MNS2_ARATH
ID MNS2_ARATH Reviewed; 572 AA.
AC Q8H116; Q94A04; Q9LJB6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2;
DE Short=AtMANIa;
DE EC=3.2.1.113 {ECO:0000269|PubMed:19914916};
DE AltName: Full=Alpha-mannosidase IA;
GN Name=MNS2; Synonyms=MANIA; OrderedLocusNames=At3g21160; ORFNames=MSA6.31;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP 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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19914916; DOI=10.1093/glycob/cwp170;
RA Kajiura H., Koiwa H., Nakazawa Y., Okazawa A., Kobayashi A., Seki T.,
RA Fujiyama K.;
RT "Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible
RT for plant N-glycan maturation.";
RL Glycobiology 20:235-247(2010).
CC -!- FUNCTION: Class I alpha-mannosidase essential for early N-glycan
CC processing. Progressively trims alpha-1,2-linked mannose residues.
CC Produces Man(5)GlcNAc(2) from Man(8)GlcNAc(2), but only Man(6)GlcNAc(2)
CC from Man(9)GlcNAc(2). Has difficulty acting on the terminal mannose of
CC the b-branch. Involved in root development and cell wall biosynthesis.
CC {ECO:0000269|PubMed:19914916, 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:19914916};
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:19914916};
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:19914916, ECO:0000269|PubMed:20023195}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. Stable from pH 5.0 to 10.0.
CC {ECO:0000269|PubMed:19914916};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:19914916};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19914916, ECO:0000269|PubMed:20023195}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:19914916,
CC ECO:0000269|PubMed:20023195}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, stems, leaves,
CC roots, pollen grains and shoot apical meristems.
CC {ECO:0000269|PubMed:19914916, ECO:0000269|PubMed:20023195}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due the redundancy with
CC MNS1. Lack of complex N-glycans, shorter roots and increased lateral
CC root formation in mns1 and mns2 double mutants.
CC {ECO:0000269|PubMed:19914916, ECO:0000269|PubMed:20023195}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01459.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000604; BAB01459.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB023045; BAB01459.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE76468.1; -; Genomic_DNA.
DR EMBL; AY050776; AAK92711.1; -; mRNA.
DR EMBL; BT000893; AAN41293.1; -; mRNA.
DR RefSeq; NP_566675.1; NM_113010.3.
DR AlphaFoldDB; Q8H116; -.
DR SMR; Q8H116; -.
DR BioGRID; 7000; 1.
DR IntAct; Q8H116; 1.
DR STRING; 3702.AT3G21160.1; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR PaxDb; Q8H116; -.
DR PRIDE; Q8H116; -.
DR ProteomicsDB; 239061; -.
DR EnsemblPlants; AT3G21160.1; AT3G21160.1; AT3G21160.
DR GeneID; 821668; -.
DR Gramene; AT3G21160.1; AT3G21160.1; AT3G21160.
DR KEGG; ath:AT3G21160; -.
DR Araport; AT3G21160; -.
DR TAIR; locus:2092965; AT3G21160.
DR eggNOG; KOG2204; Eukaryota.
DR HOGENOM; CLU_003818_3_2_1; -.
DR InParanoid; Q8H116; -.
DR OrthoDB; 693882at2759; -.
DR PhylomeDB; Q8H116; -.
DR BioCyc; ARA:AT3G21160-MON; -.
DR BRENDA; 3.2.1.113; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8H116; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H116; baseline and differential.
DR Genevisible; Q8H116; 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:0000137; C:Golgi cis cisterna; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; Coiled coil; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..572
FT /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2"
FT /id="PRO_0000397934"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..572
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 51..81
FT /evidence="ECO:0000255"
FT ACT_SITE 180
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 312
FT /evidence="ECO:0000250"
FT ACT_SITE 424
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT ACT_SITE 446
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 377..410
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CONFLICT 113
FT /note="Y -> H (in Ref. 4; AAK92711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 65136 MW; 14614DD4525F9499 CRC64;
MARNKLVSGS HGIWKYFNPA FYLRRPRRLA LLIILFVSVS MVVWDRQSLS RDYQFEVSKL
NEEVLRLQQM LEEIKSVTED VSVNSLKDVQ EDPVDAQRMQ RVKEAMVHAW SSYEKYAWGQ
DELQPQTKDG VDSFGGLGAT MIDALDTLYI MGLDEQFQKA REWVASSLDF DKDYAASMFE
TTIRVVGGLL SAYDLSGDKI FLEKAMDIAD RLLPAWDTQS GIPYNIINLK HGNAHNPTWA
GGDSILADSG TEQLEFIALS QRTGDPKYQQ KVEKVISVLN KNFPADGLLP IYINPDTANP
SQSTITFGAM GDSFYEYLLK VWVFGNKTSA VKHYRDMWEK SMNGLLSLVK KSTPLSFTYI
CEKSGNSLID KMDELACFAP GMLALGASGY SDPAEGKKFL TLAEELAWTC YNFYQSTPTK
LAGENYFFNS GSDMSVGTSW NILRPETVES LFYLWRLTGN KTYQEWGWNI FEAFEKNSRI
ESGYVGLKDV NTGVKDNKMQ SFFLAETLKY LYLLFSPTTV IPLDEWVFNT EAHPLKIKSR
NDQVNLKQSN KVLLRKPAFR IRQRHYGRIT KK
