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Q2HXL6

- EDEM3_MOUSE

UniProt

Q2HXL6 - EDEM3_MOUSE

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Protein

ER degradation-enhancing alpha-mannosidase-like protein 3

Gene

Edem3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei147 – 1471Proton donorBy similarity
Active sitei294 – 2941By similarity
Active sitei406 – 4061By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. glycoprotein endo-alpha-1,2-mannosidase activity Source: MGI
  3. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycoprotein catabolic process Source: MGI
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  3. response to unfolded protein Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Unfolded protein response

Enzyme and pathway databases

ReactomeiREACT_198606. ER Quality Control Compartment (ERQC).

Protein family/group databases

CAZyiGH47. Glycoside Hydrolase Family 47.

Names & Taxonomyi

Protein namesi
Recommended name:
ER degradation-enhancing alpha-mannosidase-like protein 3 (EC:3.2.1.113)
Alternative name(s):
Alpha-1,2-mannosidase EDEM3
Gene namesi
Name:Edem3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1914217. Edem3.

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: MGI
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi147 – 1471E → Q: Loss of ERAD activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242Sequence AnalysisAdd
BLAST
Chaini43 – 931889ER degradation-enhancing alpha-mannosidase-like protein 3PRO_0000316958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi505 – 5051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi512 – 5121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi811 – 8111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi815 – 8151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi899 – 8991N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ2HXL6.
PaxDbiQ2HXL6.
PRIDEiQ2HXL6.

PTM databases

PhosphoSiteiQ2HXL6.

Expressioni

Tissue specificityi

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

Inductioni

Slightly increased by endoplasmic reticulum stress.1 Publication

Gene expression databases

BgeeiQ2HXL6.
CleanExiMM_EDEM3.
ExpressionAtlasiQ2HXL6. baseline and differential.
GenevestigatoriQ2HXL6.

Interactioni

Protein-protein interaction databases

IntActiQ2HXL6. 6 interactions.
STRINGi10090.ENSMUSP00000058941.

Structurei

3D structure databases

ProteinModelPortaliQ2HXL6.
SMRiQ2HXL6. Positions 57-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini675 – 780106PAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi928 – 9314Prevents secretion from ERPROSITE-ProRule annotation

Domaini

Contains a protease-associated domain of unknown function.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG307610.
GeneTreeiENSGT00530000063069.
HOGENOMiHOG000007735.
HOVERGENiHBG107835.
InParanoidiQ2HXL6.
KOiK10086.
OMAiDRDPEME.
OrthoDBiEOG79W94G.
PhylomeDBiQ2HXL6.
TreeFamiTF300807.

Family and domain databases

Gene3Di1.50.10.50. 1 hit.
InterProiIPR001382. Glyco_hydro_47.
IPR003137. Protease-assoc_domain.
[Graphical view]
PANTHERiPTHR11742. PTHR11742. 1 hit.
PfamiPF01532. Glyco_hydro_47. 1 hit.
PF02225. PA. 1 hit.
[Graphical view]
PRINTSiPR00747. GLYHDRLASE47.
SUPFAMiSSF48225. SSF48225. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2HXL6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKAGGCRGC GCRVPQRASW SLVAATAALC LVLATSVCTA GAAPMSREEK
60 70 80 90 100
QKLGNQVLEM FDHAYGNYME HAYPADELMP LTCRGRVRGQ EPSRGDVDDA
110 120 130 140 150
LGKFSLTLID SLDTLVVLNK TKEFEDAVRK VLRDVNLDND VVVSVFETNI
160 170 180 190 200
RVLGGLLGGH SLAIMLKEKG EHMQWYNDEL LHMAKQLGYK LLPAFNTTSG
210 220 230 240 250
LPYPRINLKF GIRKPEARTG TETDTCTACA GTLILEFAAL SRFTGATIFE
260 270 280 290 300
EYARKALDFL WEKRQRSSNL VGVTINIHTG DWVRKDSGVG AGIDSYYEYL
310 320 330 340 350
LKAYVLLGDD SFLERFNTHY DAIMRYISQP PLLLDVHIHK PMLNARTWMD
360 370 380 390 400
ALLAFFPGLQ VLKGDIRPAI ETHEMLYQVI KKHNFLPEAF TTDFRVHWAQ
410 420 430 440 450
HPLRPEFAES TYFLYKATGD PYYLEVGKTL IENLNKYARV PCGFAAMKDV
460 470 480 490 500
RTGSHEDRMD SFFLAEMFKY LYLLFADKED IIFDIEDYIF TTEAHLLPLW
510 520 530 540 550
LSTTNRSISK KNTTSEYTEL DDSNFDWTCP NTQILFPNDP LYAQSIREPL
560 570 580 590 600
KNVVDKSCPR GIIRVEESFR SGAKPPLRAR DFMATNPEHL EILKKMGVSL
610 620 630 640 650
IHLKDGRVQL VQHAIQAASS IDAEDGLRFM QEMIELSSQQ QKEQQLPPRA
660 670 680 690 700
VQIISHPFFG RVVLTAGPAQ FGLDLSKHKE TRGFVASSKP YNGCSELTNP
710 720 730 740 750
EAVMGKIALI QRGQCMFAEK ARNIQNAGAI GGIVIDDNEG SSSDTAPLFQ
760 770 780 790 800
MAGDGKDTDD IKIPMLFLFS KEGSIILDAI REHEQVEVLL SDKARDRDPE
810 820 830 840 850
MENEDQPSSE NDSQNQSAEQ MLSLSQTVDL ADKESPEHPA DSHSEASPSD
860 870 880 890 900
SEEAAGFAPS EQISGSTENH ETTSLDGECT DLDNQVQEQS ETEEDSSPNV
910 920 930
SWGTKAQPID SILADWNEDI EAFEMMEKDE L
Length:931
Mass (Da):104,200
Last modified:March 3, 2009 - v2
Checksum:i4F010D17E84E542C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti784 – 7841E → K in BAE79485. (PubMed:16431915)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB188342 mRNA. Translation: BAE79485.1.
BC060718 mRNA. Translation: AAH60718.1.
BC138658 mRNA. Translation: AAI38659.1.
BC138659 mRNA. Translation: AAI38660.1.
CCDSiCCDS35736.1.
RefSeqiNP_001034733.2. NM_001039644.2.
UniGeneiMm.337691.

Genome annotation databases

EnsembliENSMUST00000059498; ENSMUSP00000058941; ENSMUSG00000043019.
GeneIDi66967.
KEGGimmu:66967.
UCSCiuc007czc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB188342 mRNA. Translation: BAE79485.1 .
BC060718 mRNA. Translation: AAH60718.1 .
BC138658 mRNA. Translation: AAI38659.1 .
BC138659 mRNA. Translation: AAI38660.1 .
CCDSi CCDS35736.1.
RefSeqi NP_001034733.2. NM_001039644.2.
UniGenei Mm.337691.

3D structure databases

ProteinModelPortali Q2HXL6.
SMRi Q2HXL6. Positions 57-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q2HXL6. 6 interactions.
STRINGi 10090.ENSMUSP00000058941.

Protein family/group databases

CAZyi GH47. Glycoside Hydrolase Family 47.

PTM databases

PhosphoSitei Q2HXL6.

Proteomic databases

MaxQBi Q2HXL6.
PaxDbi Q2HXL6.
PRIDEi Q2HXL6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000059498 ; ENSMUSP00000058941 ; ENSMUSG00000043019 .
GeneIDi 66967.
KEGGi mmu:66967.
UCSCi uc007czc.2. mouse.

Organism-specific databases

CTDi 80267.
MGIi MGI:1914217. Edem3.

Phylogenomic databases

eggNOGi NOG307610.
GeneTreei ENSGT00530000063069.
HOGENOMi HOG000007735.
HOVERGENi HBG107835.
InParanoidi Q2HXL6.
KOi K10086.
OMAi DRDPEME.
OrthoDBi EOG79W94G.
PhylomeDBi Q2HXL6.
TreeFami TF300807.

Enzyme and pathway databases

Reactomei REACT_198606. ER Quality Control Compartment (ERQC).

Miscellaneous databases

NextBioi 323155.
PROi Q2HXL6.
SOURCEi Search...

Gene expression databases

Bgeei Q2HXL6.
CleanExi MM_EDEM3.
ExpressionAtlasi Q2HXL6. baseline and differential.
Genevestigatori Q2HXL6.

Family and domain databases

Gene3Di 1.50.10.50. 1 hit.
InterProi IPR001382. Glyco_hydro_47.
IPR003137. Protease-assoc_domain.
[Graphical view ]
PANTHERi PTHR11742. PTHR11742. 1 hit.
Pfami PF01532. Glyco_hydro_47. 1 hit.
PF02225. PA. 1 hit.
[Graphical view ]
PRINTSi PR00747. GLYHDRLASE47.
SUPFAMi SSF48225. SSF48225. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiEDEM3_MOUSE
AccessioniPrimary (citable) accession number: Q2HXL6
Secondary accession number(s): B2RS10, B9EHZ4, Q6P9L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 3, 2009
Last modified: October 29, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3