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Q18788 (MAN12_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase C52E4.5
EC=3.2.1.113
Alternative name(s):
Processing alpha-1,2-mannosidase C52E4.5
Short name=Alpha-1,2-mannosidase C52E4.5
Gene names
ORF Names:C52E4.5
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Membrane; Single-pass type II membrane protein.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: Q18788-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform b (identifier: Q18788-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MIDVSSSITNMNVTIVESFLDFFKILAYVSKFSSWKEPNKTTFPHAM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 590590Mannosyl-oligosaccharide 1,2-alpha-mannosidase C52E4.5
PRO_0000248514

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 590560Lumenal Potential

Amino acid modifications

Glycosylation1561N-linked (GlcNAc...) Ref.3
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Ref.2 Ref.3
Glycosylation4021N-linked (GlcNAc...) Ref.3

Natural variations

Alternative sequence11M → MIDVSSSITNMNVTIVESFL DFFKILAYVSKFSSWKEPNK TTFPHAM in isoform b.
VSP_044102

Sequences

Sequence LengthMass (Da)Tools
Isoform a [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B0714A3671204843

FASTA59066,950
        10         20         30         40         50         60 
MKTVRFNKQA LAILAACFIF LLCVVCYFSA SSESHNAVVV GERARGHIAV RDVENRHLAE 

        70         80         90        100        110        120 
EKHAVIHAKT VGKIERVVSQ EKVEILRPAR VESKPPGEKT STEPEETGVG KAPIQTSEGL 

       130        140        150        160        170        180 
EKLIGKIHYE NKDEENDLRR QKVKEMMIHA WEGYKNYSWG ANELRPMSKK PNSQNIFGGS 

       190        200        210        220        230        240 
QMPATIVDAA DTLFIMDLKD KYKEARDYIE NNFSMAKSTS TLSVFETTIR FLGGLLSLYA 

       250        260        270        280        290        300 
LTQESFYIEK AREVGEALLP AFNTPSGIPK SNLDVASKHA SNYGWANGGQ SILSEIGSLH 

       310        320        330        340        350        360 
LEFLYLSRIS NAPIFEKKVK KVRDALEKAE KPNGLYSNYI NPDTGKFTGS HMSLGALGDS 

       370        380        390        400        410        420 
FYEYLIKSYV QSNYTDTQAK NMYWDVSDAI QKHMIKVSKQ SNLTYTVELN NGQAQHKMGH 

       430        440        450        460        470        480 
LACFVPGMFA LQAINEDTEE EKLRIMTLAE ELAKTCHESY IRSETHIGPE MFYFNERDEA 

       490        500        510        520        530        540 
TSKHSENGYI QRPEVIEGWF YLWRLTGKTM YRDWVWDAVQ AIEKYCRVDS GFTGLQNVYN 

       550        560        570        580        590 
PKAGREDVMQ SFFLAEFLKY AYLTFADESL ISLDKWVFNT EAHPVPVLTN

« Hide

Isoform b [UniParc].

Checksum: B012A1EEEA43463B
Show »

FASTA63672,204

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
Strain: Bristol N2.
[2]"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
Nat. Biotechnol. 21:667-672(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-373, MASS SPECTROMETRY.
Strain: Bristol N2.
[3]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156; ASN-373 AND ASN-402, MASS SPECTROMETRY.
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z78012 Genomic DNA. Translation: CAB01415.1.
Z78012 Genomic DNA. Translation: CBW48349.1.
PIRT20153.
RefSeqNP_001256388.1. NM_001269459.1.
NP_001256389.1. NM_001269460.1.

3D structure databases

HSSPHSSP built from PDB template 1X9D based on UniProtKB Q9UKM7.
ProteinModelPortalQ18788.
SMRQ18788. Positions 124-588.
ModBaseSearch...

Protein-protein interaction databases

STRING6239.C52E4.5.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Proteomic databases

PaxDbQ18788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC52E4.5a; C52E4.5a; C52E4.5.
GeneID179642.
KEGGcel:CELE_C52E4.5.
UCSCC52E4.5. c. elegans.

Organism-specific databases

CTD179642.
WormBaseC52E4.5a; CE08947; WBGene00008258.
C52E4.5b; CE45297; WBGene00008258.

Phylogenomic databases

eggNOGNOG300315.
GeneTreeENSGT00390000016529.
HOGENOMHOG000181987.
InParanoidQ18788.
OMAYLIKSYV.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ18788.

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

NextBio906268.

Entry information

Entry nameMAN12_CAEEL
AccessionPrimary (citable) accession number: Q18788
Secondary accession number(s): E1B6T6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents