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Q12563

- MNS1B_ASPPH

UniProt

Q12563 - MNS1B_ASPPH

Protein

Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B

Gene

mns1B

Organism
Aspergillus phoenicis (Aspergillus saitoi)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.1 Publication

    Catalytic activityi

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

    Cofactori

    Ca2+. Can also use Mg2+, but with lower efficiency By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei377 – 3771Proton donorBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein glycosylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    SABIO-RKQ12563.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH47. Glycoside Hydrolase Family 47.
    mycoCLAPiMSD47S_ASPPH.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B (EC:3.2.1.113)
    Alternative name(s):
    Class I alpha-mannosidase 1B
    Man(9)-alpha-mannosidase 1B
    Gene namesi
    Name:mns1B
    Synonyms:msdS
    OrganismiAspergillus phoenicis (Aspergillus saitoi)
    Taxonomic identifieri5063 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic membrane-bounded vesicle lumen Source: UniProtKB-SubCell
    2. membrane Source: InterPro

    Keywords - Cellular componenti

    Cytoplasmic vesicle

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 513492Mannosyl-oligosaccharide alpha-1,2-mannosidase 1BPRO_0000394821Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi334 ↔ 363By similarity
    Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ12563.
    SMRiQ12563. Positions 38-511.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Signal

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q12563-1 [UniParc]FASTAAdd to Basket

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    MHLPSLSLSL TALAIASPSA AYPHFGSSQP VLHSSSDTTQ SRADAIKAAF    50
    SHAWDGYLQY AFPHDELHPV SNGYGDSRNG WGASAVDALS TAVIMRNATI 100
    VNQILDHVGK IDYSKTNTTV SLFETTIRYL GGMLSGYDLL KGPVSDLVQN 150
    SSKIDVLLTQ SKNLADVLKF AFDTPSGVPY NNLNITSGGN DGAKTNGLAV 200
    TGTLALEWTR LSDLTGDTTY ADLSQKAESY LLNPQPKSAE PFPGLVGSNI 250
    NISNGQFTDA QVSWNGGDDS YYEYLIKMYV YDPKRFGLYK DRWVAAAQST 300
    MQHLASHPSS RPDLTFLASY NNGTLGLSSQ HLTCFDGGSF LLGGTVLNRT 350
    DFINFGLDLV SGCHDTYNST LTGIGPESFS WDTSDIPSSQ QSLYEKAGFY 400
    ITSGAYILRP EVIESFYYAW RVTGQETYRD WIWSAFSAVN DYCRTSSGFS 450
    GLTDVNAANG GSRYDNQESF LFAEVMKYSY MAFAEDAAWQ VQPGSGNQFV 500
    FNTEAHPVRV SST 513
    Length:513
    Mass (Da):55,875
    Last modified:November 1, 1996 - v1
    Checksum:i0FDAB2CB27E93724
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49827 mRNA. Translation: BAA08634.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49827 mRNA. Translation: BAA08634.1 .

    3D structure databases

    ProteinModelPortali Q12563.
    SMRi Q12563. Positions 38-511.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.
    mycoCLAPi MSD47S_ASPPH.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    SABIO-RK Q12563.

    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. "Molecular cloning and nucleotide sequence of the 1,2-alpha-D-mannosidase gene, msdS, from Aspergillus saitoi and expression of the gene in yeast cells."
      Inoue T., Yoshida T., Ichishima E.
      Biochim. Biophys. Acta 1253:141-145(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.

    Entry informationi

    Entry nameiMNS1B_ASPPH
    AccessioniPrimary (citable) accession number: Q12563
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3