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P32906

- MNS1_YEAST

UniProt

P32906 - MNS1_YEAST

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
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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

    Calcium.

    Pathwayi

    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

    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).
    UniPathwayiUPA00378.

    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

    GO - Cellular componenti

    1. endoplasmic reticulum Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

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

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP32906.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini25 – 354330LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2420Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG300315.
    GeneTreeiENSGT00390000016529.
    HOGENOMiHOG000181987.
    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

    MKNSVGISIA TIVAIIAAIY YVPWYEHFER KSPGAGEMRD RIESMFLESW    50
    RDYSKHGWGY DVYGPIEHTS HNMPRGNQPL GWIIVDSVDT LMLMYNSSTL 100
    YKSEFEAEIQ RSEHWINDVL DFDIDAEVNV FETTIRMLGG LLSAYHLSDV 150
    LEVGNKTVYL NKAIDLGDRL ALAFLSTQTG IPYSSINLHS GQAVKNHADG 200
    GASSTAEFTT LQMEFKYLAY LTGNRTYWEL VERVYEPLYK NNDLLNTYDG 250
    LVPIYTFPDT GKFGASTIRF GSRGDSFYEY LLKQYLLTHE TLYYDLYRKS 300
    MEGMKKHLLA QSKPSSLWYI GEREQGLHGQ LSPKMDHLVC FMGGLLASGS 350
    TEGLSIHEAR RRPFFSLSLE RKSDWDLAKG ITDTCYQMYK QSSSGLAPEI 400
    VVFNDGNIKQ DGWWRSSVGD FFVKPLDRHN LQRPETVESI MFMYHLSHDH 450
    KYREWGAEIA TSFFENTCVD CNDPKLRRFT SLSDCITLPT KKSNNMESFW 500
    LAETLKYLYI LFLDEFDLTK VVFNTEAHPF PVLDEEILKS QSLTTGWSL 549
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOi K01230.
    OMAi KHLVTYT.
    OrthoDBi EOG75TMND.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    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

    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: October 1, 2014
    This is version 138 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
    5. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    6. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3