ID   MANBA_BOVIN             Reviewed;         879 AA.
AC   Q29444;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-NOV-2023, entry version 132.
DE   RecName: Full=Beta-mannosidase;
DE            EC=3.2.1.25 {ECO:0000305|PubMed:8424779};
DE   AltName: Full=Lysosomal beta A mannosidase;
DE   AltName: Full=Mannanase;
DE            Short=Mannase;
DE   Flags: Precursor;
GN   Name=MANBA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-65; 220-228; 417-429;
RP   617-624; 680-716; 852-861 AND 864-879, DISEASE, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney, and Thyroid;
RX   PubMed=7876128; DOI=10.1074/jbc.270.8.3841;
RA   Chen H., Leipprandt J.R., Traviss C.E., Sopher B.L., Jones M.Z.,
RA   Cavanagh K.T., Friderici K.H.;
RT   "Molecular cloning and characterization of bovine beta-mannosidase.";
RL   J. Biol. Chem. 270:3841-3848(1995).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISEASE, GLYCOSYLATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=8424779; DOI=10.1042/bj2890343;
RA   Sopher B.L., Traviss C.E., Cavanagh K.T., Jones M.Z., Friderici K.H.;
RT   "Bovine kidney beta-mannosidase: purification and characterization.";
RL   Biochem. J. 289:343-347(1993).
CC   -!- FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose
CC       residue from the non-reducing end of all N-linked glycoprotein
CC       oligosaccharides. {ECO:0000305|PubMed:8424779}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC         in beta-D-mannosides.; EC=3.2.1.25;
CC         Evidence={ECO:0000305|PubMed:8424779};
CC   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC       {ECO:0000305|PubMed:8424779}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8K2I4}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q95327}.
CC   -!- TISSUE SPECIFICITY: Detected in kidney (at protein level)
CC       (PubMed:8424779). Highest expression is found in thyroid tissue. The
CC       amount of transcript is significantly higher in normal tissues than in
CC       tissues affected by the disease (PubMed:7876128).
CC       {ECO:0000269|PubMed:7876128, ECO:0000269|PubMed:8424779}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8424779}.
CC   -!- DISEASE: Note=Defects in MANBA cause beta-mannosidosis, a severe
CC       disorder that affects peripheral and central nervous system myelin
CC       resulting in tremor, nystagmus, ataxia and early death. The primary
CC       storage products associated with the enzyme deficiency are the
CC       trisaccharide Man-beta-1-4-GlcNAc-beta-1-4-GlcNAc and the disaccharide
CC       Man-beta-1-4-GlcNAc. {ECO:0000269|PubMed:7876128,
CC       ECO:0000269|PubMed:8424779}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; U17432; AAC48460.1; -; mRNA.
DR   PIR; A55881; A55881.
DR   RefSeq; NP_776812.1; NM_174387.2.
DR   AlphaFoldDB; Q29444; -.
DR   SMR; Q29444; -.
DR   STRING; 9913.ENSBTAP00000026334; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GlyCosmos; Q29444; 6 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000026334; -.
DR   GeneID; 281909; -.
DR   KEGG; bta:281909; -.
DR   CTD; 4126; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   InParanoid; Q29444; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004567; F:beta-mannosidase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR041625; Beta-mannosidase_Ig.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR041447; Mannosidase_ig.
DR   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Lysosome; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..879
FT                   /note="Beta-mannosidase"
FT                   /id="PRO_0000012164"
FT   ACT_SITE        457
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT   ACT_SITE        554
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT   BINDING         190..192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT   BINDING         456
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        803
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        167..176
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT   DISULFID        540..629
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT   DISULFID        732..761
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT   DISULFID        764..769
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2I4"
FT   VARIANT         65
FT                   /note="F -> R"
FT   VARIANT         709
FT                   /note="H -> D"
SQ   SEQUENCE   879 AA;  101176 MW;  2CA8351677E4ACFA CRC64;
     MLLRLLLLLA PCGAGFATKV VSISLRGNWK IHSGNGSLQL PATVPGCVHS ALFNKRIIKD
     PYYRFNNLDY RWIALDNWTY IKKFKLHSDM STWSKVNLVF EGIDTVAVVL LNSVPIGKTD
     NMFRRYSFDI THTVKAVNII EVRFQSPVVY ANQRSERHTA YWVPPNCPPP VQDGECHVNF
     IRKMQCSFGW DWGPSFPTQG IWKDVRIEAY NVCHLNYFMF TPIYDNYMKT WNLKIESSFD
     VVSSKLVSGE AIVAIPELNI QQTNNIELQH GERTVELFVK IDKAIIVETW WPHGHGNQTG
     YNMSVIFELD GGLRFEKSAK VYFRTVELVE EPIQNSPGLS FYFKINGLPI FLKGSNWIPA
     DSFQDRVTSA MLRLLLQSVV DANMNALRVW GGGVYEQDEF YELCDELGIM IWQDFMFACA
     LYPTDKDFMD SVREEVTHQV RRLKSHPSII TWSGNNENEA ALMMGWYDTK PGYLQTYIKD
     YVTLYVKNIR TIVLEGDQTR PFITSSPTNG AKTIAEGWLS PNPYDLNYGD VHFYDYVSDC
     WNWRTFPKAR FVSEYGYQSW PSFSTLEKVS SEEDWSYRSS FALHRQHLIN GNNEMLHQIE
     LHFKLPNSTD QLRRFKDTLY LTQVMQAQCV KTETEFYRRS RSEIVNGKGH TMGALYWQLN
     DIWQAPSWSS LEYGGKWKML HYFARHFFAP LLPVGFEDKD MLFIYGASHL HSDQQMMLTV
     RVHTWSSLEL VCSESTNPFV IKAGESVLLY TKPVPELLKG CPGCTRQSCV VSFYLSTDGE
     LLSPINYHFL SSLKNAKGLH KANITATISQ QGDTFVFDLK TSAVAPFVWL DVGSIPGRFS
     DNGFLMTEKT RTVFFYPWKP TSKSELEQSF HVTSLADTY
//