MA1A1_RABIT
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 03-AUG-2022, entry version 124.
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=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)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-
CC glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-
CC (alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-
CC asparaginyl-[protein] (N-glucan mannose isomer 5A1,2);
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=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 alpha-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: 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 STRING; 9986.ENSOCUP00000005793; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR eggNOG; KOG2204; Eukaryota.
DR InParanoid; P45701; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 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
