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Q12563 (MNS1B_ASPSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:mns1B
Synonyms:msdS
OrganismAspergillus saitoi (Aspergillus phoenicis)
Taxonomic identifier5063 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

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

Pathway

Protein modification; protein glycosylation.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasmic vesicle lumen By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasmic vesicle
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological_processprotein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasmic membrane-bounded vesicle lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 513492Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B
PRO_0000394821

Sites

Active site3771Proton donor By similarity

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Disulfide bond334 ↔ 363 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12563 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0FDAB2CB27E93724

FASTA51355,875
        10         20         30         40         50         60 
MHLPSLSLSL TALAIASPSA AYPHFGSSQP VLHSSSDTTQ SRADAIKAAF SHAWDGYLQY 

        70         80         90        100        110        120 
AFPHDELHPV SNGYGDSRNG WGASAVDALS TAVIMRNATI VNQILDHVGK IDYSKTNTTV 

       130        140        150        160        170        180 
SLFETTIRYL GGMLSGYDLL KGPVSDLVQN SSKIDVLLTQ SKNLADVLKF AFDTPSGVPY 

       190        200        210        220        230        240 
NNLNITSGGN DGAKTNGLAV TGTLALEWTR LSDLTGDTTY ADLSQKAESY LLNPQPKSAE 

       250        260        270        280        290        300 
PFPGLVGSNI NISNGQFTDA QVSWNGGDDS YYEYLIKMYV YDPKRFGLYK DRWVAAAQST 

       310        320        330        340        350        360 
MQHLASHPSS RPDLTFLASY NNGTLGLSSQ HLTCFDGGSF LLGGTVLNRT DFINFGLDLV 

       370        380        390        400        410        420 
SGCHDTYNST LTGIGPESFS WDTSDIPSSQ QSLYEKAGFY ITSGAYILRP EVIESFYYAW 

       430        440        450        460        470        480 
RVTGQETYRD WIWSAFSAVN DYCRTSSGFS GLTDVNAANG GSRYDNQESF LFAEVMKYSY 

       490        500        510 
MAFAEDAAWQ VQPGSGNQFV FNTEAHPVRV SST

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D49827 mRNA. Translation: BAA08634.1.

3D structure databases

HSSPHSSP built from PDB template 1KRE based on UniProtKB P31723.
ProteinModelPortalQ12563.
SMRQ12563. Positions 38-511.
ModBaseSearch...

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.
mycoCLAPMSD47S_ASPPH.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ12563.
UniPathwayUPA00378.

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. Glyco_hydro_47. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMNS1B_ASPSA
AccessionPrimary (citable) accession number: Q12563
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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