Lysosomal alpha-mannosidase precursor - Cavia porcellus (Guinea pig)

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Reviewed, UniProtKB/Swiss-Prot Q8VHC8 (MA2B1_CAVPO)

Last modified June 16, 2009. Version 39. History...

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

Names and origin

Protein names

Recommended 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

Gene names

Name:	MAN2B1
Synonyms:	MANB

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	1007 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	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 component	Lysosome
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	mannose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

47

Potential

Chain

960

Lysosomal alpha-mannosidase

PRO_0000012067

Sites

Active site

1

Nucleophile By similarity

Metal binding

1

Zinc By similarity

Metal binding

1

Zinc By similarity

Metal binding

1

Zinc By similarity

Metal binding

1

Zinc 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

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Natural variations

Natural variant

1

M → I Ref.1

Natural variant

1

R → W in AM. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q8VHC8-1 [UniParc].

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

1,007

113,184

        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

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: 11959458] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT AM TRP-227, VARIANT ILE-55.

Cross-references

Sequence databases
	AY036153 mRNA. Translation: AAL58982.1. AY036154 mRNA. Translation: AAL58983.1. AY036155 mRNA. Translation: AAL58984.1.
3D structure databases
HSSP	HSSP built from PDB template 1O7D based on UniProtKB Q29451.
SMR	Q8VHC8. Positions 49-338, 599-868, 882-1003.
ModBase	Search...
Protein family/group databases
CAZy	GH38. Glycoside Hydrolase Family 38.
Genome annotation databases
Ensembl	ENSCPOG00000002295. Cavia porcellus. [Contig view]
Phylogenomic databases
HOVERGEN	Q8VHC8.
Enzyme and pathway databases
BRENDA	3.2.1.24. 44.
Family and domain databases
InterPro	IPR011682. Glyco_hydro_38_C. IPR015341. Glyco_hydro_38_central. IPR000602. Glyco_hydro_38_core. [Graphical view]
Gene3D	G3DSA:3.20.110.10. Glyco_hydro_38_core. 1 hit.
Pfam	PF09261. Alpha-mann_mid. 1 hit. PF01074. Glyco_hydro_38. 1 hit. PF07748. Glyco_hydro_38C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MA2B1_CAVPO

Accession

Primary (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 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

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