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Q9P7C3 (MNS1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·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
ORF Names:SPAC2E1P5.01c, SPAPB1E7.13c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length521 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 trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 with low efficiency. Ref.2

Catalytic activity

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

Cofactor

Calcium By similarity.

Enzyme regulation

Inhibited by kifunensine. Ref.2

Pathway

Protein modification; protein glycosylation.

Subcellular location

Membrane; Single-pass type II membrane protein Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
PRO_0000210320

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 3123Helical; Signal-anchor for type II membrane protein; Potential
Topological domain32 – 521490Lumenal Potential

Amino acid modifications

Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1671N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4991N-linked (GlcNAc...) Potential
Disulfide bond330 ↔ 373 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9P7C3 [UniParc].

Last modified March 29, 2004. Version 2.
Checksum: 742E325D05EC8936

FASTA52160,813
        10         20         30         40         50         60 
MVKRRTVKYF LRRILALFVL CVPIYYLYTT VQRPPGYTKL KGSTRRKALI KKTFIESWTD 

        70         80         90        100        110        120 
YETYGWGKDE YYPIIKRGRN YLRKGMGWMI IDSLDTMMIM GLDEQVLRAR EWVNNSLTWN 

       130        140        150        160        170        180 
QDDEEVSVFE TTIRILGGLL SSYHLSQDKL YLDRAVDLAD RLLAAYNTST GLPRSNVNLG 

       190        200        210        220        230        240 
TRKSRKRTRE YFVSTAESGT VQMELRYLSY LTGDPKYWIT ADKTMEVLLG DATWSHTGLV 

       250        260        270        280        290        300 
PITVNLITGA YVGRNIRLGS HGDSYYEYLL KQDLQLFSSG TVYRKAFDLS VDGIIEYLLN 

       310        320        330        340        350        360 
YTTPNHFAYI AELPGGLEHA QLPKMDHLVC FLPGTLMWGA TNGTSLEAAR TSKNWGTRQE 

       370        380        390        400        410        420 
RDVKLAQELM RTCYEMYNMT ATGLAPEIVF FDVDQTKNEI YSKRRDQHNL MRPETVESLF 

       430        440        450        460        470        480 
ILYRITRDEI YREWGWNIFV SFLRYSRLPG RDAFTCLDSV ESKKVKDQRD KTESFWFAET 

       490        500        510        520 
LKYLYLLFED DFSILPLTNY TFNTEAHPFP NIENNMDLYT V

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradation."
Movsichoff F., Castro O.A., Parodi A.J.
Mol. Biol. Cell 16:4714-4724(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAC36930.1.
RefSeqNP_594139.2. NM_001019563.2.

3D structure databases

ProteinModelPortalQ9P7C3.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4705108.
STRING4896.SPAC2E1P5.01c-1.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC2E1P5.01c.1; SPAC2E1P5.01c.1:pep; SPAC2E1P5.01c.
GeneID2541719.
KEGGspo:SPAC2E1P5.01c.

Organism-specific databases

PomBaseSPAC2E1P5.01c.

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181987.
KOK01230.
OMAGGKDFKP.
OrthoDBEOG4WQ4BK.

Enzyme and pathway databases

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...

Other

NextBio20802810.

Entry information

Entry nameMNS1_SCHPO
AccessionPrimary (citable) accession number: Q9P7C3
Secondary accession number(s): Q9C0Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: May 29, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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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