EDEM3_XENLA
ID EDEM3_XENLA Reviewed; 913 AA.
AC Q6GQB9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=ER degradation-enhancing alpha-mannosidase-like protein 3;
DE EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE AltName: Full=Alpha-1,2-mannosidase EDEM3;
DE Flags: Precursor;
GN Name=edem3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in endoplasmic reticulum-associated
CC degradation (ERAD). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-
CC glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-
CC (alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-
CC asparaginyl-[protein] (N-glucan mannose isomer 5A1,2);
CC Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087,
CC ChEBI:CHEBI:139493; EC=3.2.1.113;
CC Evidence={ECO:0000250|UniProtKB:P32906};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]
CC (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-
CC COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628;
CC EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P45700};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P32906}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- DOMAIN: Contains a protease-associated domain (PA) of unknown function.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC072826; AAH72826.1; ALT_INIT; mRNA.
DR RefSeq; NP_001085481.2; NM_001092012.1.
DR AlphaFoldDB; Q6GQB9; -.
DR SMR; Q6GQB9; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR DNASU; 443907; -.
DR GeneID; 443907; -.
DR KEGG; xla:443907; -.
DR CTD; 443907; -.
DR Xenbase; XB-GENE-5811512; edem3.L.
DR OrthoDB; 434316at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 443907; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IEA:InterPro.
DR GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR CDD; cd02126; PA_EDEM3_like; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR044674; EDEM1/2/3.
DR InterPro; IPR037322; EDEM3_PA.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR PANTHER; PTHR45679; PTHR45679; 1.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR Pfam; PF02225; PA; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Metal-binding;
KW Reference proteome; Signal; Unfolded protein response.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..913
FT /note="ER degradation-enhancing alpha-mannosidase-like
FT protein 3"
FT /id="PRO_0000364227"
FT DOMAIN 660..766
FT /note="PA"
FT REGION 823..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 910..913
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 841..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /evidence="ECO:0000250"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT ACT_SITE 391
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 913 AA; 102735 MW; BB7164FF7FA2BC83 CRC64;
MGCPAVEARR WGDMWLVVAF CLLGHGHAAV TKEEKAHLRS QVLEMFDHAY GNYMQHAYPA
DELMPLTCRG RIRGQEPSRG DVDDALGKFS LTLIDTLDTL VVLNKTKEFE DAVRKVITDV
NLDNDIVVSV FETNIRVLGG LLGGHSVAIM LKENGDGMQW YNDELLHMAK ELGYKLLPAF
NTTSGLPYPR INLKFGIRRP EARTGTETDT CTACAGTMIL EFAALSRFTG ISVFEEHARK
ALDFLWDKRQ RSSNLVGVTI NIHTGDWVRK DSGVGAGIDS YYEYLLKAYV LLGDDSYLER
FNTHYDAIMR YISQPPLLLD VHIHKPMLTA RTWMDSLLAF FPGLQVLKGD IRPAIETHEM
LYQVIKKHNF LPEAFTTDFR VHWAQHPLRP EFAESTYFLY KATGDPYYLE VGKTLIDNLN
KYARVPCGFA AVKDVRTGSH EDRMDSFFLA EMFKYLYLLF SEREDLIFDI EDYIFTTEAH
LLPLSLSTAN PSSTKKNTTT QYTELDDSNF DWSCPNTQIL FRNDPMYAQN IREPLKNVVD
KNCPRSPSRL DEISGSGKMP PLRARDFMAS NSEHLEILKK MGVSLIHLKD GRVQLVQHAN
QAASSIDAED GLRFMQEMIE LSSQQQKEQQ LPPRAVQIVS HPFYGRVVLT AGPAQFGMDL
SKHLAGAQGL VARAEPYSGC SDITNGQAIQ GKIALMQRGQ CMFAEKARNV QKAGAIGGIV
IDDNEGSSSD TAPLFQMAGD GKSTDDVTIP MLFLFSKEGN IILDAIREYQ QVEVLLSDKA
KDRDLESESG EQKPVENDSQ KQALEDLFMT PEEIAELLIV HEEESPVSQP EVPSSDSPSG
GDRTSERDIT PESQEHKTEE TEHSPKDNVQ TPPENSEDST EEKMDNKVQP MESILADWKE
DIEAFEMMEK DEL
