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P45700 (MA1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
EC=3.2.1.113
Alternative name(s):
Man(9)-alpha-mannosidase
Short name=Man9-mannosidase
Mannosidase alpha class 1A member 1
Processing alpha-1,2-mannosidase IA
Short name=Alpha-1,2-mannosidase IA
Gene names
Name:Man1a1
Synonyms:Man1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length655 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.

Catalytic activity

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

Cofactor

Calcium.

Enzyme regulation

Inhibited by both 1-deoxymannojirimycin and kifunensine By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein.

Post-translational modification

N-linked glycan at Asn-515 consists of Man(6)-GlcNAc2.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 655655Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
PRO_0000210309

Regions

Topological domain1 – 4343Cytoplasmic Potential
Transmembrane44 – 6421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain65 – 655591Lumenal Potential

Sites

Metal binding6351Calcium

Amino acid modifications

Glycosylation5151N-linked (GlcNAc...) Ref.4
Disulfide bond478 ↔ 510 Ref.4

Secondary structure

1 .................................................................................. 655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45700 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 15AF658364930BF4

FASTA65573,276
        10         20         30         40         50         60 
MPVGGLLPLF SSPGGGGLGS GLGGGLGGGR KGSGPAAFRL TEKFVLLLVF SAFITLCFGA 

        70         80         90        100        110        120 
IFFLPDSSKL LSGVLFHSNP ALQPPAEHKP GLGARAEDAA EGRVRHREEG APGDPGAGLE 

       130        140        150        160        170        180 
DNLARIRENH ERALREAKET LQKLPEEIQR DILLEKEKVA QDQLRDKDLF RGLPKVDFLP 

       190        200        210        220        230        240 
PVGVENREPA DATIREKRAK IKEMMTHAWN NYKRYAWGLN ELKPISKEGH SSSLFGNIKG 

       250        260        270        280        290        300 
ATIVDALDTL FIMGMKTEFQ EAKSWIKKYL DFNVNAEVSV FEVNIRFVGG LLSAYYLSGE 

       310        320        330        340        350        360 
EIFRKKAVEL GVKLLPAFHT PSGIPWALLN MKSGIGRNWP WASGGSSILA EFGTLHLEFM 

       370        380        390        400        410        420 
HLSHLSGDPV FAEKVMKIRT VLNKLDKPEG LYPNYLNPSS GQWGQHHVSV GGLGDSFYEY 

       430        440        450        460        470        480 
LLKAWLMSDK TDLEAKKMYF DAVQAIETHL IRKSSGGLTY IAEWKGGLLE HKMGHLTCFA 

       490        500        510        520        530        540 
GGMFALGADG APEARAQHYL ELGAEIARTC HESYNRTYVK LGPEAFRFDG GVEAIATRQN 

       550        560        570        580        590        600 
EKYYILRPEV IETYMYMWRL THDPKYRTWA WEAVEALESH CRVNGGYSGL RDVYIARESY 

       610        620        630        640        650 
DDVQQSFFLA ETLKYLYLIF SDDDLLPLEH WIFNTEAHPF PILREQKKEI DGKEK

« Hide

References

« Hide 'large scale' references
[1]"Isolation and expression of murine and rabbit cDNAs encoding an alpha 1,2-mannosidase involved in the processing of asparagine-linked oligosaccharides."
Lal A., Schutzbach J.S., Forsee W.T., Neame P.J., Moremen K.W.
J. Biol. Chem. 269:9872-9881(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 424-437, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases."
Tempel W., Karaveg K., Liu Z.-J., Rose J., Wang B.C., Moremen K.W.
J. Biol. Chem. 279:29774-29786(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 178-655, DISULFIDE BOND, CALCIUM-BINDING SITE, GLYCOSYLATION AT ASN-515.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U04299 mRNA. Translation: AAA17747.1.
BC015265 mRNA. Translation: AAH15265.1.
IPIIPI00132493.
PIRA54408.
RefSeqNP_032574.1. NM_008548.4.
UniGeneMm.117294.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NXCX-ray1.51A178-655[»]
ProteinModelPortalP45700.
SMRP45700. Positions 178-644.
ModBaseSearch...

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSiteP45700.

Proteomic databases

PaxDbP45700.
PRIDEP45700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003843; ENSMUSP00000003843; ENSMUSG00000003746.
ENSMUST00000105470; ENSMUSP00000101110; ENSMUSG00000003746.
GeneID17155.
KEGGmmu:17155.

Organism-specific databases

CTD17155.
MGIMGI:104677. Man1a.

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181988.
HOVERGENHBG052389.
InParanoidP45700.
KOK01230.
OMADKPEGLY.
OrthoDBEOG4NVZJW.

Enzyme and pathway databases

BRENDA3.2.1.113. 3474.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP45700.
BgeeP45700.
CleanExMM_MAN1A.
GenevestigatorP45700.
GermOnlineENSMUSG00000003746. Mus musculus.

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

EvolutionaryTraceP45700.
NextBio291418.
SOURCESearch...

Entry information

Entry nameMA1A1_MOUSE
AccessionPrimary (citable) accession number: P45700
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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