ID   MA1B1_MOUSE             Reviewed;         658 AA.
AC   A2AJ15;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase;
DE            EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE   AltName: Full=ER alpha-1,2-mannosidase;
DE   AltName: Full=ER mannosidase 1;
DE            Short=ERMan1;
DE   AltName: Full=Man9GlcNAc2-specific-processing alpha-mannosidase;
DE   AltName: Full=Mannosidase alpha class 1B member 1;
GN   Name=Man1b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in glycoprotein quality control targeting of
CC       misfolded glycoproteins for degradation. It primarily trims a single
CC       alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce
CC       Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER
CC       quality control compartment (ERQC), it further trims the carbohydrates
CC       to Man(5-6)GlcNAc(2) (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:P32906};
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:0000250|UniProtKB:P32906};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P45700};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P32906}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC       II membrane protein.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR   EMBL; AL732557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466542; EDL08233.1; -; Genomic_DNA.
DR   EMBL; BC138550; AAI38551.1; -; mRNA.
DR   EMBL; BC138551; AAI38552.1; -; mRNA.
DR   CCDS; CCDS15765.1; -.
DR   RefSeq; NP_001025154.1; NM_001029983.2.
DR   AlphaFoldDB; A2AJ15; -.
DR   SMR; A2AJ15; -.
DR   BioGRID; 230645; 3.
DR   STRING; 10090.ENSMUSP00000036996; -.
DR   iPTMnet; A2AJ15; -.
DR   PhosphoSitePlus; A2AJ15; -.
DR   SwissPalm; A2AJ15; -.
DR   EPD; A2AJ15; -.
DR   MaxQB; A2AJ15; -.
DR   PaxDb; 10090-ENSMUSP00000036996; -.
DR   PeptideAtlas; A2AJ15; -.
DR   ProteomicsDB; 292073; -.
DR   Pumba; A2AJ15; -.
DR   Antibodypedia; 32359; 164 antibodies from 24 providers.
DR   DNASU; 227619; -.
DR   Ensembl; ENSMUST00000042390.5; ENSMUSP00000036996.5; ENSMUSG00000036646.14.
DR   GeneID; 227619; -.
DR   KEGG; mmu:227619; -.
DR   UCSC; uc008irp.2; mouse.
DR   AGR; MGI:2684954; -.
DR   CTD; 11253; -.
DR   MGI; MGI:2684954; Man1b1.
DR   VEuPathDB; HostDB:ENSMUSG00000036646; -.
DR   eggNOG; KOG2431; Eukaryota.
DR   GeneTree; ENSGT00940000155422; -.
DR   HOGENOM; CLU_003818_3_3_1; -.
DR   InParanoid; A2AJ15; -.
DR   OMA; AAFKHSW; -.
DR   OrthoDB; 942598at2759; -.
DR   PhylomeDB; A2AJ15; -.
DR   TreeFam; TF354274; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 227619; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Man1b1; mouse.
DR   PRO; PR:A2AJ15; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A2AJ15; Protein.
DR   Bgee; ENSMUSG00000036646; Expressed in spermatocyte and 218 other cell types or tissues.
DR   ExpressionAtlas; A2AJ15; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IMP:MGI.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006058; P:mannoprotein catabolic process; IEA:Ensembl.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:MGI.
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; A2AJ15; MM.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Endoplasmic reticulum; Glycosidase; Hydrolase;
KW   Membrane; Metal-binding; Phosphoprotein; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..658
FT                   /note="Endoplasmic reticulum mannosyl-oligosaccharide 1,2-
FT                   alpha-mannosidase"
FT                   /id="PRO_0000396622"
FT   TOPO_DOM        1..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..658
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          123..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        289
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        529
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P31723"
FT   ACT_SITE        558
FT                   /evidence="ECO:0000250"
FT   BINDING         647
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P32906"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   DISULFID        486..515
FT                   /evidence="ECO:0000250|UniProtKB:P32906"
SQ   SEQUENCE   658 AA;  75150 MW;  75BA990FA9B1470B CRC64;
     MYPPPAPPPA PHRDFISVTL SLGESYDNSK SRRRRSCWRK WKQLSRLQRN VILFVLGFLI
     LCGFLYSLHT ADQWKALSGR PAEVEKMKQE VLPVLPAPQK ESAEQEGFAD ILSQKRQRHF
     RRGPPHLQIR PPNTVSKDGM QDDAKEREAA LGKAQQEENT QRTVISWRGA VIEPEQATEL
     PYKRAEASIK PLVLASKIWK EPAPPNERQK GVIEAFLHAW KGYQKFAWGH DELKPVSKTF
     SEWFGLGLTL IDALDTMWIL GLKQEFKQAR KWVSENLDFQ KNVDVNLFES TIRILGGLLS
     TYHLSGDSLF LTKAEDFGKR LMPAFTTPSK IPYSDVNIGT GFAHSPQWTS DSTVAEVTSI
     QLEFRELSRL TGIKKFQEAV EEVTKHIHSL SGKKDGLVPM FINTNSGLFT HPGVFTLGAR
     ADSYYEYLLK QWIQGGKKET QLLEDYVKAI EGIKAHLLRQ SQPRKLTFVG ELAHGRFSAK
     MDHLVCFLPG TLALGVHHGL PADHMDLARA LMETCYQMNQ QMETGLSPEI AHFNMYPRAD
     HKDVEVKPAD RHNLLRPETV ESLFYLYRVT RDRKYQDWGW EILQSFNKYT RVPSGGYSSI
     NNVQNSHKPE PRDKMESFFV GETLKYLYLL FSDDLELLSL DSCVFNTEAH PLPIWAPA
//