MA1A1_PIG
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 03-AUG-2022, entry version 122.
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)-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: 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}.
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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; O02773; -.
DR PeptideAtlas; O02773; -.
DR GeneID; 396919; -.
DR KEGG; ssc:396919; -.
DR CTD; 4121; -.
DR eggNOG; KOG2204; Eukaryota.
DR InParanoid; O02773; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum 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; 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
