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Q2HXL6 (EDEM3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
ER degradation-enhancing alpha-mannosidase-like protein 3

EC=3.2.1.113
Alternative name(s):
Alpha-1,2-mannosidase EDEM3
Gene names
Name:Edem3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length931 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity. Ref.1

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen Ref.1.

Tissue specificity

Widely expressed. Expressed at higher level in liver, heart and kidney. Ref.1

Induction

Slightly increased by endoplasmic reticulum stress. Ref.1

Domain

Contains a protease-associated domain of unknown function.

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Contains 1 PA (protease associated) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 Potential
Chain43 – 931889ER degradation-enhancing alpha-mannosidase-like protein 3
PRO_0000316958

Regions

Domain675 – 780106PA
Motif928 – 9314Prevents secretion from ER Potential

Sites

Active site1471Proton donor By similarity
Active site2941 By similarity
Active site4061 By similarity

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation5051N-linked (GlcNAc...) Potential
Glycosylation5121N-linked (GlcNAc...) Potential
Glycosylation8111N-linked (GlcNAc...) Potential
Glycosylation8151N-linked (GlcNAc...) Potential
Glycosylation8991N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis1471E → Q: Loss of ERAD activity. Ref.1
Sequence conflict7841E → K in BAE79485. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2HXL6 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: 4F010D17E84E542C

FASTA931104,200
        10         20         30         40         50         60 
MSKAGGCRGC GCRVPQRASW SLVAATAALC LVLATSVCTA GAAPMSREEK QKLGNQVLEM 

        70         80         90        100        110        120 
FDHAYGNYME HAYPADELMP LTCRGRVRGQ EPSRGDVDDA LGKFSLTLID SLDTLVVLNK 

       130        140        150        160        170        180 
TKEFEDAVRK VLRDVNLDND VVVSVFETNI RVLGGLLGGH SLAIMLKEKG EHMQWYNDEL 

       190        200        210        220        230        240 
LHMAKQLGYK LLPAFNTTSG LPYPRINLKF GIRKPEARTG TETDTCTACA GTLILEFAAL 

       250        260        270        280        290        300 
SRFTGATIFE EYARKALDFL WEKRQRSSNL VGVTINIHTG DWVRKDSGVG AGIDSYYEYL 

       310        320        330        340        350        360 
LKAYVLLGDD SFLERFNTHY DAIMRYISQP PLLLDVHIHK PMLNARTWMD ALLAFFPGLQ 

       370        380        390        400        410        420 
VLKGDIRPAI ETHEMLYQVI KKHNFLPEAF TTDFRVHWAQ HPLRPEFAES TYFLYKATGD 

       430        440        450        460        470        480 
PYYLEVGKTL IENLNKYARV PCGFAAMKDV RTGSHEDRMD SFFLAEMFKY LYLLFADKED 

       490        500        510        520        530        540 
IIFDIEDYIF TTEAHLLPLW LSTTNRSISK KNTTSEYTEL DDSNFDWTCP NTQILFPNDP 

       550        560        570        580        590        600 
LYAQSIREPL KNVVDKSCPR GIIRVEESFR SGAKPPLRAR DFMATNPEHL EILKKMGVSL 

       610        620        630        640        650        660 
IHLKDGRVQL VQHAIQAASS IDAEDGLRFM QEMIELSSQQ QKEQQLPPRA VQIISHPFFG 

       670        680        690        700        710        720 
RVVLTAGPAQ FGLDLSKHKE TRGFVASSKP YNGCSELTNP EAVMGKIALI QRGQCMFAEK 

       730        740        750        760        770        780 
ARNIQNAGAI GGIVIDDNEG SSSDTAPLFQ MAGDGKDTDD IKIPMLFLFS KEGSIILDAI 

       790        800        810        820        830        840 
REHEQVEVLL SDKARDRDPE MENEDQPSSE NDSQNQSAEQ MLSLSQTVDL ADKESPEHPA 

       850        860        870        880        890        900 
DSHSEASPSD SEEAAGFAPS EQISGSTENH ETTSLDGECT DLDNQVQEQS ETEEDSSPNV 

       910        920        930 
SWGTKAQPID SILADWNEDI EAFEMMEKDE L 

« Hide

References

« Hide 'large scale' references
[1]"EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming."
Hirao K., Natsuka Y., Tamura T., Wada I., Morito D., Natsuka S., Romero P., Sleno B., Tremblay L.O., Herscovics A., Nagata K., Hosokawa N.
J. Biol. Chem. 281:9650-9658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF GLU-147.
[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: C57BL/6.
Tissue: Brain, Embryonic brain and Testis.
[3]"Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins."
Olivari S., Molinari M.
FEBS Lett. 581:3658-3664(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB188342 mRNA. Translation: BAE79485.1.
BC060718 mRNA. Translation: AAH60718.1.
BC138658 mRNA. Translation: AAI38659.1.
BC138659 mRNA. Translation: AAI38660.1.
CCDSCCDS35736.1.
RefSeqNP_001034733.2. NM_001039644.2.
UniGeneMm.337691.

3D structure databases

ProteinModelPortalQ2HXL6.
SMRQ2HXL6. Positions 57-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ2HXL6. 6 interactions.
STRING10090.ENSMUSP00000058941.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSiteQ2HXL6.

Proteomic databases

MaxQBQ2HXL6.
PaxDbQ2HXL6.
PRIDEQ2HXL6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059498; ENSMUSP00000058941; ENSMUSG00000043019.
GeneID66967.
KEGGmmu:66967.
UCSCuc007czc.2. mouse.

Organism-specific databases

CTD80267.
MGIMGI:1914217. Edem3.

Phylogenomic databases

eggNOGNOG307610.
GeneTreeENSGT00530000063069.
HOGENOMHOG000007735.
HOVERGENHBG107835.
InParanoidB2RS10.
KOK10086.
OMADRDPEME.
OrthoDBEOG79W94G.
PhylomeDBQ2HXL6.
TreeFamTF300807.

Gene expression databases

BgeeQ2HXL6.
CleanExMM_EDEM3.
GenevestigatorQ2HXL6.

Family and domain databases

Gene3D1.50.10.50. 1 hit.
InterProIPR001382. Glyco_hydro_47.
IPR003137. Protease-assoc_domain.
[Graphical view]
PANTHERPTHR11742. PTHR11742. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
PF02225. PA. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
SUPFAMSSF48225. SSF48225. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio323155.
PROQ2HXL6.
SOURCESearch...

Entry information

Entry nameEDEM3_MOUSE
AccessionPrimary (citable) accession number: Q2HXL6
Secondary accession number(s): B2RS10, B9EHZ4, Q6P9L0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 3, 2009
Last modified: July 9, 2014
This is version 71 of the entry and version 2 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

MGD cross-references

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries