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Q95327 (MANBA_CAPHI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-mannosidase

EC=3.2.1.25
Alternative name(s):
Lysosomal beta A mannosidase
Mannanase
Short name=Mannase
Gene names
Name:MANBA
OrganismCapra hircus (Goat)
Taxonomic identifier9925 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides.

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.

Pathway

Glycan metabolism; N-glycan degradation.

Subcellular location

Lysosome.

Tissue specificity

Found in spleen and to a lesser extent in liver. Not detected in kidney or brain.

Involvement in disease

Defects in MANBA cause beta-mannosidosis, a severe disorder that affects peripheral and central nervous system myelin resulting in tremor, nystagmus, ataxia and early death. The primary storage products associated with the enzyme deficiency are the trisaccharide Man-beta-1-4-GlcNAc-beta-1-4-GlcNAc and the disaccharide Man-beta-1-4-GlcNAc.

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological_processmannan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 879862Beta-mannosidase
PRO_0000012165

Sites

Active site4571Proton donor By similarity

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation8031N-linked (GlcNAc...) Potential

Natural variations

Natural variant561R → Q.
Natural variant3401T → S.

Sequences

Sequence LengthMass (Da)Tools
Q95327 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 2B96F03596B480C0

FASTA879101,386
        10         20         30         40         50         60 
MLLRLLLLLA PCGAGFATEV VSISLRGNWK IHNGNGSLQL PAAVPGCVHS ALFNKRIIKD 

        70         80         90        100        110        120 
PYYRFNNLDY RWIALDNWTY IKKFKLHSDM SEWNKVNLVF EGIDTVAVVL LNSVPIGKTD 

       130        140        150        160        170        180 
NMFRRYSFDI THMVKAVNII EVRFQSPVIY ANQRSERHTA YWVPPNCPPP VQDGECHVNF 

       190        200        210        220        230        240 
IRKMQCSFGW DWGPSFPTQG IWKDVRIEAY NICHLNYFMF TPIYDNYMET WNLKIESSFD 

       250        260        270        280        290        300 
VVSSKLVSGE AIVAIPELNI QQRNNIELRH GERTVKLFVK IDKAVIVETW WPHGHGNQTG 

       310        320        330        340        350        360 
YDMTVTFELD GGLRFEKSAK VYFRTVELVE EPIQNSPGLT FYFKINGLPI FLKGSNWIPA 

       370        380        390        400        410        420 
DSFQDRVTSD MLRLLLQSVV DANMNALRVW GGGIYEQDEF YELCDELGIM IWQDFMFACA 

       430        440        450        460        470        480 
LYPTDEDFMD SVREEVTHQV RRLKSHPSII TWSGNNENEA ALMMGWYDTK PGYLHTYIKD 

       490        500        510        520        530        540 
YVTLYVKNIR TIVLEGDQTR PFIISSPTNG AKTTAEGWLS PNPYDLNYGD VHFYDYMSDC 

       550        560        570        580        590        600 
WNWRTFPKAR FVSEYGYQSW PSFSTLEKVS SEEDWSYESS FALHRQHLIN GNSEMLQQIE 

       610        620        630        640        650        660 
LHFKLPNSAD QLRRFKDTLY LTQVMQAQCV KTETEFYRRS RNEIVDGKGH TMGALYWQLN 

       670        680        690        700        710        720 
DIWQAPSWSS LEYGGKWKML HYFARRFFAP LLPVGFEDKD VLFIYGVSDL PSDHQMMLTV 

       730        740        750        760        770        780 
RVHTWSSLEL VCSELTNPFV MKAGESVVLY SKPVPELLKG CPGCTRQSCV VSFYLSTDGE 

       790        800        810        820        830        840 
LLSPINYHFL SSLKNAKGLH KANITATISQ QGNTFVFDLK TSAVAPFVWL DVGSIPGRFS 

       850        860        870 
DNGFLMTEKT RTVFFYPWKP TSKSELEQSF HVTSLADTY 

« Hide

References

[1]"Caprine beta-mannosidase: sequencing and characterization of the cDNA and identification of the molecular defect of caprine beta-mannosidosis."
Leipprandt J.R., Kraemer S.A., Haithcock B.E., Chen H., Dyme J.L., Cavanagh K.T., Friderici K.H., Jones M.Z.
Genomics 37:51-56(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46067 mRNA. Translation: AAC48665.1.
RefSeqNP_001272620.1. NM_001285691.1.
UniGeneChi.8280.

3D structure databases

ProteinModelPortalQ95327.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Proteomic databases

PRIDEQ95327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100750234.
KEGGchx:100750234.

Organism-specific databases

CTD4126.

Phylogenomic databases

HOVERGENHBG052404.
KOK01192.

Enzyme and pathway databases

UniPathwayUPA00280.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProIPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR028369. Mannanase.
[Graphical view]
PANTHERPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamPF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANBA_CAPHI
AccessionPrimary (citable) accession number: Q95327
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries