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 27-MAR-2024, entry version 84. 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)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan CC mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man- CC (1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]- CC beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl- CC [protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, CC Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; CC EC=3.2.1.113; 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 beta-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 GlyCosmos; Q6GQB9; 4 sites, No reported glycans. DR DNASU; 443907; -. DR GeneID; 443907; -. DR KEGG; xla:443907; -. DR AGR; Xenbase:XB-GENE-5811512; -. DR CTD; 443907; -. DR Xenbase; XB-GENE-5811512; edem3.L. DR OrthoDB; 942598at2759; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000186698; Chromosome 4L. DR Bgee; 443907; Expressed in egg cell and 19 other cell types or tissues. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. 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: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 Gene3D; 3.50.30.30; -; 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; IPR046450; PA_dom_sf. DR InterPro; IPR003137; PA_domain. DR InterPro; IPR036026; Seven-hairpin_glycosidases. DR PANTHER; PTHR45679; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1. DR PANTHER; PTHR45679:SF2; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 3; 1. DR Pfam; PF01532; Glyco_hydro_47; 1. DR Pfam; PF02225; PA; 1. DR PRINTS; PR00747; GLYHDRLASE47. DR SUPFAM; SSF52025; PA domain; 1. DR SUPFAM; SSF48225; Seven-hairpin glycosidases; 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 //