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 24-JAN-2024, entry version 139. 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)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan CC mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man- CC (1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]- CC beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl- CC [protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, CC Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; CC EC=3.2.1.113; 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 beta-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)-beta-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)-beta-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q9C512; -. DR CAZy; GH47; Glycoside Hydrolase Family 47. DR GlyCosmos; Q9C512; 2 sites, No reported glycans. DR iPTMnet; Q9C512; -. DR PaxDb; 3702-AT1G51590-1; -. 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; AT1G51590; MNS1. DR eggNOG; KOG2204; Eukaryota. DR InParanoid; Q9C512; -. DR OMA; PESFGWD; -. DR OrthoDB; 942598at2759; -. DR PhylomeDB; Q9C512; -. DR BioCyc; ARA:AT1G51590-MONOMER; -. 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 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; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-EC. 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 PANTHER; PTHR11742:SF6; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE IA-RELATED; 1. DR PANTHER; PTHR11742; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED; 1. DR Pfam; PF01532; Glyco_hydro_47; 1. DR PRINTS; PR00747; GLYHDRLASE47. DR SUPFAM; SSF48225; Seven-hairpin glycosidases; 1. DR Genevisible; Q9C512; AT. 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 //