ID   MA1A1_RABIT             Reviewed;         469 AA.
AC   P45701;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 137.
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   AltName: Full=Mannosidase alpha class 1A member 1;
DE   AltName: Full=Processing alpha-1,2-mannosidase IA;
DE            Short=Alpha-1,2-mannosidase IA;
DE   Flags: Fragment;
GN   Name=MAN1A1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=8144580; DOI=10.1016/s0021-9258(17)36964-8;
RA   Lal A., Schutzbach J.S., Forsee W.T., Neame P.J., Moremen K.W.;
RT   "Isolation and expression of murine and rabbit cDNAs encoding an alpha 1,2-
RT   mannosidase involved in the processing of asparagine-linked
RT   oligosaccharides.";
RL   J. Biol. Chem. 269:9872-9881(1994).
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=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   -!- 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: Golgi apparatus membrane; Single-pass type II
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR   EMBL; U04301; AAA17748.1; -; mRNA.
DR   AlphaFoldDB; P45701; -.
DR   SMR; P45701; -.
DR   FunCoup; P45701; 2198.
DR   CAZy; GH47; Glycoside Hydrolase Family 47.
DR   GlyCosmos; P45701; 1 site, No reported glycans.
DR   PaxDb; 9986-ENSOCUP00000037605; -.
DR   eggNOG; KOG2204; Eukaryota.
DR   InParanoid; P45701; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter.
DR   GO; GO:0070062; C:extracellular exosome; IEA:TreeGrafter.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   FunFam; 1.50.10.10:FF:000002; alpha-1,2-Mannosidase; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001382; Glyco_hydro_47.
DR   InterPro; IPR050749; Glycosyl_Hydrolase_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; Glycoprotein;
KW   Glycosidase; Golgi apparatus; Hydrolase; Membrane; Metal-binding;
KW   Reference proteome; Signal-anchor; Transmembrane.
FT   CHAIN           <1..469
FT                   /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA"
FT                   /id="PRO_0000210311"
FT   TOPO_DOM        <1..469
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        338
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P31723"
FT   BINDING         449
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P32906"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        292..324
FT                   /evidence="ECO:0000250|UniProtKB:P32906"
FT   NON_TER         1
SQ   SEQUENCE   469 AA;  53427 MW;  A1B9128144FD0D39 CRC64;
     REPADAAVRE KRAKIKEMME HAWNSYKRYA WGLNELKPIT KEGHSSSLFG TIKGATIVDA
     LDTLFIMGME SEFQEAKSWI AENLDFNVNA EISVFEVNIR FVGGLLSAYY LSGEEIFRKK
     AVELGIKLLP AFHTPSGIPW ALLNIKSGIG RNWPWASGGS SILAEFGTLH LEFMHLSHLS
     GNPIFAEKVM NIRKVLNKLE KPEGLYPNYL NPSSGQWGQH HVSIGGLGDS FYEYLLKAWL
     MSEKTDLEAK KMYFDAVQAI ETHLIRKSSG GLTYIAEWKG GLLEHKMGHL TCFAGGMFAL
     GADGAPEGRA QHYLELGAEI ARTCHESYNR TFMKLGPEAF RFDGGVEAIA TRQNEKYYIL
     RPEVVETYMY MWRLTHDPKY RKWAWEAVEA LESHCRVNGG YSGLRDVYFT HEKYDNVQQS
     FFLAETLKYL YLIFSDDDLL PLEHWIFNTE AHLLPILPTD QKEVEVKVK
//