MNS1_ARATH
ID MNS1_ARATH Reviewed; 560 AA.
AC Q9C512; Q2V4H4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1;
DE Short=AtMANIb;
DE EC=3.2.1.113 {ECO:0000269|PubMed:19914916};
DE EC=3.2.1.209 {ECO:0000269|PubMed:19914916};
DE AltName: Full=Alpha-mannosidase IB;
GN Name=MNS1; Synonyms=MANIB; OrderedLocusNames=At1g51590;
GN ORFNames=F19C24.18, F5D21.1;
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, 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 [5]
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 -!- 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: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 6.0. Stable from pH 4.5 to 6.5.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C512-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C512-2; Sequence=VSP_039724;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, stems, leaves,
CC roots, pollen grains, shoot apical meristems, hypocotyls and upper
CC region of the root. {ECO:0000269|PubMed:19914916,
CC ECO:0000269|PubMed:20023195}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due the redundancy with
CC MNS2. 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}.
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DR EMBL; AC024261; AAG52623.1; -; Genomic_DNA.
DR EMBL; AC025294; AAG50876.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32686.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32687.1; -; Genomic_DNA.
DR EMBL; AY081353; AAL91242.1; -; mRNA.
DR EMBL; AY128845; AAM91245.1; -; mRNA.
DR PIR; E96554; E96554.
DR RefSeq; NP_001031171.1; NM_001036094.1. [Q9C512-2]
DR RefSeq; NP_175570.1; NM_104037.4. [Q9C512-1]
DR AlphaFoldDB; Q9C512; -.
DR SMR; Q9C512; -.
DR BioGRID; 26809; 2.
DR STRING; 3702.AT1G51590.1; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR PaxDb; Q9C512; -.
DR PRIDE; Q9C512; -.
DR ProteomicsDB; 251344; -. [Q9C512-1]
DR EnsemblPlants; AT1G51590.1; AT1G51590.1; AT1G51590. [Q9C512-1]
DR EnsemblPlants; AT1G51590.2; AT1G51590.2; AT1G51590. [Q9C512-2]
DR GeneID; 841584; -.
DR Gramene; AT1G51590.1; AT1G51590.1; AT1G51590. [Q9C512-1]
DR Gramene; AT1G51590.2; AT1G51590.2; AT1G51590. [Q9C512-2]
DR KEGG; ath:AT1G51590; -.
DR Araport; AT1G51590; -.
DR TAIR; locus:2017597; AT1G51590.
DR eggNOG; KOG2204; Eukaryota.
DR InParanoid; Q9C512; -.
DR OMA; PWNEEIW; -.
DR PhylomeDB; Q9C512; -.
DR BioCyc; ARA:AT1G51590-MON; -.
DR BRENDA; 3.2.1.113; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9C512; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C512; baseline and differential.
DR Genevisible; Q9C512; 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 Alternative splicing; Calcium; Coiled coil; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..560
FT /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1"
FT /id="PRO_0000397933"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..560
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 47..80
FT /evidence="ECO:0000255"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 312
FT /evidence="ECO:0000250"
FT ACT_SITE 423
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT ACT_SITE 445
FT /evidence="ECO:0000250"
FT BINDING 529
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 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 377..409
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039724"
SQ SEQUENCE 560 AA; 63532 MW; BCC20CB9E63020B9 CRC64;
MARSRSISGY GIWKYLNPAY YLRRPRRLAL LFIVFVSVSM LVWDRINLAR EHEVEVFKLN
EEVSRLEQML EELNGGVGNK PLKTLKDAPE DPVDKQRRQK VKEAMIHAWS SYEKYAWGKD
ELQPRTKDGT DSFGGLGATM VDSLDTLYIM GLDEQFQKAR EWVASSLDFD KDYDASMFET
TIRVVGGLLS AYDLSGDKMF LEKAKDIADR LLPAWNTPTG IPYNIINLRN GNAHNPSWAA
GGDSILADSG TEQLEFIALS QRTGDPKYQQ KVEKVITELN KNFPADGLLP IYINPDNANP
SYSTTTFGAM GDSFYEYLLK VWVQGNKTSA VKPYRDMWEK SMKGLLSLVK KSTPSSFTYI
CEKNGNNLID KMDELACFAP GMLALGASGY GPDEEKKFLS LAGELAWTCY NFYQSTPTKL
AGENYFFTAG QDMSVGTSWN ILRPETVESL FYLWRLTGNK TYQEWGWNIF QAFEKNSRVE
SGYVGLKDVN TGAKDNKMQS FFLAETLKYL YLLFSPSSVI SLDEWVFNTE AHPLKIVARN
DPRKPTIALR QRKFGHQINV
