ID MA1A1_PIG Reviewed; 659 AA. AC O02773; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 24-JAN-2024, entry version 129. DE RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA; DE EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906}; DE AltName: Full=Man(9)-alpha-mannosidase; DE Short=Man9-mannosidase; DE AltName: Full=Mannosidase alpha class 1A member 1; DE AltName: Full=Processing alpha-1,2-mannosidase IA; DE Short=Alpha-1,2-mannosidase IA; GN Name=MAN1A1; Synonyms=MAN1A; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR RP LOCATION. RC TISSUE=Liver; RX PubMed=9219526; DOI=10.1111/j.1432-1033.1997.t01-1-00681.x; RA Bieberich E., Treml K., Volker C., Rolfs A., Kalz-Fueller B., Bause E.; RT "Man9-mannosidase from pig liver is a type-II membrane protein that resides RT in the endoplasmic reticulum. cDNA cloning and expression of the enzyme in RT COS 1 cells."; RL Eur. J. Biochem. 246:681-689(1997). RN [2] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=8223597; DOI=10.1111/j.1432-1033.1993.tb18274.x; RA Bause E., Bieberich E., Rolfs A., Voelker C., Schmidt B.; RT "Molecular cloning and primary structure of Man9-mannosidase from human RT kidney."; RL Eur. J. Biochem. 217:535-540(1993). CC -!- FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. CC Progressively trim alpha-1,2-linked mannose residues from CC Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2). 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 -!- ACTIVITY REGULATION: Inhibited by both 1-deoxymannojirimycin and CC kifunensine. {ECO:0000250}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000250|UniProtKB:P32906}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:9219526}; Single-pass type II membrane protein CC {ECO:0000269|PubMed:9219526}. 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; Y12503; CAA73105.1; -; mRNA. DR PIR; S78554; S78554. DR RefSeq; NP_999050.1; NM_213885.1. DR AlphaFoldDB; O02773; -. DR SMR; O02773; -. DR STRING; 9823.ENSSSCP00000004583; -. DR CAZy; GH47; Glycoside Hydrolase Family 47. DR PaxDb; 9823-ENSSSCP00000004583; -. DR PeptideAtlas; O02773; -. DR GeneID; 396919; -. DR KEGG; ssc:396919; -. DR CTD; 4121; -. DR eggNOG; KOG2204; Eukaryota. DR InParanoid; O02773; -. DR OrthoDB; 942598at2759; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. 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:SF31; MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE IA; 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 1: Evidence at protein level; KW Calcium; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Glycosidase; Hydrolase; Membrane; Metal-binding; Reference proteome; KW Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1..659 FT /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA" FT /id="PRO_0000210310" FT TOPO_DOM 1..48 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 49..69 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 70..659 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 88..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 96..113 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 528 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P31723" FT BINDING 639 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P32906" FT DISULFID 482..514 FT /evidence="ECO:0000250|UniProtKB:P32906" SQ SEQUENCE 659 AA; 73197 MW; AA7F17FEAAFE43A6 CRC64; MPVGGLLPLF SSPAGGGLGG GLGGGLGGGG GGGGRKGSGP SAFRLTEKFV LLLVFSAFIT LCFGAIFFLP DSSKLLSGVL FHSSPALQPA ADHKPGPGAR AEDAADGRAR PGEEGAPGDP AAALEDNLAR IRENHERALM EAKETLQKLP EEIQRDILME KEKVAQDQMS NRMGFRLPPV YLVPLIGAID REPADAAVRE KRAKIKEMMK HAWNNYKLYA WGKNELKPVS KGGHSSSLFG NIKGATIVDA LDTLFIMKMK NEFEEAKAWV EEHLNFNVNA EVSVFEVNIR FIGGLISAYY LSGEEIFRKK AVELGVKLLP AFYTPSGIPW ALLNIKSGIG RNWPWASGGS SILAEFGTLH LEFIHLSYLS GNPFFAEKVM NIRKVLNNLE KPQGLYPNYL NPNSGQWGQY HVSVGGLGDS FYEYLLKAWL MSDKTDLEAK KMYFDAIKAI ETHLIRKSRN GLTYIAEWKG GLLEHKMGHL TCFAGGMFAL GADDAPDGLT QHYLQLGAEI ARTCHESYSR TFVKLGPEAF RFDGGVEAIA TRQNEKYYIL RPEVVETYLY MWRLTHDPKY RKWAWEAVEA LEKHCRVNGG YSGLRDVYVS AQTYDDVQQS FFLAETLKYL YLIFSDDDLL PLEHWIFNTE AHPLPVLSRN IKKVEDNEK //