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Q5RDJ3 (MA2B2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. 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:
Epididymis-specific alpha-mannosidase

EC=3.2.1.24
Alternative name(s):
Mannosidase alpha class 2B member 2
Gene names
Name:MAN2B2
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length1009 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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

Secreted Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmannose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

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 – 2323 Potential
Chain24 – 1009986Epididymis-specific alpha-mannosidase
PRO_0000012080

Sites

Active site1511Nucleophile By similarity
Metal binding361Zinc By similarity
Metal binding381Zinc By similarity
Metal binding1511Zinc By similarity
Metal binding4201Zinc By similarity

Amino acid modifications

Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation5161N-linked (GlcNAc...) Potential
Glycosylation6081N-linked (GlcNAc...) Potential
Glycosylation6701N-linked (GlcNAc...) Potential
Glycosylation6751N-linked (GlcNAc...) Potential
Glycosylation7481N-linked (GlcNAc...) Potential
Glycosylation8081N-linked (GlcNAc...) Potential
Glycosylation8121N-linked (GlcNAc...) Potential
Glycosylation8901N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5RDJ3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 0F25A14EEA5D30C5

FASTA1,009113,832
        10         20         30         40         50         60 
MGRLYWLPLL APLLLLRPPG VQSAGPIRAF VVPHSHMDVG WVYTVQESMQ AYAANVYTSV 

        70         80         90        100        110        120 
VEELARGQQR RFIAVEQEFF RLWWGGVASD QQKHQVHQLL EEGRLEFVIG GQVMHDEAVT 

       130        140        150        160        170        180 
HLDDQILQLT EGHGFLYETF GIRPQFSWHV DPFGASATTP TLFALAGFNA HLSSRIDYDL 

       190        200        210        220        230        240 
KAAMQEARGL QFVWRGSPSL SEQEEIFTHI MDQYSYCTPS HIPFSNRSGF YWNGVAIFPK 

       250        260        270        280        290        300 
PPPDGVYPNM SEPVTPANIN LYAEALVANV KQRAAWFRTP HVLWPWGCDK QFFNASVQFA 

       310        320        330        340        350        360 
NMNPLLDHIN SHAAKLGVSV QYATLGDYFR ALHTLNITWR VRDHHDFLPY STEPFQAWTG 

       370        380        390        400        410        420 
FYTSRSALKG LARRASALLY AGESMFTHYM WPAPCGHLDP TWALQQLQQL RWAVSEVQHH 

       430        440        450        460        470        480 
DAITGTESPK VRDMYVMHLA SGMLGVRKLM ASIILDKLQP QAPMAASSGA GPAGHFASVY 

       490        500        510        520        530        540 
NPLAWTVTTI VTLTVGFPGV HVTDEAGHPV PSQIQNSTET PSVYDLLILT TIPGLSYRHY 

       550        560        570        580        590        600 
SIRPTAGAQE GTQEPAATVA TTLQFGRRLR RRTSHVGRHL VPVANDCYTV LLDQDTNLMH 

       610        620        630        640        650        660 
SIWERQSNQT VRVTQEFLEY HVNGDVKQGP ISDNYLFTPG KAAVPAWEAV EMEIVAGQLV 

       670        680        690        700        710        720 
TEIRQYFYRN MTARNYTYAI RSRLTHVPQG HDGELLCHRI EQEYQAGPLE LNREAVLRTS 

       730        740        750        760        770        780 
TNLNSQQVIY SDNNGYQMQR RPYVSYVNNS IARNYYPMVQ SAFMEDGKSR LVLLSERAHG 

       790        800        810        820        830        840 
ISSQGNGQVE VMLHRRLWNN FDWDLGYNLT LNDTSIVHPV LWLLLGSWSL TTALRQRSAM 

       850        860        870        880        890        900 
ALQHRPVVLF GDLAGTAPKL PGPQQQEAVT LPPNLHLQIL SIPGWRYSSN HTEHAQNLRK 

       910        920        930        940        950        960 
GNRGEVQADL HRVLLRLHHL YEVGEDPVLS QPVTVNLEAV LQALGSVVAV EERSLTGTWD 

       970        980        990       1000 
VSMLHRWSWR TGSGRRRGDT TSPSRPPGGP IITVHPKEIR TFFIHFQQQ 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857915 mRNA. Translation: CAH90164.1.
RefSeqNP_001125051.1. NM_001131579.1.
UniGenePab.7285.

3D structure databases

ProteinModelPortalQ5RDJ3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100171932.
KEGGpon:100171932.

Organism-specific databases

CTD23324.

Phylogenomic databases

HOVERGENHBG052392.
KOK12312.

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 nameMA2B2_PONAB
AccessionPrimary (citable) accession number: Q5RDJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 57 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