MANBA_BOVIN
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 03-AUG-2022, entry version 129.
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 PaxDb; Q29444; -.
DR GeneID; 281909; -.
DR KEGG; bta:281909; -.
DR CTD; 4126; -.
DR eggNOG; KOG2230; Eukaryota.
DR InParanoid; Q29444; -.
DR OrthoDB; 517710at2759; -.
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; 2.60.40.10; -; 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 Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF49303; SSF49303; 3.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 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
