ID MNS1_CANAX Reviewed; 565 AA. AC Q8J0Q0; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 2. DT 24-JAN-2024, entry version 84. DE RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase; DE EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906}; DE AltName: Full=Man(9)-alpha-mannosidase; GN Name=MNS1; OS Candida albicans (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5476; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 26555; RA Mora-Montes H.M., Flores-Carreon A., Ponce-Noyola P., Lopez-Romero E., RA Zinker-Ruzal S.; RT "Identification of the alpha1,2-mannosidase gene (Mns1) in Candida RT albicans."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. CC Trim a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to CC produce Man(8)GlcNAc(2) (By similarity). {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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {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; AY167027; AAN86059.2; -; Genomic_DNA. DR AlphaFoldDB; Q8J0Q0; -. DR SMR; Q8J0Q0; -. DR CAZy; GH47; Glycoside Hydrolase Family 47. DR VEuPathDB; FungiDB:C1_03730C_A; -. DR VEuPathDB; FungiDB:CAWG_01018; -. DR BRENDA; 3.2.1.113; 1096. DR BRENDA; 3.2.1.209; 1096. DR UniPathway; UPA00378; -. 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:0030433; P:ubiquitin-dependent ERAD pathway; IEA:UniProt. DR Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR001382; Glyco_hydro_47. DR InterPro; IPR036026; Seven-hairpin_glycosidases. DR PANTHER; PTHR11742:SF55; ENDOPLASMIC RETICULUM MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE; 1. DR PANTHER; PTHR11742; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED; 1. DR Pfam; PF01532; Glyco_hydro_47; 1. DR PRINTS; PR00747; GLYHDRLASE47. DR SUPFAM; SSF48225; Seven-hairpin glycosidases; 1. PE 3: Inferred from homology; KW Calcium; Disulfide bond; Glycosidase; Hydrolase; Metal-binding. FT CHAIN 1..565 FT /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase" FT /id="PRO_0000210318" FT REGION 526..565 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 550..565 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 378 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P31723" FT BINDING 501 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P32906" FT DISULFID 320..363 FT /evidence="ECO:0000250|UniProtKB:P32906" SQ SEQUENCE 565 AA; 64659 MW; C3581A0D889CCAF2 CRC64; MLLKGFMLSL VLYAVYHLAS NGGQFMFDFS GQSKWERAQS EVRQAILDSW HTYEKYGWGY DVYHPIKQEG ENMGPKPLGW MIVDSLDTLM IMDCPEEVSR ARDWIKNDLD YTFDYNVNTF ETTIRMLGGL LSAYHFSNDD VYLDKAVQLA NALHGAYDSP SGIPYSSVNL KSGKGIKNHV DNGASSTAEA ATVQLEMKYL SKLTGEILWW NLAEKVMQVL ESNKPQDGLV PIYVNPDTGK YQGHLIRLGS RGDSYYEYLL KQYLQTNKQE LVYWDMYRES VEGVKKHLVS DSYPSGLTFI GELDNGIGGK LSTKMDHLVC FYGGLLALGA TGGLTLNEAQ SLKSWNEERE ADFKLGEELT YTCYKMYHDV SPTGLSPEIV VFNEDTSKSK DFIIKPLDRH NLQRPETVES LFYLYRLTGD VKYREMGYEI FQNFIKYTKV VNSEGEVSFS SLSDVTSFDS NGLPKFKDNT ESFWWAETLK YLYLLFDDTN KIPLTDYVFN TEAHPFPRFD TNDYFKTGWR RKIDENEKAQ MRESKVIDKS NLPEAQPVDK SADQEAKEII EEIAG //