytoplasmic Potential

Transmembrane

5 – 24

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

25 – 354

330

Lumenal Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Probable

Glycosylation

155

N-linked (GlcNAc...) Probable

Glycosylation

224

N-linked (GlcNAc...) Probable

Disulfide bond

340 ↔ 385

Disulfide bond

468 ↔ 471

Natural variations

Natural variant

D → Y.

Natural variant

376

D → L.

Secondary structure

549

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32906 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: B85FF351900A9BB2
Show »

FASTA

549

63,057

        10         20         30         40         50         60 
MKNSVGISIA TIVAIIAAIY YVPWYEHFER KSPGAGEMRD RIESMFLESW RDYSKHGWGY 

        70         80         90        100        110        120 
DVYGPIEHTS HNMPRGNQPL GWIIVDSVDT LMLMYNSSTL YKSEFEAEIQ RSEHWINDVL 

       130        140        150        160        170        180 
DFDIDAEVNV FETTIRMLGG LLSAYHLSDV LEVGNKTVYL NKAIDLGDRL ALAFLSTQTG 

       190        200        210        220        230        240 
IPYSSINLHS GQAVKNHADG GASSTAEFTT LQMEFKYLAY LTGNRTYWEL VERVYEPLYK 

       250        260        270        280        290        300 
NNDLLNTYDG LVPIYTFPDT GKFGASTIRF GSRGDSFYEY LLKQYLLTHE TLYYDLYRKS 

       310        320        330        340        350        360 
MEGMKKHLLA QSKPSSLWYI GEREQGLHGQ LSPKMDHLVC FMGGLLASGS TEGLSIHEAR 

       370        380        390        400        410        420 
RRPFFSLSLE RKSDWDLAKG ITDTCYQMYK QSSSGLAPEI VVFNDGNIKQ DGWWRSSVGD 

       430        440        450        460        470        480 
FFVKPLDRHN LQRPETVESI MFMYHLSHDH KYREWGAEIA TSFFENTCVD CNDPKLRRFT 

       490        500        510        520        530        540 
SLSDCITLPT KKSNNMESFW LAETLKYLYI LFLDEFDLTK VVFNTEAHPF PVLDEEILKS 


QSLTTGWSL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase." Camirand A., Heysen A., Grondin B., Herscovics A. J. Biol. Chem. 266:15120-15127(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-51; 226-233; 241-259; 314-323 AND 369-383, DISRUPTION PHENOTYPE.
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported." Herscovics A., Romero P.A., Tremblay L.O. Glycobiology 12:14G-15G(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
[5]	"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].
[6]	"Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control." Vallee F., Lipari F., Yip P., Sleno B., Herscovics A., Howell P.L. EMBO J. 19:581-588(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 34-549.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63598 Genomic DNA. Translation: AAA34799.1.
Z49631 Genomic DNA. Translation: CAA89662.1.
BK006943 Genomic DNA. Translation: DAA08915.1.

PIR

A39345.

RefSeq

NP_012665.3. NM_001181789.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DL2	X-ray	1.54	A	34-549	[»]
1G6I	X-ray	1.59	A	1-549	[»]

ProteinModelPortal

P32906.

SMR

P32906. Positions 34-549.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1441N.

IntAct

P32906. 6 interactions.

MINT

MINT-386600.

STRING

4932.YJR131W.

Protein family/group databases

CAZy

GH47. Glycoside Hydrolase Family 47.

Proteomic databases

PaxDb

P32906.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJR131W; YJR131W; YJR131W.

GeneID

853595.

KEGG

sce:YJR131W.
sce:YJR134C.

Organism-specific databases

CYGD

YJR131w.

SGD

S000003892. MNS1.

Phylogenomic databases

eggNOG

NOG300315.

GeneTree

ENSGT00390000016529.

HOGENOM

HOG000181987.

K01230.

OMA

RLMPAFS.

OrthoDB

EOG4WQ4BK.

Enzyme and pathway databases

BRENDA

3.2.1.113. 984.

UniPathway

UPA00378.

Gene expression databases

Genevestigator

P32906.

GermOnline

YJR131W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.50.10.50. 1 hit.

InterPro

IPR001382. Glyco_hydro_47.
[Graphical view]

PANTHER

PTHR11742. PTHR11742. 1 hit.

Pfam

PF01532. Glyco_hydro_47. 1 hit.
[Graphical view]

PRINTS

PR00747. GLYHDRLASE47.

SUPFAM

SSF48225. Glyco_hydro_47. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P32906.

NextBio

974409.

Entry information

Entry name

MNS1_YEAST

Accession

Primary (citable) accession number: P32906
Secondary accession number(s): D6VWU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome X

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents