MNS3_ARATH
ID MNS3_ARATH Reviewed; 624 AA.
AC Q93Y37; Q9C8R9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3;
DE EC=3.2.1.113 {ECO:0000269|PubMed:20023195};
DE EC=3.2.1.209 {ECO:0000269|PubMed:20023195};
GN Name=MNS3; OrderedLocusNames=At1g30000; ORFNames=T1P2.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND COFACTOR.
RX PubMed=20023195; DOI=10.1105/tpc.109.072363;
RA Liebminger E., Huttner S., Vavra U., Fischl R., Schoberer J., Grass J.,
RA Blaukopf C., Seifert G.J., Altmann F., Mach L., Strasser R.;
RT "Class I alpha-mannosidases are required for N-glycan processing and root
RT development in Arabidopsis thaliana.";
RL Plant Cell 21:3850-3867(2009).
CC -!- FUNCTION: Class I alpha-mannosidase essential for early N-glycan
CC processing. Removes preferentially alpha-1,2-linked mannose residues
CC from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root
CC development and cell wall biosynthesis. {ECO:0000269|PubMed:20023195}.
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:20023195};
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:20023195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 9A1,2,3B1,2,3) = beta-D-mannose + N(4)-(alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] (N-glucan mannose isomer 8A1,2,3B1,3);
CC Xref=Rhea:RHEA:56004, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14358,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:60628,
CC ChEBI:CHEBI:139493; EC=3.2.1.209;
CC Evidence={ECO:0000269|PubMed:20023195};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:20023195};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20023195};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20023195};
CC Note=Ca(2+) or Mn(2+). Mg(2+) can be used to a lesser extent.
CC {ECO:0000269|PubMed:20023195};
CC -!- ACTIVITY REGULATION: Inhibited by kifunensine and 1-
CC deoxymannojirimycin, but not by swainsonine.
CC {ECO:0000269|PubMed:20023195}.
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000305|PubMed:20023195}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:20023195}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, stems, leaves,
CC roots, stamens and sepals. {ECO:0000269|PubMed:20023195}.
CC -!- DISRUPTION PHENOTYPE: Formation of aberrant N-glycan structures.
CC {ECO:0000269|PubMed:20023195}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022455; AAG52061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31166.1; -; Genomic_DNA.
DR EMBL; AY054482; AAK96673.1; -; mRNA.
DR EMBL; AY093280; AAM13279.1; -; mRNA.
DR PIR; H86423; H86423.
DR RefSeq; NP_564345.1; NM_102740.3.
DR AlphaFoldDB; Q93Y37; -.
DR SMR; Q93Y37; -.
DR STRING; 3702.AT1G30000.1; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR SwissPalm; Q93Y37; -.
DR PaxDb; Q93Y37; -.
DR PRIDE; Q93Y37; -.
DR ProteomicsDB; 238294; -.
DR EnsemblPlants; AT1G30000.1; AT1G30000.1; AT1G30000.
DR GeneID; 839879; -.
DR Gramene; AT1G30000.1; AT1G30000.1; AT1G30000.
DR KEGG; ath:AT1G30000; -.
DR Araport; AT1G30000; -.
DR TAIR; locus:2198299; AT1G30000.
DR eggNOG; KOG2431; Eukaryota.
DR HOGENOM; CLU_003818_3_1_1; -.
DR InParanoid; Q93Y37; -.
DR OMA; AAFKHSW; -.
DR PhylomeDB; Q93Y37; -.
DR BRENDA; 3.2.1.209; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q93Y37; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93Y37; baseline and differential.
DR Genevisible; Q93Y37; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0004559; F:alpha-mannosidase activity; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; Golgi apparatus; Hydrolase;
KW Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..624
FT /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3"
FT /id="PRO_0000397935"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..624
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 91..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 357
FT /evidence="ECO:0000250"
FT ACT_SITE 485
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT ACT_SITE 526
FT /evidence="ECO:0000250"
FT BINDING 613
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 428..471
FT /evidence="ECO:0000250|UniProtKB:P32906"
SQ SEQUENCE 624 AA; 69069 MW; A28B82AD7FAAD29D CRC64;
MSKSLPYSVK DIHYDNAKFR HRSPLKVFSQ SLLTLSTKRN YASCSTGKFL ILILFFGVAC
LMLMSKSPNE SGLNEKGKVT FVGGLRLGGL LRKPPRLPPR LSPDEGQLRG SSTNGSTISN
SDPKWAARQQ SVKEAFDHAW SGYRKYAMGY DELMPISQKG VDGLGGLGAT VVDALDTAMI
MGLDNIVSEA GSWVETHLLE RISQKGQVNL FETTIRVLGG LLSAYHLSGG EQGTVNMTHV
GPKPVIYLNI AKDLADRLLS AFTSSPTPVP FCDVILHEST AHPAPGGASS TAEVASVQLE
FNYLSSISGD PKYSTEAMKV LAHIKTLPKT EGLVPIYISP QTGDFVGENI RLGSRGDSYY
EYLIKVWLQQ GAKLNSNFTY LHDMYIEAMK GVRHLLVQNS IPKGLVFVGE LPYGSKGEFS
PKMDHLVCFL PGTLALGATK GLTKEQALKE NLLSFEDLEN LKLAEDLAKT CFEMYEVTAT
GLAPEIAYFH TKDYTEDGLD GGNKSSMYAN DIIIKPADRH NLLRPETVES LFVLYRITKD
TKYRDQGWQI FEAFEKYTKV KSGGYTSLDD VTEVPPHRRD KMETFFLGET LKYLYLLFGD
DSVIPLDKFV FNTEAHPLPI RRNT
