MANBA_CAPHI
ID MANBA_CAPHI Reviewed; 879 AA.
AC Q95327;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Beta-mannosidase;
DE EC=3.2.1.25 {ECO:0000305|PubMed:1556126, ECO:0000305|PubMed:7228876};
DE AltName: Full=Lysosomal beta A mannosidase;
DE AltName: Full=Mannanase;
DE Short=Mannase;
DE Flags: Precursor;
GN Name=MANBA;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE.
RC TISSUE=Kidney;
RX PubMed=8921369; DOI=10.1006/geno.1996.0519;
RA Leipprandt J.R., Kraemer S.A., Haithcock B.E., Chen H., Dyme J.L.,
RA Cavanagh K.T., Friderici K.H., Jones M.Z.;
RT "Caprine beta-mannosidase: sequencing and characterization of the cDNA and
RT identification of the molecular defect of caprine beta-mannosidosis.";
RL Genomics 37:51-56(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISEASE, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7228876; DOI=10.1016/s0021-9258(19)69384-1;
RA Jones M.Z., Dawson G.;
RT "Caprine beta-mannosidosis. Inherited deficiency of beta-D-mannosidase.";
RL J. Biol. Chem. 256:5185-5188(1981).
RN [3]
RP CATALYTIC ACTIVITY, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=1556126; DOI=10.1016/s0021-9258(18)42678-6;
RA Sopher B.L., Traviss C.E., Cavanagh K.T., Jones M.Z., Friderici K.H.;
RT "Purification and characterization of goat lysosomal beta-mannosidase using
RT monoclonal and polyclonal antibodies.";
RL J. Biol. Chem. 267:6178-6182(1992).
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:0000269|PubMed:7228876}.
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:1556126, ECO:0000305|PubMed:7228876};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:7228876};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000269|PubMed:7228876}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8K2I4}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305|PubMed:7228876}.
CC -!- TISSUE SPECIFICITY: Detected in kidney (at protein level)
CC (PubMed:1556126). Found in spleen and to a lesser extent in liver. Not
CC detected in kidney or brain. {ECO:0000269|PubMed:1556126}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:1556126}.
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:7228876,
CC ECO:0000269|PubMed:8921369}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; U46067; AAC48665.1; -; mRNA.
DR RefSeq; NP_001272620.1; NM_001285691.1.
DR AlphaFoldDB; Q95327; -.
DR SMR; Q95327; -.
DR STRING; 9925.ENSCHIP00000023174; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GeneID; 100750234; -.
DR KEGG; chx:100750234; -.
DR CTD; 4126; -.
DR OrthoDB; 517710at2759; -.
DR BRENDA; 3.2.1.25; 1166.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
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; -; 3.
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 Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..879
FT /note="Beta-mannosidase"
FT /id="PRO_0000012165"
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 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 56
FT /note="R -> Q"
FT VARIANT 340
FT /note="T -> S"
SQ SEQUENCE 879 AA; 101386 MW; 2B96F03596B480C0 CRC64;
MLLRLLLLLA PCGAGFATEV VSISLRGNWK IHNGNGSLQL PAAVPGCVHS ALFNKRIIKD
PYYRFNNLDY RWIALDNWTY IKKFKLHSDM SEWNKVNLVF EGIDTVAVVL LNSVPIGKTD
NMFRRYSFDI THMVKAVNII EVRFQSPVIY ANQRSERHTA YWVPPNCPPP VQDGECHVNF
IRKMQCSFGW DWGPSFPTQG IWKDVRIEAY NICHLNYFMF TPIYDNYMET WNLKIESSFD
VVSSKLVSGE AIVAIPELNI QQRNNIELRH GERTVKLFVK IDKAVIVETW WPHGHGNQTG
YDMTVTFELD GGLRFEKSAK VYFRTVELVE EPIQNSPGLT FYFKINGLPI FLKGSNWIPA
DSFQDRVTSD MLRLLLQSVV DANMNALRVW GGGIYEQDEF YELCDELGIM IWQDFMFACA
LYPTDEDFMD SVREEVTHQV RRLKSHPSII TWSGNNENEA ALMMGWYDTK PGYLHTYIKD
YVTLYVKNIR TIVLEGDQTR PFIISSPTNG AKTTAEGWLS PNPYDLNYGD VHFYDYMSDC
WNWRTFPKAR FVSEYGYQSW PSFSTLEKVS SEEDWSYESS FALHRQHLIN GNSEMLQQIE
LHFKLPNSAD QLRRFKDTLY LTQVMQAQCV KTETEFYRRS RNEIVDGKGH TMGALYWQLN
DIWQAPSWSS LEYGGKWKML HYFARRFFAP LLPVGFEDKD VLFIYGVSDL PSDHQMMLTV
RVHTWSSLEL VCSELTNPFV MKAGESVVLY SKPVPELLKG CPGCTRQSCV VSFYLSTDGE
LLSPINYHFL SSLKNAKGLH KANITATISQ QGNTFVFDLK TSAVAPFVWL DVGSIPGRFS
DNGFLMTEKT RTVFFYPWKP TSKSELEQSF HVTSLADTY
