MNS1B_ARTBC
ID MNS1B_ARTBC Reviewed; 509 AA.
AC D4AV26;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Probable mannosyl-oligosaccharide alpha-1,2-mannosidase ARB_00035 {ECO:0000305};
DE EC=3.2.1.113 {ECO:0000250|UniProtKB:E9CXX8};
DE AltName: Full=Class I alpha-mannosidase {ECO:0000250|UniProtKB:E9CXX8};
DE AltName: Full=Man(9)-alpha-mannosidase {ECO:0000250|UniProtKB:E9CXX8};
DE Flags: Precursor;
GN ORFNames=ARB_00035;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
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 {ECO:0000250|UniProtKB:E9CXX8}.
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:E9CXX8};
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:E9CXX8};
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:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; ABSU01000012; EFE32948.1; -; Genomic_DNA.
DR RefSeq; XP_003013588.1; XM_003013542.1.
DR AlphaFoldDB; D4AV26; -.
DR SMR; D4AV26; -.
DR STRING; 663331.D4AV26; -.
DR EnsemblFungi; EFE32948; EFE32948; ARB_00035.
DR GeneID; 9519867; -.
DR KEGG; abe:ARB_00035; -.
DR eggNOG; KOG2204; Eukaryota.
DR HOGENOM; CLU_003818_0_2_1; -.
DR OMA; LIKMYLY; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008866; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..509
FT /note="Probable mannosyl-oligosaccharide alpha-1,2-
FT mannosidase ARB_00035"
FT /id="PRO_5003053524"
FT ACT_SITE 374
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 331..360
FT /evidence="ECO:0000250|UniProtKB:P31723"
SQ SEQUENCE 509 AA; 56291 MW; 46EE8725BBCD8015 CRC64;
MKSLSLLGVS SLALTSLALP TMNQNQHRFV ALADLADEDK PQAIKDAFNH AWKGYMTHAY
PMDELRPVSN EGSNPLNGWG ATPVDALSTA IIMGLPDVVN QILDHISKID FSKTDDLCSL
FETTIRYLGG LISGYDLLKN SGAMNADPEK VDVLLKKAVE LADVLKFSFN STTGIPSNTL
NIPKQTTDGA TSNGLATVGT LVLEWTRLSD LTNKEEYGKL AQKAEEYLLN PQPKSNEVFP
GLVGGSINIQ TGKFERASAS WEGGDDSFYE YLIKMYVYDR SAFGKYKDRW VLAAQSTIEH
LKSSPLLHPD TTFVGAWANG ALVKSSQHLA CFDGGNFILG GRELNRPEFT RFGLKLVDGC
HKTYANTVTK IGPESFGWDE KNVPSDQASF FTKSGFYINS SGYVLRPEVI ESFYYAYRVT
GDKKYQRWIW DAFVAISETT KTDSGFSSIS DVNAAKGGSK TDSQPSFFFA ETLKYTYLAF
SDEADWQISR SGKDKFVFNT EAHPIRVRN
