MA1B1_MOUSE
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 03-AUG-2022, entry version 107.
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)-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: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 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: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; A2AJ15; -.
DR PeptideAtlas; A2AJ15; -.
DR PRIDE; A2AJ15; -.
DR ProteomicsDB; 292073; -.
DR Antibodypedia; 32359; 145 antibodies from 24 providers.
DR DNASU; 227619; -.
DR Ensembl; ENSMUST00000042390; ENSMUSP00000036996; ENSMUSG00000036646.
DR GeneID; 227619; -.
DR KEGG; mmu:227619; -.
DR UCSC; uc008irp.2; mouse.
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; 693882at2759; -.
DR PhylomeDB; A2AJ15; -.
DR TreeFam; TF354274; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 227619; 2 hits in 72 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 214 other tissues.
DR ExpressionAtlas; A2AJ15; baseline and differential.
DR Genevisible; A2AJ15; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:1904380; P:endoplasmic reticulum mannose trimming; ISO:MGI.
DR GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; ISO:MGI.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0036508; P:protein alpha-1,2-demannosylation; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0036509; P:trimming of terminal mannose on B branch; ISO:MGI.
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 Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 1.
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
