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Q2HXL6

- EDEM3_MOUSE

UniProt

Q2HXL6 - EDEM3_MOUSE

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
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (03 Mar 2009)
      Previous versions | rss
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    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

    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

    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.
    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.
    InParanoidiB2RS10.
    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

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    MSKAGGCRGC GCRVPQRASW SLVAATAALC LVLATSVCTA GAAPMSREEK    50
    QKLGNQVLEM FDHAYGNYME HAYPADELMP LTCRGRVRGQ EPSRGDVDDA 100
    LGKFSLTLID SLDTLVVLNK TKEFEDAVRK VLRDVNLDND VVVSVFETNI 150
    RVLGGLLGGH SLAIMLKEKG EHMQWYNDEL LHMAKQLGYK LLPAFNTTSG 200
    LPYPRINLKF GIRKPEARTG TETDTCTACA GTLILEFAAL SRFTGATIFE 250
    EYARKALDFL WEKRQRSSNL VGVTINIHTG DWVRKDSGVG AGIDSYYEYL 300
    LKAYVLLGDD SFLERFNTHY DAIMRYISQP PLLLDVHIHK PMLNARTWMD 350
    ALLAFFPGLQ VLKGDIRPAI ETHEMLYQVI KKHNFLPEAF TTDFRVHWAQ 400
    HPLRPEFAES TYFLYKATGD PYYLEVGKTL IENLNKYARV PCGFAAMKDV 450
    RTGSHEDRMD SFFLAEMFKY LYLLFADKED IIFDIEDYIF TTEAHLLPLW 500
    LSTTNRSISK KNTTSEYTEL DDSNFDWTCP NTQILFPNDP LYAQSIREPL 550
    KNVVDKSCPR GIIRVEESFR SGAKPPLRAR DFMATNPEHL EILKKMGVSL 600
    IHLKDGRVQL VQHAIQAASS IDAEDGLRFM QEMIELSSQQ QKEQQLPPRA 650
    VQIISHPFFG RVVLTAGPAQ FGLDLSKHKE TRGFVASSKP YNGCSELTNP 700
    EAVMGKIALI QRGQCMFAEK ARNIQNAGAI GGIVIDDNEG SSSDTAPLFQ 750
    MAGDGKDTDD IKIPMLFLFS KEGSIILDAI REHEQVEVLL SDKARDRDPE 800
    MENEDQPSSE NDSQNQSAEQ MLSLSQTVDL ADKESPEHPA DSHSEASPSD 850
    SEEAAGFAPS EQISGSTENH ETTSLDGECT DLDNQVQEQS ETEEDSSPNV 900
    SWGTKAQPID SILADWNEDI EAFEMMEKDE L 931
    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 B2RS10.
    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.
    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

    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 1, 2014
    This is version 73 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