MAN2_SPOFR
ID MAN2_SPOFR Reviewed; 1130 AA.
AC O18497;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Alpha-mannosidase 2 {ECO:0000305};
DE EC=3.2.1.114 {ECO:0000269|PubMed:9061370};
DE AltName: Full=Alpha-mannosidase II {ECO:0000303|PubMed:9061370};
DE AltName: Full=Class II alpha-mannosidase {ECO:0000303|PubMed:9061370};
DE AltName: Full=Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase {ECO:0000305};
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:AAB62719.1};
RN [1] {ECO:0000312|EMBL:AAB62719.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=9061370; DOI=10.1093/glycob/7.1.113;
RA Jarvis D.L., Bohlmeyer D.A., Liao Y.F., Lomax K.K., Merkle R.K.,
RA Weinkauf C., Moremen K.W.;
RT "Isolation and characterization of a class II alpha-mannosidase cDNA from
RT lepidopteran insect cells.";
RL Glycobiology 7:113-127(1997).
CC -!- FUNCTION: Catalyzes the first committed step in the biosynthesis of
CC complex N-glycans. It controls conversion of high mannose to complex N-
CC glycans; the final hydrolytic step in the N-glycan maturation pathway.
CC {ECO:0000250|UniProtKB:P28494}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-
CC D-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 2 alpha-D-mannopyranose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein]; Xref=Rhea:RHEA:56052,
CC Rhea:RHEA-COMP:14368, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28729, ChEBI:CHEBI:60615, ChEBI:CHEBI:60625;
CC EC=3.2.1.114; Evidence={ECO:0000269|PubMed:9061370};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|RuleBase:RU361199};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|RuleBase:RU361199};
CC -!- ACTIVITY REGULATION: Inhibited by swainsonine.
CC {ECO:0000269|PubMed:9061370}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P28494}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P28494}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9061370};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:9061370}.
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:Q24451}; Single-pass
CC type II membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9061370}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000255|RuleBase:RU361199}.
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DR EMBL; AF005034; AAB62719.1; -; mRNA.
DR PIR; T29089; T29089.
DR AlphaFoldDB; O18497; -.
DR SMR; O18497; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR UniPathway; UPA00378; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004572; F:mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IDA:UniProtKB.
DR GO; GO:0006491; P:N-glycan processing; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Golgi apparatus; Hydrolase; Membrane; Metal-binding; Microsome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..1130
FT /note="Alpha-mannosidase 2"
FT /id="PRO_0000450694"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..1130
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 247
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1056
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1095
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 553
FT /note="Interchain (with C-414)"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
SQ SEQUENCE 1130 AA; 131066 MW; 2714BC98775E2DDA CRC64;
MRTRVLRCRP FSTRILLLLL FVLAFGVYCY FYNASPQNYN KPRISYPASM EHFKSSLTHT
VKSRDEPTPD QCPALKESEA DIDTVAIYPT FDFQPSWLRT KEFWDKSFED RYERIHNDTT
RPRLKVIVVP HSHNDPGWLK TFEQYFEWKT KNIINNIVNK LHQYPNMTFI WTEISFLNAW
WERSHPVKQK ALKKLIKEGR LEITTGGWVM PDEACTHIYA LIDQFIEGHH WVKTNLGVIP
KTGWSIDPFG HGATVPYLLD QSGLEGTIIQ RIHYAWKQWL AERQIEEFYW LASWATTKPS
MIVHNQPFDI YSIKSTCGPH PSICLSFDFR KIPGEYSEYT AKHEDITEHN LHSKAKTLIE
EYDRIGSLTP HNVVLVPLGD DFRYEYSVEF DAQYVNYMKM FNYINAHKEI FNADVQFGTP
LDYFNAMKER HQNIPSLKGD FFVYSDIFSE GKPAYWSGYY TTRPYQKILA RQFEHQLRSA
EILFTLVSNY IRQMGRQGEF GASEKKLEKS YEQLIYARRN LGLFQHHDAI TGTSKSSVMQ
DYGTKLFTSL YHCIRLQEAA LTTIMLPDQS LHSQSIIQSE VEWETYGKPP KKLQVSFIDK
KKVILFNPLA ETRTEVVTVR SNTSNIRVYD THKRKHVLYQ IMPSITIQDN GKSIVSDTTF
DIMFVATIPP LTSISYKLQE HTNTSHHCVI FCNNCEQYQK SNVFQIKKMM PGDIQLENAV
LKLLVNRNTG FLRQVYRKDI RKRTVVDVQF GAYQSAQRHS GAYLFMPHYD SPEKNVLHPY
TNQNNMQDDN IIIVSGPIST EITTMYLPFL VHTIRIYNVP DPVLSRAILL ETDVDFEAPP
KNRETELFMR LQTDIQNGDI PEFYTDQNGF QYQKRVKVNK LGIEANYYPI TTMACLQDEE
TRLTLLTNHA QGAAAYEPGR LEVMLDRRTL YDDFRGIGEG VVDNKPTTFQ NWILIESMPG
VTRAKRDTSE PGFKFVNERR FGPGQKESPY QVPSQTADYL SRMFNYPVNV YLVDTSEVGE
IEVKPYQSFL QSFPPGIHLV TLRTITDDVL ELFPSNESYM VLHRPGYSCA VGEKPVAKSP
KFSSKTRFNG LNIQNITAVS LTGLKSLRPL TGLSDIHLNA MEVKTYKIRF
