MA1B1_RAT
ID MA1B1_RAT Reviewed; 657 AA.
AC B2GUY0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=Mannosidase alpha class 1B member 1;
GN Name=Man1b1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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).
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; BC166449; AAI66449.1; -; mRNA.
DR RefSeq; NP_001102666.1; NM_001109196.1.
DR AlphaFoldDB; B2GUY0; -.
DR SMR; B2GUY0; -.
DR IntAct; B2GUY0; 1.
DR STRING; 10116.ENSRNOP00000016846; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR jPOST; B2GUY0; -.
DR PaxDb; B2GUY0; -.
DR PeptideAtlas; B2GUY0; -.
DR GeneID; 499751; -.
DR KEGG; rno:499751; -.
DR UCSC; RGD:1563595; rat.
DR CTD; 11253; -.
DR RGD; 1563595; Man1b1.
DR VEuPathDB; HostDB:ENSRNOG00000012559; -.
DR eggNOG; KOG2431; Eukaryota.
DR HOGENOM; CLU_003818_3_3_1; -.
DR InParanoid; B2GUY0; -.
DR OMA; AAFKHSW; -.
DR OrthoDB; 693882at2759; -.
DR PhylomeDB; B2GUY0; -.
DR TreeFam; TF354274; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:B2GUY0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000012559; Expressed in pancreas and 19 other tissues.
DR Genevisible; B2GUY0; RN.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; ISO:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; ISO:RGD.
DR GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; ISO:RGD.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0036508; P:protein alpha-1,2-demannosylation; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0036509; P:trimming of terminal mannose on B branch; ISO:RGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD.
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 2: Evidence at transcript 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..657
FT /note="Endoplasmic reticulum mannosyl-oligosaccharide 1,2-
FT alpha-mannosidase"
FT /id="PRO_0000396623"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..657
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 118..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 288
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 421
FT /evidence="ECO:0000250"
FT ACT_SITE 528
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT ACT_SITE 557
FT /evidence="ECO:0000250"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AJ15"
FT DISULFID 485..514
FT /evidence="ECO:0000250|UniProtKB:P32906"
SQ SEQUENCE 657 AA; 74895 MW; A846B228A461367C CRC64;
MYPPPPAPAP HRDFISVTLS LGESYDNSKS RRRRSCWRKW KQLSRLQRNV ILFVLGFLIL
CGFLYSLQVS DQWKALSGSR AEVEKMKLEV LPVLPAPQKE SAEPEGFADI LSQKRQRHLR
RGPPHLQIRP PNTVSKDGMQ DDAKEREAAL GKAQQEENTQ RTVISWRGAV IEPEQATEPP
SKRAEASIKP LFLASRIWKE PAPPNERQKG VIEAFLHAWK GYQKFAWGHD ELKPVSKTFS
EWFGLGLTLI DALDTMWILG LKQEFKEARK WVSENLDFQK NVDVNLFEST IRILGGLLSA
YHLSGDSLFL SKAEDFGNRL MPAFTTPSKI PYSDVNIGTG FAHSPQWTSD STVAEVTSIQ
LEFRELSRLT GIKKFQEAVE EVTKHIHSLS GKKDGLVPMF INTNSGLFTH PGVFTLGARA
DSYYEYLLKQ WIQGGKKETQ LLEDYVRAIE GIKAHLLRQS QPRKLTFVGE LAHGRFSAKM
DHLVCFLPGT LALGVHHGLP ADHMDLARAL METCYQMNQQ METGLSPEIA HFNMYPRADH
KDVEVKPADR HNLLRPETVE SLFYLYRVTK DRKYQDWGWE ILQSFNKYTR VPSGGYSSIN
NVQNSHKPEP RDKMESFFVG ETLKYLYLLF SDDLELLGLD TCVFNTEAHP LPIWSPA
