MNS1B_COCPS
ID MNS1B_COCPS Reviewed; 519 AA.
AC E9CXX8; A0A059NZV8;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Mannosyl-oligosaccharide alpha-1,2-mannosidase {ECO:0000305};
DE EC=3.2.1.113 {ECO:0000269|Ref.2};
DE AltName: Full=Class I alpha-mannosidase {ECO:0000303|Ref.2};
DE AltName: Full=Man(9)-alpha-mannosidase {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=CPSG_02648;
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=RMSCC 757 / Silveira;
RX PubMed=17363438; DOI=10.1196/annals.1406.015;
RA Lunetta J.M., Simmons K.A., Johnson S.M., Pappagianis D.;
RT "Molecular cloning and expression of a cDNA encoding a Coccidioides
RT posadasii 1,2-alpha-mannosidase identified in the coccidioidal T27K vaccine
RT by immunoproteomic methods.";
RL Ann. N. Y. Acad. Sci. 1111:164-180(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Alpha-mannosidase involved in the maturation of Asn-linked
CC oligosaccharides. Progressively trims alpha-1,2-linked mannose residues
CC from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
CC {ECO:0000269|PubMed:17363438, ECO:0000269|Ref.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; Evidence={ECO:0000269|Ref.2};
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:0000269|Ref.2};
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|UniProtKB:P31723}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; DQ233502; ABB36773.3; -; mRNA.
DR EMBL; GL636488; EFW20805.1; -; Genomic_DNA.
DR AlphaFoldDB; E9CXX8; -.
DR SMR; E9CXX8; -.
DR STRING; 443226.E9CXX8; -.
DR CLAE; MSD47A_COCPO; -.
DR EnsemblFungi; EFW20805; EFW20805; CPSG_02648.
DR VEuPathDB; FungiDB:CPSG_02648; -.
DR eggNOG; KOG2204; Eukaryota.
DR HOGENOM; CLU_003818_0_2_1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002497; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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:InterPro.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..519
FT /note="Mannosyl-oligosaccharide alpha-1,2-mannosidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432784"
FT ACT_SITE 380
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 337..366
FT /evidence="ECO:0000250|UniProtKB:P31723"
SQ SEQUENCE 519 AA; 56874 MW; B695FCCA71586013 CRC64;
MKGSPVLAVC AAALTLIPSV VALPMIDKDL PSSISQSSDK TSQERAEAVK AAFRFAWEGY
LEHAFPNDEL HPVSNTPGNS RNGWGASAVD ALSTAIIMDM PDVVEKILDH ISNIDYSQTD
TMCSLFETTI RYLGGMISAY DLLKGPGSHL VSDPAKVDVL LAQSLKLADV LKFAFDTKTG
IPANELNITD KSTDGSTTNG LATTGTLVLE WTRLSDITGD PEYGRLAQKG ESYLLNPQPS
SSEPFPGLVG RTIDIETGLF RDDYVSWGGG SDSFYEYLIK MYVYDKGRFG KYKDRWVTAA
ESTIEHLKSS PSTRKDLTFV ATYSGGRLGL NSGHLTCFDG GNFLLGGQIL NRDDFTKFGL
ELVEGCYATY AATATKIGPE GFGWDATKVP EAQAEFYKEA GFYITTSYYN LRPEVIESIY
YAYRMTKDPK YQEWAWDAFV AINATTRTST GFTAIGDVNT PDGGRKYDNQ ESFLFAEVMK
YSYLIHSPEA DWQVAGPGGT NAYVFNTEAH PVKVFSRGC
