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P32906 (MNS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YBR296C-AQ8TGU51EBI-11094,EBI-2042814

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 549549Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
PRO_0000210319

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2420Helical; Signal-anchor for type II membrane protein; Potential
Topological domain25 – 354330Lumenal Potential

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Probable
Glycosylation1551N-linked (GlcNAc...) Probable
Glycosylation2241N-linked (GlcNAc...) Probable
Disulfide bond340 ↔ 385
Disulfide bond468 ↔ 471

Natural variations

Natural variant401D → Y.
Natural variant3761D → L.

Secondary structure

.................................................................................... 549
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32906 [UniParc].

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

FASTA54963,057
        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' 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. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
PIRA39345.
RefSeqNP_012665.3. NM_001181789.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DL2X-ray1.54A34-549[»]
1G6IX-ray1.59A1-549[»]
ProteinModelPortalP32906.
SMRP32906. Positions 34-549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33886. 35 interactions.
DIPDIP-1441N.
IntActP32906. 6 interactions.
MINTMINT-386600.
STRING4932.YJR131W.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Proteomic databases

MaxQBP32906.
PaxDbP32906.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR131W; YJR131W; YJR131W.
GeneID853595.
KEGGsce:YJR131W.

Organism-specific databases

CYGDYJR131w.
SGDS000003892. MNS1.

Phylogenomic databases

eggNOGNOG300315.
GeneTreeENSGT00390000016529.
HOGENOMHOG000181987.
KOK01230.
OMAKHLVTYT.
OrthoDBEOG75TMND.

Enzyme and pathway databases

BioCycYEAST:YJR131W-MONOMER.
BRENDA3.2.1.113. 984.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorP32906.

Family and domain databases

Gene3D1.50.10.50. 1 hit.
InterProIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERPTHR11742. PTHR11742. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
SUPFAMSSF48225. SSF48225. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32906.
NextBio974409.
PROP32906.

Entry information

Entry nameMNS1_YEAST
AccessionPrimary (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: May 14, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries