ID EDEM3_HUMAN Reviewed; 932 AA. AC Q9BZQ6; B2RCH6; B7ZLZ2; Q0VGM5; Q5TEZ0; Q7L2Y5; Q9HCW1; Q9UFV7; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 2. DT 10-JUN-2026, entry version 191. 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; Synonyms=C1orf22; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 78-319 AND 853-932 (ISOFORM 1). RC TISSUE=Brain, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-932 (ISOFORM 1). RX PubMed=11318611; DOI=10.1006/geno.2001.6500; RA Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M., RA Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H., RA Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M., RA Carpten J.D.; RT "Cloning and characterization of 13 novel transcripts and the human RGS8 RT gene from the 1q25 region encompassing the hereditary prostate cancer RT (HPC1) locus."; RL Genomics 73:211-222(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 553-932 (ISOFORM 1), AND VARIANT RP SER-820. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-195. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [7] RP FUNCTION. RX PubMed=25092655; DOI=10.1083/jcb.201404075; RA Ninagawa S., Okada T., Sumitomo Y., Kamiya Y., Kato K., Horimoto S., RA Ishikawa T., Takeda S., Sakuma T., Yamamoto T., Mori K.; RT "EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first RT mannose trimming step."; RL J. Cell Biol. 206:347-356(2014). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [10] RP INVOLVEMENT IN CDG2V, FUNCTION, AND VARIANTS CDG2V GLY-61; 314-ARG--LEU-932 RP DEL; ASN-456 AND 469-TYR--LEU-932 DEL. RX PubMed=34143952; DOI=10.1016/j.ajhg.2021.05.010; RA Polla D.L., Edmondson A.C., Duvet S., March M.E., Sousa A.B., Lehman A., RA Niyazov D., van Dijk F., Demirdas S., van Slegtenhorst M.A., Kievit A.J.A., RA Schulz C., Armstrong L., Bi X., Rader D.J., Izumi K., Zackai E.H., RA de Franco E., Jorge P., Huffels S.C., Hommersom M., Ellard S., RA Lefeber D.J., Santani A., Hand N.J., van Bokhoven H., He M., RA de Brouwer A.P.M.; RT "Bi-allelic variants in the ER quality-control mannosidase gene EDEM3 cause RT a congenital disorder of glycosylation."; RL Am. J. Hum. Genet. 108:1342-1349(2021). CC -!- FUNCTION: Involved in endoplasmic reticulum-associated degradation CC (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing CC mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans CC (PubMed:25092655). May also participate in mannose trimming from all CC glycoproteins and not just misfolded ones targeted to ERAD CC (PubMed:34143952). May have alpha 1,2-mannosidase activity (By CC similarity). {ECO:0000250, ECO:0000269|PubMed:25092655, CC ECO:0000269|PubMed:34143952}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man- CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)- CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D- CC GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan CC mannose isomer 9A1,2,3B1,2,3) + 4 H2O = N(4)-(alpha-D-Man-(1->3)- CC [alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D- CC Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl- CC [protein] (N-glucan mannose isomer 5A1,2) + 4 beta-D-mannose; 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=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man- CC (1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]- CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- CC GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) CC + 3 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[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 5A1,2) + 3 beta-D-mannose; 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BZQ6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZQ6-2; Sequence=VSP_056375, VSP_056376; CC -!- DOMAIN: Contains a protease-associated domain (PA) of unknown function. CC -!- DISEASE: Congenital disorder of glycosylation 2V (CDG2V) [MIM:619493]: CC A form of congenital disorder of glycosylation, a genetically CC heterogeneous group of multisystem disorders caused by a defect in CC glycoprotein biosynthesis and characterized by under-glycosylated serum CC glycoproteins. Congenital disorders of glycosylation result in a wide CC variety of clinical features, such as defects in the nervous system CC development, psychomotor retardation, dysmorphic features, hypotonia, CC coagulation disorders, and immunodeficiency. The broad spectrum of CC features reflects the critical role of N-glycoproteins during embryonic CC development, differentiation, and maintenance of cell functions. CDG2V CC is an autosomal recessive form characterized by neurodevelopmental CC delay and variable facial dysmorphic features. CC {ECO:0000269|PubMed:34143952}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG60613.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG37573.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AK315118; BAG37573.1; ALT_INIT; mRNA. DR EMBL; AL096819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC016464; AAH16464.2; -; mRNA. DR EMBL; BC105586; AAI05587.1; -; mRNA. DR EMBL; BC144149; AAI44150.1; -; mRNA. DR EMBL; AF288393; AAG60613.1; ALT_INIT; mRNA. DR EMBL; AL117441; CAB55926.1; -; mRNA. DR CCDS; CCDS1363.2; -. [Q9BZQ6-1] DR PIR; T17236; T17236. DR RefSeq; NP_001306889.1; NM_001319960.1. DR RefSeq; NP_079467.3; NM_025191.3. [Q9BZQ6-1] DR AlphaFoldDB; Q9BZQ6; -. DR SMR; Q9BZQ6; -. DR BioGRID; 123207; 179. DR FunCoup; Q9BZQ6; 2472. DR IntAct; Q9BZQ6; 66. DR MINT; Q9BZQ6; -. DR NDEx; IQUERY-CP-EDEM3; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000318147; -. DR GlyConnect; Q9BZQ6; 4 N-Linked glycans (1 site). DR GlyCosmos; Q9BZQ6; 7 sites, 4 glycans. DR GlyGen; Q9BZQ6; 9 sites, 10 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q9BZQ6; -. DR PhosphoSitePlus; Q9BZQ6; -. DR SwissPalm; Q9BZQ6; -. DR BioMuta; EDEM3; -. DR DMDM; 166897965; -. DR jPOST; Q9BZQ6; -. DR MassIVE; Q9BZQ6; -. DR PaxDb; 9606-ENSP00000318147; -. DR PeptideAtlas; Q9BZQ6; -. DR ProteomicsDB; 7240; -. DR ProteomicsDB; 79892; -. [Q9BZQ6-1] DR Pumba; Q9BZQ6; -. DR Antibodypedia; 20607; 125 antibodies from 25 providers. DR DNASU; 80267; -. DR Ensembl; ENST00000318130.13; ENSP00000318147.7; ENSG00000116406.21. [Q9BZQ6-1] DR GeneID; 80267; -. DR KEGG; hsa:80267; -. DR MANE-Select; ENST00000318130.13; ENSP00000318147.7; NM_025191.4; NP_079467.3. DR UCSC; uc010pok.3; human. [Q9BZQ6-1] DR AGR; HGNC:16787; -. DR ClinPGx; PA38186; -. DR CTD; 80267; -. DR DisGeNET; 80267; -. DR GeneCards; EDEM3; -. DR HGNC; HGNC:16787; EDEM3. DR HPA; ENSG00000116406; Low tissue specificity. DR MalaCards; EDEM3; -. DR MIM; 610214; gene. DR MIM; 619493; phenotype. DR OpenTargets; ENSG00000116406; -. DR Orphanet; 695783; EDEM3-CDG. DR VEuPathDB; HostDB:ENSG00000116406; -. DR eggNOG; KOG2430; Eukaryota. DR GeneTree; ENSGT00940000159391; -. DR HOGENOM; CLU_003818_4_1_1; -. DR InParanoid; Q9BZQ6; -. DR OMA; RRWDRRE; -. DR OrthoDB; 8118055at2759; -. DR PAN-GO; Q9BZQ6; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q9BZQ6; -. DR BRENDA; 3.2.1.113; 2681. DR PathwayCommons; Q9BZQ6; -. DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC). DR SignaLink; Q9BZQ6; -. DR UniPathway; UPA00378; -. DR Agora; ENSG00000116406; -. DR BioGRID-ORCS; 80267; 15 hits in 1169 CRISPR screens. DR ChiTaRS; EDEM3; human. DR GeneWiki; EDEM3; -. DR GenomeRNAi; 80267; -. DR Pharos; Q9BZQ6; Tbio. DR PRO; PR:Q9BZQ6; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BZQ6; protein. DR Bgee; ENSG00000116406; Expressed in pylorus and 196 other cell types or tissues. DR ExpressionAtlas; Q9BZQ6; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; TAS:Reactome. 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; IMP:ParkinsonsUK-UCL. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IMP:ParkinsonsUK-UCL. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central. DR GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; TAS:Reactome. DR GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; IBA:GO_Central. DR CDD; cd02126; PA_EDEM3_like; 1. DR FunFam; 1.50.10.10:FF:000008; alpha-1,2-Mannosidase; 1. DR FunFam; 3.50.30.30:FF:000004; alpha-1,2-Mannosidase; 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 1: Evidence at protein level; KW Alternative splicing; Congenital disorder of glycosylation; KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Metal-binding; KW Proteomics identification; Reference proteome; Signal; KW Unfolded protein response. FT SIGNAL 1..41 FT /evidence="ECO:0000255" FT CHAIN 42..932 FT /note="ER degradation-enhancing alpha-mannosidase-like FT protein 3" FT /id="PRO_0000210323" FT DOMAIN 674..779 FT /note="PA" FT REGION 790..908 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 929..932 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT COMPBIAS 790..799 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 812..825 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 856..890 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 146 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 293 FT /evidence="ECO:0000250" FT ACT_SITE 387 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P31723" FT ACT_SITE 405 FT /evidence="ECO:0000250" FT BINDING 491 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P32906" FT CARBOHYD 118 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 195 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 504 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 511 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 810 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 814 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 900 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..43 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056375" FT VAR_SEQ 796..797 FT /note="RD -> RAAILKGKMIPSYIINSN (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056376" FT VARIANT 61 FT /note="D -> G (in CDG2V; uncertain significance; FT dbSNP:rs777353823)" FT /evidence="ECO:0000269|PubMed:34143952" FT /id="VAR_086113" FT VARIANT 314..932 FT /note="Missing (in CDG2V; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34143952" FT /id="VAR_086114" FT VARIANT 456 FT /note="D -> N (in CDG2V; uncertain significance; FT dbSNP:rs2102081233)" FT /evidence="ECO:0000269|PubMed:34143952" FT /id="VAR_086115" FT VARIANT 469..932 FT /note="Missing (in CDG2V; uncertain significance; FT dbSNP:rs902837579)" FT /evidence="ECO:0000269|PubMed:34143952" FT /id="VAR_086116" FT VARIANT 820 FT /note="I -> S (in dbSNP:rs9425343)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_059306" FT CONFLICT 276 FT /note="I -> T (in Ref. 1; BAG37573)" FT /evidence="ECO:0000305" FT CONFLICT 318..319 FT /note="HY -> VS (in Ref. 4; AAI05587)" FT /evidence="ECO:0000305" SQ SEQUENCE 932 AA; 104664 MW; 3C040FDF48284D36 CRC64; MSEAGGRGCG SPVPQRARWR LVAATAAFCL VSATSVWTAG AEPMSREEKQ KLGNQVLEMF DHAYGNYMEH AYPADELMPL TCRGRVRGQE PSRGDVDDAL GKFSLTLIDS LDTLVVLNKT KEFEDAVRKV LRDVNLDNDV VVSVFETNIR VLGGLLGGHS LAIMLKEKGE YMQWYNDELL QMAKQLGYKL LPAFNTTSGL PYPRINLKFG IRKPEARTGT ETDTCTACAG TLILEFAALS RFTGATIFEE YARKALDFLW EKRQRSSNLV GVTINIHTGD WVRKDSGVGA GIDSYYEYLL KAYVLLGDDS FLERFNTHYD AIMRYISQPP LLLDVHIHKP MLNARTWMDA LLAFFPGLQV LKGDIRPAIE THEMLYQVIK KHNFLPEAFT TDFRVHWAQH PLRPEFAEST YFLYKATGDP YYLEVGKTLI ENLNKYARVP CGFAAMKDVR TGSHEDRMDS FFLAEMFKYL YLLFADKEDI IFDIEDYIFT TEAHLLPLWL STTNQSISKK NTTSEYTELD DSNFDWTCPN TQILFPNDPL YAQSIREPLK NVVDKSCPRG IIRVEESFRS GAKPPLRARD FMATNPEHLE ILKKMGVSLI HLKDGRVQLV QHAIQAASSI DAEDGLRFMQ EMIELSSQQQ KEQQLPPRAV QIVSHPFFGR VVLTAGPAQF GLDLSKHKET RGFVASSKPS NGCSELTNPE AVMGKIALIQ RGQCMFAEKA RNIQNAGAIG GIVIDDNEGS SSDTAPLFQM AGDGKDTDDI KIPMLFLFSK EGSIILDAIR EYEEVEVLLS DKAKDRDPEM ENEEQPSSEN DSQNQSGEQI SSSSQEVDLV DQESSEENSL NSHPESLSLA DMDNAASISP SEQTSNPTEN HETTNLNGEC TDLDNQLQEQ SETEEDSNPN VSWGKKVQPI DSILADWNED IEAFEMMEKD EL //