ID   MNS1_SCHPO              Reviewed;         521 AA.
AC   Q9P7C3; Q9C0Z6;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase;
DE            EC=3.2.1.113 {ECO:0000269|PubMed:16079177};
DE   AltName: Full=ER alpha-1,2-mannosidase;
DE   AltName: Full=Man(9)-alpha-mannosidase;
GN   ORFNames=SPAC2E1P5.01c, SPAPB1E7.13c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=16079177; DOI=10.1091/mbc.e05-03-0246;
RA   Movsichoff F., Castro O.A., Parodi A.J.;
RT   "Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a
RT   reevaluation of the role of the enzyme on ER-associated degradation.";
RL   Mol. Biol. Cell 16:4714-4724(2005).
CC   -!- FUNCTION: Involved in glycoprotein quality control as it is important
CC       for the targeting of misfolded glycoproteins for degradation. It trims
CC       a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to
CC       produce Man(8)GlcNAc(2) with low efficiency.
CC       {ECO:0000269|PubMed:16079177}.
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:16079177};
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:16079177};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P45700};
CC   -!- ACTIVITY REGULATION: Inhibited by kifunensine.
CC       {ECO:0000269|PubMed:16079177}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P32906}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAC36930.1; -; Genomic_DNA.
DR   RefSeq; NP_594139.2; NM_001019563.2.
DR   AlphaFoldDB; Q9P7C3; -.
DR   SMR; Q9P7C3; -.
DR   STRING; 284812.Q9P7C3; -.
DR   CAZy; GH47; Glycoside Hydrolase Family 47.
DR   iPTMnet; Q9P7C3; -.
DR   MaxQB; Q9P7C3; -.
DR   PaxDb; 4896-SPAC2E1P5-01c-1; -.
DR   EnsemblFungi; SPAC2E1P5.01c.1; SPAC2E1P5.01c.1:pep; SPAC2E1P5.01c.
DR   GeneID; 2541719; -.
DR   KEGG; spo:SPAC2E1P5.01c; -.
DR   PomBase; SPAC2E1P5.01c; -.
DR   VEuPathDB; FungiDB:SPAC2E1P5.01c; -.
DR   eggNOG; KOG2431; Eukaryota.
DR   HOGENOM; CLU_003818_3_0_1; -.
DR   InParanoid; Q9P7C3; -.
DR   OMA; AAFKHSW; -.
DR   PhylomeDB; Q9P7C3; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q9P7C3; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IC:PomBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; ISM:PomBase.
DR   GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IMP:PomBase.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; IMP:PomBase.
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.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW   Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..521
FT                   /note="Endoplasmic reticulum mannosyl-oligosaccharide 1,2-
FT                   alpha-mannosidase"
FT                   /id="PRO_0000210320"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..521
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        387
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P31723"
FT   BINDING         504
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P32906"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        330..373
FT                   /evidence="ECO:0000250|UniProtKB:P32906"
SQ   SEQUENCE   521 AA;  60813 MW;  742E325D05EC8936 CRC64;
     MVKRRTVKYF LRRILALFVL CVPIYYLYTT VQRPPGYTKL KGSTRRKALI KKTFIESWTD
     YETYGWGKDE YYPIIKRGRN YLRKGMGWMI IDSLDTMMIM GLDEQVLRAR EWVNNSLTWN
     QDDEEVSVFE TTIRILGGLL SSYHLSQDKL YLDRAVDLAD RLLAAYNTST GLPRSNVNLG
     TRKSRKRTRE YFVSTAESGT VQMELRYLSY LTGDPKYWIT ADKTMEVLLG DATWSHTGLV
     PITVNLITGA YVGRNIRLGS HGDSYYEYLL KQDLQLFSSG TVYRKAFDLS VDGIIEYLLN
     YTTPNHFAYI AELPGGLEHA QLPKMDHLVC FLPGTLMWGA TNGTSLEAAR TSKNWGTRQE
     RDVKLAQELM RTCYEMYNMT ATGLAPEIVF FDVDQTKNEI YSKRRDQHNL MRPETVESLF
     ILYRITRDEI YREWGWNIFV SFLRYSRLPG RDAFTCLDSV ESKKVKDQRD KTESFWFAET
     LKYLYLLFED DFSILPLTNY TFNTEAHPFP NIENNMDLYT V
//