MA1A2_MOUSE
ID MA1A2_MOUSE Reviewed; 641 AA.
AC P39098; Q5SUY6; Q5SUY7; Q60599; Q9CUY9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB;
DE EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE AltName: Full=Mannosidase alpha class 1A member 2;
DE AltName: Full=Processing alpha-1,2-mannosidase IB;
DE Short=Alpha-1,2-mannosidase IB;
GN Name=Man1a2; Synonyms=Man1b;
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 [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Fibroblast;
RX PubMed=8144579; DOI=10.1016/s0021-9258(17)36963-6;
RA Herscovics A.A., Schneikert J., Athanassiadis A., Moremen K.W.;
RT "Isolation of a mouse Golgi mannosidase cDNA, a member of a gene family
RT conserved from yeast to mammals.";
RL J. Biol. Chem. 269:9864-9871(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Ola;
RX PubMed=9143489; DOI=10.1006/geno.1997.4663;
RA Campbell-Dyke N., Athanassiadis A., Herscovics A.;
RT "Genomic organization and chromosomal mapping of the murine alpha 1,2-
RT mannosidase IB involved in N-glycan maturation.";
RL Genomics 41:155-159(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, and Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOD;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, 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 the maturation of Asn-linked oligosaccharides.
CC Progressively trim alpha-1,2-linked mannose residues from
CC Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
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 -!- ACTIVITY REGULATION: Inhibited by both 1-deoxymannojirimycin and
CC kifunensine. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P32906}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P39098-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P39098-2; Sequence=VSP_018615;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; U03458; AAB60439.1; -; mRNA.
DR EMBL; U03457; AAB60438.1; -; mRNA.
DR EMBL; AF078095; AAC34829.1; -; Genomic_DNA.
DR EMBL; AF078083; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078084; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078085; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078086; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078087; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078088; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078089; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078090; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078091; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078092; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078093; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AF078094; AAC34829.1; JOINED; Genomic_DNA.
DR EMBL; AK013515; BAB28892.3; -; mRNA.
DR EMBL; AK153336; BAE31915.1; -; mRNA.
DR EMBL; AL645760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049121; AAH49121.1; -; mRNA.
DR EMBL; BC068192; AAH68192.1; -; mRNA.
DR CCDS; CCDS17676.1; -. [P39098-1]
DR PIR; A54407; A54407.
DR RefSeq; NP_034893.1; NM_010763.2. [P39098-1]
DR AlphaFoldDB; P39098; -.
DR SMR; P39098; -.
DR BioGRID; 201303; 4.
DR STRING; 10090.ENSMUSP00000008907; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR GlyGen; P39098; 1 site.
DR iPTMnet; P39098; -.
DR PhosphoSitePlus; P39098; -.
DR EPD; P39098; -.
DR MaxQB; P39098; -.
DR PaxDb; P39098; -.
DR PeptideAtlas; P39098; -.
DR PRIDE; P39098; -.
DR ProteomicsDB; 252705; -. [P39098-1]
DR ProteomicsDB; 252706; -. [P39098-2]
DR Antibodypedia; 33890; 96 antibodies from 25 providers.
DR DNASU; 17156; -.
DR Ensembl; ENSMUST00000008907; ENSMUSP00000008907; ENSMUSG00000008763. [P39098-1]
DR GeneID; 17156; -.
DR KEGG; mmu:17156; -.
DR UCSC; uc008qqw.3; mouse. [P39098-1]
DR CTD; 10905; -.
DR MGI; MGI:104676; Man1a2.
DR VEuPathDB; HostDB:ENSMUSG00000008763; -.
DR eggNOG; KOG2204; Eukaryota.
DR GeneTree; ENSGT00940000157498; -.
DR HOGENOM; CLU_003818_3_2_1; -.
DR InParanoid; P39098; -.
DR OMA; LIKMYLY; -.
DR OrthoDB; 693882at2759; -.
DR PhylomeDB; P39098; -.
DR TreeFam; TF313420; -.
DR BRENDA; 3.2.1.113; 3474.
DR BRENDA; 3.2.1.209; 3474.
DR Reactome; R-MMU-964827; Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 17156; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Man1a2; mouse.
DR PRO; PR:P39098; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P39098; protein.
DR Bgee; ENSMUSG00000008763; Expressed in undifferentiated genital tubercle and 259 other tissues.
DR ExpressionAtlas; P39098; baseline and differential.
DR Genevisible; P39098; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009100; P:glycoprotein metabolic process; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; 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 Acetylation; Alternative splicing; Calcium; Disulfide bond; Glycoprotein;
KW Glycosidase; Golgi apparatus; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60476"
FT CHAIN 2..641
FT /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB"
FT /id="PRO_0000210313"
FT TOPO_DOM 2..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..641
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 508
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT BINDING 619
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:O60476"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 462..494
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT VAR_SEQ 259..285
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018615"
FT CONFLICT 411
FT /note="M -> T (in Ref. 1; AAB60438)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="F -> L (in Ref. 1; AAB60438)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="F -> S (in Ref. 1; AAB60438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 72871 MW; 7747FE57CCB2C4C5 CRC64;
MTTPALLPLS GRRIPPLNLG PPSFPHHRAT LRLSEKFILL LILSAFITLC FGAFFFLPDS
SKHKRFDLGL EDVLIPHVDA GKGAKNPGVF LIHGPDEHRH REEEERLRNK IRADHEKALE
EAKEKLRKSR EEIRAEIQTE KNKVAQAMKT KETRVLPPVP VPQRVGVSGG DPEDMEIKKK
RDKIKEMMKH AWDNYRTYGW GHNELRPIAR KGHSTNIFGS SQMGATIVDA LDTLYIMGLH
DEFMDGQRWI EENLDFSVNS EVSVFEVNIR FIGGLLAAYY LSGEEIFKTK AVQLAEKLLP
AFNTPTGIPW AMVNLKSGVG RNWGWASAGS SILAEFGTLH MEFVHLSYLT GDLTYYNKVM
HIRKLLQKME RPNGLYPNYL NPRTGRWGQY HTSVGGLGDS FYEYLLKAWL MSDKTDHEAR
RMYDDAVEAI EKHLIKKSRG GLVFIGEWKN GHLERKMGHL ACFAGGMFAL GADGSRKDKA
GHYLELGAEI ARTCHESYDR TALKLGPESF KFDGAVEAVA VRQAEKYYIL RPEVIETYWY
LWRFTHDPRY RQWGWEAALA IEKSCRVSGG FSGVKDVYAP TPVHDDVQQS FFLAETLKYL
YLLFSGDDLL PLDHWVFNTE AHPLPVLRLA NSTLSGNPAV R
