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Reviewed, UniProtKB/Swiss-Prot Q29451 (MA2B1_BOVIN)

Last modified September 1, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Lysosomal alpha-mannosidase
      Short name=Laman
    EC=3.2.1.24
Alternative name(s):
    Lysosomal acid alpha-mannosidase
    Mannosidase alpha class 2B member 1
      Short name=Mannosidase, alpha B
Cleaved into the following 5 chains:
    1- Recommended name:
            Lysosomal alpha-mannosidase A peptide
    2- Recommended name:
            Lysosomal alpha-mannosidase B peptide
    3- Recommended name:
            Lysosomal alpha-mannosidase C peptide
    4- Recommended name:
            Lysosomal alpha-mannosidase D peptide
    5- Recommended name:
            Lysosomal alpha-mannosidase E peptide
Gene names
Name: MAN2B1
Synonyms: MANB
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length999 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Homodimer.

Subcellular location

Lysosome.

Post-translational modification

Processed into 5 peptides of 35/38 kDa (A), 11/13 kDa (B) and 22 kDa (C), 38 kDa (D) and 13/15 kDa (E). The A, B and C peptides are disulfide-linked into a 67 kDa complex.

Heavily glycosylated. Some sugar chains are of the high-mannose type.

Involvement in disease

Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

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Ontologies

Keywords
   Cellular componentLysosome
   DiseaseDisease mutation
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-mannosidase activity

Inferred from electronic annotation. Source: EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5050
Chain51 – 999949Lysosomal alpha-mannosidase
PRO_0000012060
Chain51 – 347297Lysosomal alpha-mannosidase A peptide
PRO_0000012061
Chain348 – 43184Lysosomal alpha-mannosidase B peptide
PRO_0000012062
Chain432 – 590159Lysosomal alpha-mannosidase C peptide
PRO_0000012063
Propeptide591 – 62131 Potential
PRO_0000012064
Chain622 – 871250Lysosomal alpha-mannosidase D peptide
PRO_0000012065
Chain872 – 999128Lysosomal alpha-mannosidase E peptide
PRO_0000012066

Sites

Active site1971Nucleophile
Metal binding731Zinc
Metal binding751Zinc
Metal binding1971Zinc
Metal binding4481Zinc

Amino acid modifications

Glycosylation1341N-linked (GlcNAc...)
Glycosylation3691N-linked (GlcNAc...)
Glycosylation4991N-linked (GlcNAc...)
Glycosylation6341N-linked (GlcNAc...)
Glycosylation6401N-linked (GlcNAc...)
Glycosylation6811N-linked (GlcNAc...)
Glycosylation7551N-linked (GlcNAc...)
Glycosylation9191N-linked (GlcNAc...)
Disulfide bond56 ↔ 360
Disulfide bond269 ↔ 274
Disulfide bond414 ↔ 474
Disulfide bond495 ↔ 503

Natural variations

Natural variant2211R → H in AM; Galloway cattle. Ref.1
Natural variant3211F → L in AM; Angus cattle. Ref.1

Experimental info

Sequence conflict512 – 55039Missing in AAC48763. Ref.1

Secondary structure

1 ........................................................................................................................................................ 999
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q29451-1 [UniParc].

Last modified January 16, 2004. Version 3.
Checksum: 4A8108A69407A2D4

FASTA999113,018
        10         20         30         40         50         60 
MVGDARPSGV RAGGCRGAVG SRTSSRALRP PLPPLSSLFV LFLAAPCAWA AGYKTCPKVK 

        70         80         90        100        110        120 
PDMLNVHLVP HTHDDVGWLK TVDQYFYGIY NNIQPAGVQY ILDSVISSLL ANPTRRFIYV 

       130        140        150        160        170        180 
EIAFFSRWWR QQTNATQKIV RELVRQGRLE FANGGWVMND EATTHYGAII DQMTLRLRFL 

       190        200        210        220        230        240 
EETFGSDGRP RVAWHIDPFG HSREQASLFA QMGFDGFFFG RLDYQDKKVR KKTLQMEQVW 

       250        260        270        280        290        300 
RASTSLKPPT ADLFTSVLPN MYNPPEGLCW DMLCADKPVV EDTRSPEYNA KELVRYFLKL 

       310        320        330        340        350        360 
ATDQGKLYRT KHTVMTMGSD FQYENANTWF KNLDKLIQLV NAQQRANGIR VNVLYSTPAC 

       370        380        390        400        410        420 
YLWELNKANL SWSVKKDDFF PYADGPYMFW TGYFSSRPAL KRYERLSYNF LQVCNQLEAL 

       430        440        450        460        470        480 
AGPAANVGPY GSGDSAPLNE AMAVLQHHDA VSGTSRQHVA NDYARQLSEG WRPCEVLMSN 

       490        500        510        520        530        540 
ALAHLSGLKE DFAFCRKLNI SICPLTQTAE RFQVIVYNPL GRKVDWMVRL PVSKHVYLVK 

       550        560        570        580        590        600 
DPGGKIVPSD VVTIPSSDSQ ELLFSALVPA VGFSIYSVSQ MPNQRPQKSW SRDLVIQNEY 

       610        620        630        640        650        660 
LRARFDPNTG LLMELENLEQ NLLLPVRQAF YWYNASTGNN LSSQASGAYI FRPNQNKPLF 

       670        680        690        700        710        720 
VSHWAQTHLV KASLVQEVHQ NFSAWCSQVV RLYPRQRHLE LEWTVGPIPV GDGWGKEVIS 

       730        740        750        760        770        780 
RFDTALATRG LFYTDSNGRE ILERRRNYRP TWKLNQTEPV AGNYYPVNSR IYITDGNMQL 

       790        800        810        820        830        840 
TVLTDRSQGG SSLRDGSLEL MVHRRLLKDD ARGVGEPLNK EGSGLWVRGR HLVLLDKKET 

       850        860        870        880        890        900 
AAARHRLQAE MEVLAPQVVL AQGGGARYRL EKAPRTQFSG LRRELPPSVR LLTLARWGPE 

       910        920        930        940        950        960 
TLLLRLEHQF AVGEDSGRNL SSPVTLDLTN LFSAFTITNL RETTLAANQL LAYASRLQWT 

       970        980        990 
TDTGPTPHPS PSRPVSATIT LQPMEIRTFL ASVQWEEDG

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References

[1]"Purification of bovine lysosomal alpha-mannosidase, characterization of its gene and determination of two mutations that cause alpha-mannosidosis."
Tollersrud O.-K., Berg T., Healy P., Evjen G., Ramachandran U., Nilssen O.
Eur. J. Biochem. 246:410-419(1997) [PubMed: 9208932] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS AM HIS-221 AND LEU-321.
Tissue: Kidney.
[2]Berg T.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 358.
[3]"The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation."
Heikinheimo P., Helland R., Leiros H.-K.S., Leiros I., Karlsen S., Evjen G., Ravelli R., Schoehn G., Ruigrok R., Tollersrud O.-K., McSweeney S., Hough E.
J. Mol. Biol. 327:631-644(2003) [PubMed: 12634058] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 52-999.

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Cross-references

Sequence databases

L31373 mRNA. Translation: AAB67726.2.
U97694 expand/collapse EMBL AC list , U97686, U97687, U97688, U97689, U97690, U97691, U97692, U97693 Genomic DNA. Translation: AAC48763.1.
IPIIPI00705699.
RefSeqNP_776986.2.
UniGeneBt.4622

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1O7DX-ray2.70A51-348[»]
B349-432[»]
C433-591[»]
D592-873[»]
E874-999[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ29451.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Genome annotation databases

EnsemblENSBTAT00000008193; ENSBTAP00000008193; ENSBTAG00000006241; Bos taurus. [Genome view]
GeneID282272.
KEGGbta:282272.

Organism-specific databases

CTD282272.

Phylogenomic databases

HOVERGENQ29451.

Enzyme and pathway databases

BRENDA3.2.1.24. 251.

Family and domain databases

InterProIPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_central.
IPR000602. Glyco_hydro_38_core.
[Graphical view]
Gene3DG3DSA:3.20.110.10. Glyco_hydro_38_core. 1 hit.
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMA2B1_BOVIN
AccessionPrimary (citable) accession number: Q29451
Secondary accession number(s): O02848, O19138
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 16, 2004
Last modified: September 1, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents