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P32906

- MNS1_YEAST

UniProt

P32906 - MNS1_YEAST

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Protein

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

Gene

MNS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 Man5GlcNAc2.1 Publication

Catalytic activityi

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.1 Publication

Cofactori

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  2. protein deglycosylation involved in glycoprotein catabolic process Source: SGD
  3. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciYEAST:YJR131W-MONOMER.
BRENDAi3.2.1.113. 984.
ReactomeiREACT_189184. ER Quality Control Compartment (ERQC).

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MNS1
Ordered Locus Names:YJR131W
ORF Names:J2110
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJR131w.
SGDiS000003892. MNS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence Analysis
Transmembranei5 – 2420Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini25 – 354330LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidasePRO_0000210319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi96 – 961N-linked (GlcNAc...)Curated
Glycosylationi155 – 1551N-linked (GlcNAc...)Curated
Glycosylationi224 – 2241N-linked (GlcNAc...)Curated
Disulfide bondi340 ↔ 385
Disulfide bondi468 ↔ 471

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP32906.
PaxDbiP32906.

Expressioni

Gene expression databases

GenevestigatoriP32906.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
YBR296C-AQ8TGU51EBI-11094,EBI-2042814

Protein-protein interaction databases

BioGridi33886. 35 interactions.
DIPiDIP-1441N.
IntActiP32906. 6 interactions.
MINTiMINT-386600.
STRINGi4932.YJR131W.

Structurei

Secondary structure

1
549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 5622Combined sources
Beta strandi61 – 644Combined sources
Turni65 – 684Combined sources
Beta strandi69 – 713Combined sources
Helixi84 – 9714Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 11817Combined sources
Beta strandi125 – 1295Combined sources
Helixi130 – 15122Combined sources
Helixi156 – 17116Combined sources
Helixi172 – 1754Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi184 – 1874Combined sources
Turni188 – 1903Combined sources
Helixi199 – 2013Combined sources
Helixi205 – 2084Combined sources
Helixi212 – 22211Combined sources
Helixi225 – 2328Combined sources
Helixi235 – 2428Combined sources
Helixi244 – 2485Combined sources
Beta strandi253 – 2564Combined sources
Turni258 – 2603Combined sources
Turni272 – 2743Combined sources
Helixi275 – 28814Combined sources
Helixi291 – 30717Combined sources
Beta strandi309 – 3113Combined sources
Turni313 – 3153Combined sources
Beta strandi318 – 3203Combined sources
Turni324 – 3285Combined sources
Beta strandi334 – 3363Combined sources
Helixi337 – 3415Combined sources
Helixi342 – 35110Combined sources
Helixi356 – 3594Combined sources
Helixi372 – 39019Combined sources
Beta strandi399 – 4035Combined sources
Beta strandi417 – 4237Combined sources
Helixi425 – 4273Combined sources
Helixi435 – 44713Combined sources
Helixi451 – 46717Combined sources
Beta strandi468 – 4703Combined sources
Turni474 – 4763Combined sources
Beta strandi482 – 4898Combined sources
Helixi498 – 5025Combined sources
Helixi504 – 5118Combined sources
Beta strandi520 – 5234Combined sources
Beta strandi529 – 5313Combined sources
Helixi535 – 5406Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DL2X-ray1.54A34-549[»]
1G6IX-ray1.59A1-549[»]
ProteinModelPortaliP32906.
SMRiP32906. Positions 34-549.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32906.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300315.
GeneTreeiENSGT00390000016529.
HOGENOMiHOG000181987.
InParanoidiP32906.
KOiK01230.
OMAiKHLVTYT.
OrthoDBiEOG75TMND.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.

Sequencei

Sequence statusi: Complete.

P32906-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNSVGISIA TIVAIIAAIY YVPWYEHFER KSPGAGEMRD RIESMFLESW
60 70 80 90 100
RDYSKHGWGY DVYGPIEHTS HNMPRGNQPL GWIIVDSVDT LMLMYNSSTL
110 120 130 140 150
YKSEFEAEIQ RSEHWINDVL DFDIDAEVNV FETTIRMLGG LLSAYHLSDV
160 170 180 190 200
LEVGNKTVYL NKAIDLGDRL ALAFLSTQTG IPYSSINLHS GQAVKNHADG
210 220 230 240 250
GASSTAEFTT LQMEFKYLAY LTGNRTYWEL VERVYEPLYK NNDLLNTYDG
260 270 280 290 300
LVPIYTFPDT GKFGASTIRF GSRGDSFYEY LLKQYLLTHE TLYYDLYRKS
310 320 330 340 350
MEGMKKHLLA QSKPSSLWYI GEREQGLHGQ LSPKMDHLVC FMGGLLASGS
360 370 380 390 400
TEGLSIHEAR RRPFFSLSLE RKSDWDLAKG ITDTCYQMYK QSSSGLAPEI
410 420 430 440 450
VVFNDGNIKQ DGWWRSSVGD FFVKPLDRHN LQRPETVESI MFMYHLSHDH
460 470 480 490 500
KYREWGAEIA TSFFENTCVD CNDPKLRRFT SLSDCITLPT KKSNNMESFW
510 520 530 540
LAETLKYLYI LFLDEFDLTK VVFNTEAHPF PVLDEEILKS QSLTTGWSL
Length:549
Mass (Da):63,057
Last modified:October 1, 1993 - v1
Checksum:iB85FF351900A9BB2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401D → Y.
Natural varianti376 – 3761D → L.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63598 Genomic DNA. Translation: AAA34799.1.
Z49631 Genomic DNA. Translation: CAA89662.1.
BK006943 Genomic DNA. Translation: DAA08915.1.
PIRiA39345.
RefSeqiNP_012665.3. NM_001181789.3.

Genome annotation databases

EnsemblFungiiYJR131W; YJR131W; YJR131W.
GeneIDi853595.
KEGGisce:YJR131W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63598 Genomic DNA. Translation: AAA34799.1 .
Z49631 Genomic DNA. Translation: CAA89662.1 .
BK006943 Genomic DNA. Translation: DAA08915.1 .
PIRi A39345.
RefSeqi NP_012665.3. NM_001181789.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DL2 X-ray 1.54 A 34-549 [» ]
1G6I X-ray 1.59 A 1-549 [» ]
ProteinModelPortali P32906.
SMRi P32906. Positions 34-549.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33886. 35 interactions.
DIPi DIP-1441N.
IntActi P32906. 6 interactions.
MINTi MINT-386600.
STRINGi 4932.YJR131W.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

Proteomic databases

MaxQBi P32906.
PaxDbi P32906.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR131W ; YJR131W ; YJR131W .
GeneIDi 853595.
KEGGi sce:YJR131W.

Organism-specific databases

CYGDi YJR131w.
SGDi S000003892. MNS1.

Phylogenomic databases

eggNOGi NOG300315.
GeneTreei ENSGT00390000016529.
HOGENOMi HOG000181987.
InParanoidi P32906.
KOi K01230.
OMAi KHLVTYT.
OrthoDBi EOG75TMND.

Enzyme and pathway databases

BioCyci YEAST:YJR131W-MONOMER.
BRENDAi 3.2.1.113. 984.
Reactomei REACT_189184. ER Quality Control Compartment (ERQC).

Miscellaneous databases

EvolutionaryTracei P32906.
NextBioi 974409.
PROi P32906.

Gene expression databases

Genevestigatori P32906.

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiMNS1_YEAST
AccessioniPrimary (citable) accession number: P32906
Secondary accession number(s): D6VWU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 26, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8260 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3