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   24-JAN-2024, entry version 129.
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)-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: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         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: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)-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: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.Q93Y37; -.
DR   CAZy; GH47; Glycoside Hydrolase Family 47.
DR   GlyCosmos; Q93Y37; 5 sites, No reported glycans.
DR   SwissPalm; Q93Y37; -.
DR   PaxDb; 3702-AT1G30000-1; -.
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; AT1G30000; MNS3.
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   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:0016020; C: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; 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:SF55; ENDOPLASMIC RETICULUM MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE; 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; Q93Y37; AT.
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
//