Beta-mannosidase precursor - Bos taurus (Bovine)

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Q29444 (MANBA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-mannosidase
EC=3.2.1.25

Alternative name(s):
Lysosomal beta A mannosidase
Mannanase
Short name=Mannase

Gene names

Name:

MANBA

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	879 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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	Highest expression is found in thyroid tissue. The amount of transcript is significantly higher in normal tissues than in tissues affected by the disease.
Post-translational modification	The N-terminus is blocked.
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 component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-mannosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

17

Potential

Chain

862

Beta-mannosidase

PRO_0000012164

Sites

Active site

1

Proton donor By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

1

F → R.

Natural variant

1

H → D.

Sequences

Sequence

Length

Mass (Da)

Tools

Q29444 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2CA8351677E4ACFA
Show »

879

101,176

        10         20         30         40         50         60 
MLLRLLLLLA PCGAGFATKV VSISLRGNWK IHSGNGSLQL PATVPGCVHS ALFNKRIIKD 

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

       130        140        150        160        170        180 
NMFRRYSFDI THTVKAVNII EVRFQSPVVY ANQRSERHTA YWVPPNCPPP VQDGECHVNF 

       190        200        210        220        230        240 
IRKMQCSFGW DWGPSFPTQG IWKDVRIEAY NVCHLNYFMF TPIYDNYMKT WNLKIESSFD 

       250        260        270        280        290        300 
VVSSKLVSGE AIVAIPELNI QQTNNIELQH GERTVELFVK IDKAIIVETW WPHGHGNQTG 

       310        320        330        340        350        360 
YNMSVIFELD GGLRFEKSAK VYFRTVELVE EPIQNSPGLS FYFKINGLPI FLKGSNWIPA 

       370        380        390        400        410        420 
DSFQDRVTSA MLRLLLQSVV DANMNALRVW GGGVYEQDEF YELCDELGIM IWQDFMFACA 

       430        440        450        460        470        480 
LYPTDKDFMD SVREEVTHQV RRLKSHPSII TWSGNNENEA ALMMGWYDTK PGYLQTYIKD 

       490        500        510        520        530        540 
YVTLYVKNIR TIVLEGDQTR PFITSSPTNG AKTIAEGWLS PNPYDLNYGD VHFYDYVSDC 

       550        560        570        580        590        600 
WNWRTFPKAR FVSEYGYQSW PSFSTLEKVS SEEDWSYRSS FALHRQHLIN GNNEMLHQIE 

       610        620        630        640        650        660 
LHFKLPNSTD QLRRFKDTLY LTQVMQAQCV KTETEFYRRS RSEIVNGKGH TMGALYWQLN 

       670        680        690        700        710        720 
DIWQAPSWSS LEYGGKWKML HYFARHFFAP LLPVGFEDKD MLFIYGASHL HSDQQMMLTV 

       730        740        750        760        770        780 
RVHTWSSLEL VCSESTNPFV IKAGESVLLY TKPVPELLKG CPGCTRQSCV VSFYLSTDGE 

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

       850        860        870 
DNGFLMTEKT RTVFFYPWKP TSKSELEQSF HVTSLADTY

References

[1]

"Molecular cloning and characterization of bovine beta-mannosidase."
Chen H., Leipprandt J.R., Traviss C.E., Sopher B.L., Jones M.Z., Cavanagh K.T., Friderici K.H.
J. Biol. Chem. 270:3841-3848(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-65; 220-228; 417-429; 617-624; 680-716; 852-861 AND 864-879.
Tissue: Kidney and Thyroid.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U17432 mRNA. Translation: AAC48460.1.
IPI	IPI00693341.
PIR	A55881.
RefSeq	NP_776812.1. NM_174387.2.
UniGene	Bt.111461.
3D structure databases
ProteinModelPortal	Q29444.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000026334.
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
Proteomic databases
PRIDE	Q29444.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	281909.
KEGG	bta:281909.
Organism-specific databases
CTD	4126.
Phylogenomic databases
eggNOG	COG3250.
HOGENOM	HOG000186862.
HOVERGEN	HBG052404.
InParanoid	Q29444.
KO	K01192.
OrthoDB	EOG40VVP2.
Enzyme and pathway databases
UniPathway	UPA00280.
Family and domain databases
Gene3D	2.60.40.320. 1 hit. 3.20.20.80. 2 hits.
InterPro	IPR008979. Galactose-bd-like. IPR013812. Glyco_hydro_2/20_Ig-like. IPR006104. Glyco_hydro_2_N. IPR006103. Glyco_hydro_2_TIM. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF02836. Glyco_hydro_2_C. 1 hit. PF02837. Glyco_hydro_2_N. 1 hit. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
NextBio	20805803.

Entry information

Entry name

MANBA_BOVIN

Accession

Primary (citable) accession number: Q29444

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents