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Q8VHC8 (MA2B1_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Lysosomal alpha-mannosidase

Short name=Laman
EC=3.2.1.24
Alternative name(s):
Lysosomal acid alpha-mannosidase
Mannosidase alpha class 2B member 1
Mannosidase alpha-B
Gene names
Name:MAN2B1
Synonyms:MANB
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length1007 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Lysosome.

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. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmannose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4747 Potential
Chain48 – 1007960Lysosomal alpha-mannosidase
PRO_0000012067

Sites

Active site1941Nucleophile By similarity
Metal binding701Zinc By similarity
Metal binding721Zinc By similarity
Metal binding1941Zinc By similarity
Metal binding4441Zinc By similarity

Amino acid modifications

Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation3651N-linked (GlcNAc...) Potential
Glycosylation4951N-linked (GlcNAc...) Potential
Glycosylation5401N-linked (GlcNAc...) Potential
Glycosylation6391N-linked (GlcNAc...) Potential
Glycosylation6861N-linked (GlcNAc...) Potential
Glycosylation7601N-linked (GlcNAc...) Potential
Glycosylation9271N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 356 By similarity
Disulfide bond266 ↔ 271 By similarity
Disulfide bond410 ↔ 470 By similarity
Disulfide bond491 ↔ 499 By similarity

Natural variations

Natural variant551M → I. Ref.1
Natural variant2271R → W in AM. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VHC8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: C128EB9948A44D41

FASTA1,007113,184
        10         20         30         40         50         60 
MGASVLPLGL GAGDCQSSSG RRMSACLPRT ALSFLLSLLL ATPGARAAGY ETCPMVQPGM 

        70         80         90        100        110        120 
LNVHLVAHTH DDVGWLKTVD QYYWGIHNDL QQAGVQYILD SVISALLAEP TRRFVYVEMA 

       130        140        150        160        170        180 
FFSRWWHQQT NETQEVVRRL VRQGRLEFAN GGWVMNDEAA THYGAIVDQM TLGLRFLEDT 

       190        200        210        220        230        240 
FGSDGRPRVA WHIDPFGHSR EQASLFAQMG FDGVFFGRID YQDKLVRKKR REMELVWRAS 

       250        260        270        280        290        300 
ASLKAPAADL FTGVLPNNYG PPEGLCWDVL CADPPVVDDP RSPEYNAKKL VSYFLQLATA 

       310        320        330        340        350        360 
QGRYYRTNHT VMTMGSDFQY ENANTWFKNL DKLIQLVNMQ QANGSRVHVL YSTPACYLWE 

       370        380        390        400        410        420 
LNKANLTWPV KEDDFFPYAD GPHMFWTGYF SSRPALKRYE RLSYNFLQVC NQLEAQVGPA 

       430        440        450        460        470        480 
ANVGPYGHGD SSPLNQAMAV LQHHDAVSGT SKQHVADDYA RQLAAGWGPC EVLLSNALAK 

       490        500        510        520        530        540 
LSGSKETFLF CRDLNISICP FSQTSERFQV LVYNPLGRKV DRMVRLPVRK GLFLIKDPGN 

       550        560        570        580        590        600 
NTVPSTVVEL TSSGNPELLF PALVPALGFS VYSVTRVSDQ NPQTRSQHSR PQKYSSPVLS 

       610        620        630        640        650        660 
IKNEYLRASF HPDTGLLSMI EVLDRKLTLP VNQAFFWYNA SVGDKRSSQA SGAYIFRPSQ 

       670        680        690        700        710        720 
QWPFPVSHLA RTRLVKTALV QEVHQNFTAW CSQVVRLYSG QRHLELEWTV GPIPVGDKWG 

       730        740        750        760        770        780 
KEIISRFDTP LETGGVFFTD SNGREVLERR RDYRPSWKLN QTEPVAGNYY PVNSRIYITD 

       790        800        810        820        830        840 
GKMQLTVLTD RSQGGSSMSD GSLELMVHRR LLKDDGRGVG EALQEPGSGG WVRGRHLLLL 

       850        860        870        880        890        900 
DTAREAAAEH RLLAEKELLA PQLVLAPGQG PSYHHDHHEA VPRKQFSGLR RQLPPSVRLL 

       910        920        930        940        950        960 
TLARWGPDTL LLRLEHQFAL GEDSSRNLSL PVTLDLQDLF STFTITRLQE TTLAANQLRA 

       970        980        990       1000 
SASRLKWTTE IDPISRPAVP RLDPSSITLQ PMEIRTFVAS VQWEENS 

« Hide

References

[1]"Alpha-mannosidosis in the guinea pig: cloning of the lysosomal alpha-mannosidase cDNA and identification of a missense mutation causing alpha-mannosidosis."
Berg T., Hopwood J.J.
Biochim. Biophys. Acta 1586:169-176(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT AM TRP-227, VARIANT ILE-55.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY036153 mRNA. Translation: AAL58982.1.
AY036154 mRNA. Translation: AAL58983.1.
AY036155 mRNA. Translation: AAL58984.1.
RefSeqNP_001244175.1. NM_001257246.1.

3D structure databases

ProteinModelPortalQ8VHC8.
SMRQ8VHC8. Positions 49-338, 346-419, 429-577, 599-868, 882-1003.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000024185; ENSCPOP00000017509; ENSCPOG00000002295.
GeneID100718205.

Organism-specific databases

CTD4125.

Phylogenomic databases

eggNOGCOG0383.
GeneTreeENSGT00510000046304.
HOGENOMHOG000007676.
HOVERGENHBG052391.
OrthoDBEOG786H2P.

Family and domain databases

Gene3D1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013780. Glyco_hydro_13_b.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMA2B1_CAVPO
AccessionPrimary (citable) accession number: Q8VHC8
Secondary accession number(s): Q8VHC6, Q8VHC7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 67 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries