MA1A1_SPOFR
ID MA1A1_SPOFR Reviewed; 670 AA.
AC O18498;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Mannosyl-oligosaccharide alpha-1,2-mannosidase IA {ECO:0000305};
DE EC=3.2.1.113 {ECO:0000269|PubMed:10764822, ECO:0000269|PubMed:9147053};
DE AltName: Full=Alpha-1,2-mannosidase {ECO:0000303|PubMed:10764822, ECO:0000303|PubMed:11222938, ECO:0000303|PubMed:9147053};
DE AltName: Full=Class I alpha-1,2-mannosidase {ECO:0000303|PubMed:10764822};
DE AltName: Full=Man(9)-alpha-mannosidase {ECO:0000305};
DE AltName: Full=SfManI {ECO:0000303|PubMed:10764822, ECO:0000303|PubMed:11222938, ECO:0000303|PubMed:9147053};
OS Spodoptera frugiperda (Fall armyworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7108 {ECO:0000312|EMBL:AAB62720.1};
RN [1] {ECO:0000312|EMBL:AAB62720.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=9147053; DOI=10.1093/glycob/7.3.433;
RA Kawar Z., Herscovics A., Jarvis D.L.;
RT "Isolation and characterization of an alpha 1,2-mannosidase cDNA from the
RT lepidopteran insect cell line Sf9.";
RL Glycobiology 7:433-443(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=10764822; DOI=10.1093/glycob/10.4.347;
RA Kawar Z., Romero P.A., Herscovics A., Jarvis D.L.;
RT "N-Glycan processing by a lepidopteran insect alpha1,2-mannosidase.";
RL Glycobiology 10:347-355(2000).
RN [3]
RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-61, AND MUTAGENESIS OF ASN-61
RP AND 62-ASP-SER-63.
RX PubMed=11222938; DOI=10.1016/s0965-1748(00)00121-1;
RA Kawar Z., Jarvis D.L.;
RT "Biosynthesis and subcellular localization of a lepidopteran insect alpha
RT 1,2-mannosidase.";
RL Insect Biochem. Mol. Biol. 31:289-297(2001).
CC -!- FUNCTION: Involved in the maturation of Asn-linked oligosaccharides.
CC Converts Man(9)GlcNAc(2) to Man(5)GlcNAc(2) primarily through the
CC Man(7)GlcNAc(2) isomer C processing intermediate.
CC {ECO:0000269|PubMed:10764822}.
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:0000269|PubMed:10764822, ECO:0000269|PubMed:9147053};
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|PubMed:10764822};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q2ULB2};
CC -!- ACTIVITY REGULATION: Strongly inhibited by 1-deoxymannojirimycin, an
CC inhibitor of class I alpha-mannosidases, and by EDTA. EDTA inhibition
CC is reversed by the addition of calcium, but not of magnesium.
CC {ECO:0000269|PubMed:9147053}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P32906}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:11222938}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8H116}. Note=Localizes in cytoplasmic punctate
CC structures representing Golgi elements. {ECO:0000269|PubMed:11222938}.
CC -!- PTM: N-glycosylated (PubMed:10764822, PubMed:11222938). Contains high
CC mannose-type oligosaccharides (PubMed:11222938).
CC {ECO:0000269|PubMed:10764822, ECO:0000269|PubMed:11222938}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
CC {ECO:0000255|RuleBase:RU361193}.
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DR EMBL; AF005035; AAB62720.1; -; mRNA.
DR AlphaFoldDB; O18498; -.
DR SMR; O18498; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR UniPathway; UPA00378; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IDA:UniProtKB.
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; Disulfide bond; Glycoprotein; Glycosidase; Golgi apparatus;
KW Hydrolase; Membrane; Metal-binding; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..670
FT /note="Mannosyl-oligosaccharide alpha-1,2-mannosidase IA"
FT /id="PRO_0000450598"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..670
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 135..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 526
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT BINDING 637
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:11222938"
FT DISULFID 480..512
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT MUTAGEN 61
FT /note="N->S: Loss of N-glycosylation."
FT /evidence="ECO:0000269|PubMed:11222938"
FT MUTAGEN 62..63
FT /note="DS->ST: Increased N-glycosylation."
FT /evidence="ECO:0000269|PubMed:11222938"
SQ SEQUENCE 670 AA; 75242 MW; A2DA1104C9F1510C CRC64;
MTGILPTYQR FVNGVPVPSI SRRSFRLREK YLIVSVLLTF GIVWLGALFY LPEFKSSNSV
NDSVYNVYKR IQKAGPELLM PPPLAQNDVG DFPVIGIAHH GEGGDDPHVI EDRNRLRAKI
EEDMGMKVLE RPQFDVAPSV SSSRGPSKPP VDAIEEPAVG NNAANKDVSP SGPKAESSDK
FVAVALAPGA DPEIKHKLET VKKMMLHAWY NYKLYAWGKN ELKPMSKRAH LSSVFGAGEL
GATIVDGLDT LYLMGLNDEF REGRDWVAEH LHINEIDSDL SVFETTIRFV GGLLSCYALT
GDTMFRDKAA EVGDALLPAF DTPTGLPYAL INPSTKASRQ YHWAGPNSIL SELGTLHLEF
TYLSDVTGRD IYRQKVSRIR EVLDQIDKPG DLYPNFINPR TGQWGQRHMS LGALGDSFYE
YLLKAWLMSG GADEQARIMF DTAMQAALDK MLRVSPSGLA YLAELKYGRI IEEKMDHLSC
FAGGMFALAS TTLDNSMSER YMDVAKKLTN TCHESYARSE TKLGPEAFRF SNAAEARAQK
SNEKVYLLRP ETFESYFIMW RLTKQQMYRD WAWEAVQALE KHCRVEGGYT GLVNVYHANP
QGDDVQQSFF LAETLKYLYL IFGDDSFLPL DEWVFNTEAH PFPIRGKNPL YRAVDKPVLP
EPAHAQNNRI
