MNS1B_ASPPH
ID MNS1B_ASPPH Reviewed; 513 AA.
AC Q12563;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B;
DE EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE AltName: Full=Class I alpha-mannosidase 1B;
DE AltName: Full=Man(9)-alpha-mannosidase 1B;
DE Flags: Precursor;
GN Name=mns1B; Synonyms=msdS;
OS Aspergillus phoenicis (Aspergillus saitoi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5063;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8519794; DOI=10.1016/0167-4838(95)00195-6;
RA Inoue T., Yoshida T., Ichishima E.;
RT "Molecular cloning and nucleotide sequence of the 1,2-alpha-D-mannosidase
RT gene, msdS, from Aspergillus saitoi and expression of the gene in yeast
RT cells.";
RL Biochim. Biophys. Acta 1253:141-145(1995).
CC -!- FUNCTION: Involved in the maturation of Asn-linked oligosaccharides.
CC Progressively trims alpha-1,2-linked mannose residues from
CC Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
CC {ECO:0000269|PubMed:8519794}.
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:Q2ULB2};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q2ULB2};
CC Note=Ca(2+). Can also use Mg(2+), but with lower efficiency.
CC {ECO:0000250|UniProtKB:Q2ULB2};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P32906}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle lumen {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; D49827; BAA08634.1; -; mRNA.
DR AlphaFoldDB; Q12563; -.
DR SMR; Q12563; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR CLAE; MSD47S_ASPPH; -.
DR SABIO-RK; Q12563; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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 Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..513
FT /note="Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B"
FT /id="PRO_0000394821"
FT ACT_SITE 377
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT BINDING 503
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 334..363
FT /evidence="ECO:0000250|UniProtKB:P32906"
SQ SEQUENCE 513 AA; 55875 MW; 0FDAB2CB27E93724 CRC64;
MHLPSLSLSL TALAIASPSA AYPHFGSSQP VLHSSSDTTQ SRADAIKAAF SHAWDGYLQY
AFPHDELHPV SNGYGDSRNG WGASAVDALS TAVIMRNATI VNQILDHVGK IDYSKTNTTV
SLFETTIRYL GGMLSGYDLL KGPVSDLVQN SSKIDVLLTQ SKNLADVLKF AFDTPSGVPY
NNLNITSGGN DGAKTNGLAV TGTLALEWTR LSDLTGDTTY ADLSQKAESY LLNPQPKSAE
PFPGLVGSNI NISNGQFTDA QVSWNGGDDS YYEYLIKMYV YDPKRFGLYK DRWVAAAQST
MQHLASHPSS RPDLTFLASY NNGTLGLSSQ HLTCFDGGSF LLGGTVLNRT DFINFGLDLV
SGCHDTYNST LTGIGPESFS WDTSDIPSSQ QSLYEKAGFY ITSGAYILRP EVIESFYYAW
RVTGQETYRD WIWSAFSAVN DYCRTSSGFS GLTDVNAANG GSRYDNQESF LFAEVMKYSY
MAFAEDAAWQ VQPGSGNQFV FNTEAHPVRV SST
