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Q60HE9 (MA2B1_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 45. 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
ORF Names:QmoA-10471
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length1012 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
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 – 5050 By similarity
Chain51 – 1012962Lysosomal alpha-mannosidase
PRO_0000012075

Sites

Active site1971Nucleophile By similarity
Metal binding731Zinc By similarity
Metal binding751Zinc By similarity
Metal binding1971Zinc By similarity
Metal binding4471Zinc By similarity

Amino acid modifications

Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation6461N-linked (GlcNAc...) Potential
Glycosylation6521N-linked (GlcNAc...) Potential
Glycosylation6931N-linked (GlcNAc...) Potential
Glycosylation7671N-linked (GlcNAc...) Potential
Glycosylation8331N-linked (GlcNAc...) Potential
Glycosylation9311N-linked (GlcNAc...) Potential
Glycosylation9901N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 359 By similarity
Disulfide bond269 ↔ 274 By similarity
Disulfide bond413 ↔ 473 By similarity
Disulfide bond494 ↔ 502 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60HE9 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 87FA3277FFBF1326

FASTA1,012113,922
        10         20         30         40         50         60 
MGAYAPAAGV SARGCLDAAG PWTISRALRP PLPPLCFFLL LLLAAPCARA GGYETCPTVQ 

        70         80         90        100        110        120 
PNILNVHLVP HTHDDVGWLK TVDQYFYGIK NDIQHAGVQY ILDSVISALL ADPTRRFIYV 

       130        140        150        160        170        180 
EIAFFSRWWH QQTNAMREVV RDLVRQGRLE FANGGWVMND EAATHYGAIV DQMTLGLRFL 

       190        200        210        220        230        240 
EDTFGSDGRP RVAWHIDPFG HSREQASLFA QMGFDGFFFG RLDYQDKRVR MQKLEMEQVW 

       250        260        270        280        290        300 
RASASLKPPT ADLFTGVLPN GYNPPMNLCW DVLCVDQPVV EDPRSPEYNA KELVDYFLNV 

       310        320        330        340        350        360 
ATAQGRHYRT NHIVMTMGSD FQYENANMWF KNLDKLIRLV NAQQAKGSSV HVLYSTPACY 

       370        380        390        400        410        420 
LWELNKANLT WSVKHDDFFP YADGPHQFWT GYFSSRPALK RYERLSYNFL QVCNQLEALV 

       430        440        450        460        470        480 
GLAANVGPYG SGDSAPLNKA MAVLQHHDAV SGTSRQHVAD DYARQLAAGW VSCEVLLSNA 

       490        500        510        520        530        540 
LARLRGFKDH LTFCRQLNIS ICPLSQTAAR FQVIVYNPLG RKVNWMVRLP VSEGVFVVKD 

       550        560        570        580        590        600 
PNGRTVPSDV VIYPSSDSQA HPPELLFSAS LPALGFSTYS VAQVPRWKPQ ARAPQPIPRR 

       610        620        630        640        650        660 
SWSPALTIEN EHIRATFDPD TGLLMEIMNM NQRLLLPVRQ TFFWYNASIG DNESDQASGA 

       670        680        690        700        710        720 
YIFRPNQQKP LPVSRWAQIR LVKTPLVQEV HQNFSAWCSQ VVRLYPGRRH LELEWSVGPI 

       730        740        750        760        770        780 
PVGDTWGKEV ISRFDTPLET KGRFYTDSNG REILERRRDY RPTWKLNQTE PVAGNYYPVN 

       790        800        810        820        830        840 
TRIYITDGKM QLTVLTDRSQ GGSSLRDGSL ELMVHRRLLK DDERGVSEPL MENGSGAWVR 

       850        860        870        880        890        900 
GRHLVLLDTA QAAAAGHRLL AEQEVLAPQV VLAPGGGAAY NLGAPPRTQF SGLRRELPPS 

       910        920        930        940        950        960 
VHLLTLASWG PEMLLLRLEH QFAVGEDSGR NLSAPVTLNL RDLFSTFTIT RLQETTLVAN 

       970        980        990       1000       1010 
QLREAASRLK WTTNTGPTPH QTPYQLDPAN ITLEPMEIRT FLASVQWKEV DG 

« Hide

References

[1]"Isolation and characterization of cDNA for macaque neurological disease genes."
Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Medulla oblongata.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB125178 mRNA. Translation: BAD51966.1.

3D structure databases

ProteinModelPortalQ60HE9.
SMRQ60HE9. Positions 52-342, 350-421, 432-585, 606-875, 886-1007.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Proteomic databases

PRIDEQ60HE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052391.

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.
[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.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMA2B1_MACFA
AccessionPrimary (citable) accession number: Q60HE9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: November 23, 2004
Last modified: March 19, 2014
This is version 45 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