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A2AJ15 (MA1B1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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
ER mannosidase 1
Short name=ERMan1
Man9GlcNAc2-specific-processing alpha-mannosidase
Mannosidase alpha class 1B member 1
Gene names
Name:Man1b1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2, but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man5-6GlcNAc2 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

Endoplasmic reticulum membrane; Single-pass type II membrane protein.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 658658Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
PRO_0000396622

Regions

Topological domain1 – 5050Cytoplasmic Potential
Transmembrane51 – 7121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain72 – 658587Lumenal Potential

Sites

Active site2891Proton donor By similarity
Active site4221 By similarity
Active site5581 By similarity

Amino acid modifications

Disulfide bond486 ↔ 515 By similarity

Sequences

Sequence LengthMass (Da)Tools
A2AJ15 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 75BA990FA9B1470B

FASTA65875,150
        10         20         30         40         50         60 
MYPPPAPPPA PHRDFISVTL SLGESYDNSK SRRRRSCWRK WKQLSRLQRN VILFVLGFLI 

        70         80         90        100        110        120 
LCGFLYSLHT ADQWKALSGR PAEVEKMKQE VLPVLPAPQK ESAEQEGFAD ILSQKRQRHF 

       130        140        150        160        170        180 
RRGPPHLQIR PPNTVSKDGM QDDAKEREAA LGKAQQEENT QRTVISWRGA VIEPEQATEL 

       190        200        210        220        230        240 
PYKRAEASIK PLVLASKIWK EPAPPNERQK GVIEAFLHAW KGYQKFAWGH DELKPVSKTF 

       250        260        270        280        290        300 
SEWFGLGLTL IDALDTMWIL GLKQEFKQAR KWVSENLDFQ KNVDVNLFES TIRILGGLLS 

       310        320        330        340        350        360 
TYHLSGDSLF LTKAEDFGKR LMPAFTTPSK IPYSDVNIGT GFAHSPQWTS DSTVAEVTSI 

       370        380        390        400        410        420 
QLEFRELSRL TGIKKFQEAV EEVTKHIHSL SGKKDGLVPM FINTNSGLFT HPGVFTLGAR 

       430        440        450        460        470        480 
ADSYYEYLLK QWIQGGKKET QLLEDYVKAI EGIKAHLLRQ SQPRKLTFVG ELAHGRFSAK 

       490        500        510        520        530        540 
MDHLVCFLPG TLALGVHHGL PADHMDLARA LMETCYQMNQ QMETGLSPEI AHFNMYPRAD 

       550        560        570        580        590        600 
HKDVEVKPAD RHNLLRPETV ESLFYLYRVT RDRKYQDWGW EILQSFNKYT RVPSGGYSSI 

       610        620        630        640        650 
NNVQNSHKPE PRDKMESFFV GETLKYLYLL FSDDLELLSL DSCVFNTEAH PLPIWAPA 

« Hide

References

[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL732557 Genomic DNA. Translation: CAM25606.1.
CH466542 Genomic DNA. Translation: EDL08233.1.
BC138550 mRNA. Translation: AAI38551.1.
BC138551 mRNA. Translation: AAI38552.1.
RefSeqNP_001025154.1. NM_001029983.2.
UniGeneMm.270798.

3D structure databases

ProteinModelPortalA2AJ15.
SMRA2AJ15. Positions 206-655.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteA2AJ15.

Proteomic databases

PaxDbA2AJ15.
PRIDEA2AJ15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042390; ENSMUSP00000036996; ENSMUSG00000036646.
GeneID227619.
KEGGmmu:227619.
UCSCuc008irp.2. mouse.

Organism-specific databases

CTD11253.
MGIMGI:2684954. Man1b1.

Phylogenomic databases

eggNOGNOG300315.
GeneTreeENSGT00390000016529.
HOGENOMHOG000181987.
HOVERGENHBG052389.
InParanoidA2AJ15.
KOK01230.
OMAYAQVETG.
OrthoDBEOG7ZGX2S.
PhylomeDBA2AJ15.
TreeFamTF354274.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressA2AJ15.
BgeeA2AJ15.
GenevestigatorA2AJ15.

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. SSF48225. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMAN1B1. mouse.
NextBio378670.
PROA2AJ15.
SOURCESearch...

Entry information

Entry nameMA1B1_MOUSE
AccessionPrimary (citable) accession number: A2AJ15
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: February 20, 2007
Last modified: April 16, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries