MA2B1_MOUSE
ID MA2B1_MOUSE Reviewed; 1013 AA.
AC O09159; O55037; Q3UGH3; Q64443; Q9DBQ1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Lysosomal alpha-mannosidase;
DE Short=Laman;
DE EC=3.2.1.24;
DE AltName: Full=Lysosomal acid alpha-mannosidase;
DE AltName: Full=Mannosidase alpha class 2B member 1;
DE AltName: Full=Mannosidase alpha-B;
DE Flags: Precursor;
GN Name=Man2b1; Synonyms=Laman, Man2b, Manb;
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].
RC TISSUE=Macrophage;
RX PubMed=9355733; DOI=10.1042/bj3270045;
RA Beccari T., Appolloni M.G., Costanzi E., Stinchi S., Stirling J.L.,
RA Della Fazia M.A., Servillo G., Viola M.P., Orlacchio A.;
RT "Lysosomal alpha-mannosidases of mouse tissues: characteristics of the
RT isoenzymes, and cloning and expression of a full-length cDNA.";
RL Biochem. J. 327:45-49(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9799835; DOI=10.1007/s003359900885;
RA Stinchi S., Orlacchio A., Costanzi E., Stirling J.L., Menghini A.R.,
RA Orlacchio A., Beccari T.;
RT "Promoter characterization and structure of the gene encoding mouse
RT lysosomal alpha-d-mannosidase.";
RL Mamm. Genome 9:869-873(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-1013.
RC TISSUE=Liver;
RX PubMed=9305783; DOI=10.1016/s0304-4165(97)00023-8;
RA Merkle R.K., Zhang Y., Ruest P.J., Lal A., Liao Y.-F., Moremen K.W.;
RT "Cloning, expression, purification, and characterization of the murine
RT lysosomal acid alpha-mannosidase.";
RL Biochim. Biophys. Acta 1336:132-146(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, 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: Necessary for the catabolism of N-linked carbohydrates
CC released during glycoprotein turnover.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC09470.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC53369.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U29947; AAC53369.1; ALT_INIT; mRNA.
DR EMBL; AF044192; AAC78560.1; -; Genomic_DNA.
DR EMBL; AF044174; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044175; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044176; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044177; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044178; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044179; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044180; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044181; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044182; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044183; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044184; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044185; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044186; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044187; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044188; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044189; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044190; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AF044191; AAC78560.1; JOINED; Genomic_DNA.
DR EMBL; AK147928; BAE28235.1; -; mRNA.
DR EMBL; AK004817; BAB23588.1; -; mRNA.
DR EMBL; BC005430; AAH05430.1; -; mRNA.
DR EMBL; U87240; AAC09470.1; ALT_INIT; mRNA.
DR CCDS; CCDS22494.1; -.
DR PIR; T42385; T42385.
DR RefSeq; NP_034894.2; NM_010764.2.
DR AlphaFoldDB; O09159; -.
DR SMR; O09159; -.
DR BioGRID; 201305; 25.
DR IntAct; O09159; 1.
DR STRING; 10090.ENSMUSP00000034121; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR GlyConnect; 2491; 3 N-Linked glycans (3 sites).
DR GlyGen; O09159; 11 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; O09159; -.
DR PhosphoSitePlus; O09159; -.
DR CPTAC; non-CPTAC-3591; -.
DR EPD; O09159; -.
DR jPOST; O09159; -.
DR MaxQB; O09159; -.
DR PaxDb; O09159; -.
DR PeptideAtlas; O09159; -.
DR PRIDE; O09159; -.
DR ProteomicsDB; 287287; -.
DR DNASU; 17159; -.
DR Ensembl; ENSMUST00000034121; ENSMUSP00000034121; ENSMUSG00000005142.
DR GeneID; 17159; -.
DR KEGG; mmu:17159; -.
DR UCSC; uc009mpk.1; mouse.
DR CTD; 4125; -.
DR MGI; MGI:107286; Man2b1.
DR VEuPathDB; HostDB:ENSMUSG00000005142; -.
DR eggNOG; KOG1959; Eukaryota.
DR GeneTree; ENSGT01030000234638; -.
DR HOGENOM; CLU_004690_2_0_1; -.
DR InParanoid; O09159; -.
DR OMA; LEFIWRP; -.
DR OrthoDB; 201312at2759; -.
DR PhylomeDB; O09159; -.
DR TreeFam; TF313840; -.
DR BRENDA; 3.2.1.24; 3474.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8853383; Lysosomal oligosaccharide catabolism.
DR BioGRID-ORCS; 17159; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Man2b1; mouse.
DR PRO; PR:O09159; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O09159; protein.
DR Bgee; ENSMUSG00000005142; Expressed in stroma of bone marrow and 271 other tissues.
DR ExpressionAtlas; O09159; baseline and differential.
DR Genevisible; O09159; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0004559; F:alpha-mannosidase activity; IDA:MGI.
DR GO; GO:0005537; F:mannose binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0006013; P:mannose metabolic process; IDA:MGI.
DR GO; GO:0036211; P:protein modification process; ISO:MGI.
DR Gene3D; 1.20.1270.50; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Metal-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..49
FT /evidence="ECO:0000255"
FT CHAIN 50..1013
FT /note="Lysosomal alpha-mannosidase"
FT /id="PRO_0000012076"
FT ACT_SITE 196
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..358
FT /evidence="ECO:0000250"
FT DISULFID 268..273
FT /evidence="ECO:0000250"
FT DISULFID 412..472
FT /evidence="ECO:0000250"
FT DISULFID 493..501
FT /evidence="ECO:0000250"
FT CONFLICT 45..49
FT /note="PGARA -> LASG (in Ref. 1; AAC53369 and 2; AAC78560)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="V -> A (in Ref. 1; AAC53369, 2; AAC78560, 4;
FT AAH05430 and 5; AAC09470)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="Y -> F (in Ref. 1; AAC53369, 2; AAC78560, 4;
FT AAH05430 and 5; AAC09470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 114648 MW; A83B5397D9D38D31 CRC64;
MGTGPLTSGV RAGGGNTGWL WMSSCNLGSP VLPISFLFWL LLAAPGARAA GYKTCPPTKP
GMLNVHLLPH THDDVGWLKT VDQYYYGILS DVQHASVQYI LDSVVSSLLE KPTRRFIYVE
MAFFSRWWKQ QTSATQDAVR NLVRQGRLEF VNGGWVMNDE AATHYGAIVD QMTLGLRFLQ
DTFGSDGLPR VAWHIDPFGH SREQASLFAQ MGFDGFFLGR IDYQDKLNRK KKLRMEELWR
ASDSLEPPAA DLFTGVLPNN YNPPKYLCWD VLCTDPPVVD NPRSPEFNAK TLVNYFLKLA
SSQKGFYRTN HTVMTMGSDF HYENANMWFK NMDKLIRLVN AQQVNGSLVH VLYSTPTCYL
WELNKANLTW TVKEDDFFPY ADGPHMFWTG YFSSRPALKR YERLSYNFLQ VCNQLEALVG
PEANVGPYGS GDSAPLQEAM AVLQHHDAVS GTARQNVVND YARQLAAGWG PCEVLVSNAL
ARLSHYKQNF SFCRELNISI CPVSQTSERF QVTLYNPLGR KVDQMVRLPV YEGNFIVKDP
HDKNISSNVV MVPSYYSETY QWELLFPASV PALGFSTYSV AKMSDLNHQA HNLLSRPRKH
KSHHVLVIEN KYMRATFDSG TGLLMKIENL EQNLSLPVSQ GFFWYNASVG DEESSQASGA
YIFRPNVGKP IPVSRWAQIS LVKTALVQEV HQNFSAWCSQ VIRLYKGQRH LELEWTVGPI
PVRDDWGKEV ISRFDTPMKT KGQFFTDSNG REILKRRDDY RPTWTLNQTE PVAGNYYPVN
TRIYITDGQM QLTVLTDRSQ GGSSLQDGSL ELMVHRRLLV DDDRGVSEPL LETDTGDKVR
GRHLVLLSSV SDAAARHRLL AEQEVLAPQV VLSLGGSSPY HSRATPKTQF SGLRQELPPQ
VHLLTLARWG PKMLLLRLEH QFALKEDSDR NLSSPVTLNV QNLFQTFTIN YLQETTLAAN
QPLSRASRLK WMTNTGPTSY PEPSKLDPTS VTLKPMEIRT FLASVQWQEH RPA
