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Q28949 (MA2B2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length995 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can digest both p-nitro-phenyl-alpha-D-mannoside and high mannose oligosaccharide (Man(8)-GlcNAc2). May be involved in sperm maturation. Has a possible role in specific sperm-egg interaction since sperm surface mannosidase acts like a receptor for mannose-containing oligosaccharides located on the zona pellucida.

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. Note: Found at the sperm surface as a 27 kDa fragment.

Tissue specificity

Specific to the caput and corpus of the epididymis.

Post-translational modification

Processed into a 27 kDa fragment localized on the equatorial segment and the apical rim of the head of mature sperm.

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5.

Sequence caution

The sequence BAA05877.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
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 – 2121
Chain22 – 995974Epididymis-specific alpha-mannosidase
PRO_0000012079

Sites

Active site1511Nucleophile By similarity
Metal binding361Zinc By similarity
Metal binding381Zinc By similarity
Metal binding1511Zinc By similarity
Metal binding4111Zinc By similarity

Amino acid modifications

Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation5931N-linked (GlcNAc...) Potential
Glycosylation6251N-linked (GlcNAc...) Potential
Glycosylation6571N-linked (GlcNAc...) Potential
Glycosylation7331N-linked (GlcNAc...) Potential
Glycosylation7931N-linked (GlcNAc...) Potential
Glycosylation8751N-linked (GlcNAc...) Potential
Glycosylation9771N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict9451D → A AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q28949 [UniParc].

Last modified November 16, 2001. Version 2.
Checksum: 79D21B8CE5AE6FC2

FASTA995114,230
        10         20         30         40         50         60 
MGPHSWLPLF MQLALLGPQW ALHFYKVKVF VVPHSHMDVG WLHTVQESMQ VYVPDVYNSV 

        70         80         90        100        110        120 
VEALTRGKRR RFIAVEQEYF RLWWDGFASA KRKQQVRQLL AEQRLEFVLG GQVMHDEAVT 

       130        140        150        160        170        180 
HFDDQILQLT EGHGFLYETF GIRPQFSWQV DPFGASATTP TLLALAGFNG HIISRIDYDL 

       190        200        210        220        230        240 
KDTMQHTQGL QFVWRGSRSL EARQEIFTHV LDQYSYCSDG FMWNGSPRFP DRPFDMDYSA 

       250        260        270        280        290        300 
VEMPVSQDSM NHYVLNLVDN VNKRAAWFRT QHVLWPWGCD RQFFNASQQF ANMDRLMDHI 

       310        320        330        340        350        360 
NKHTPELGIS MQYATLAEYF QAVFAQDVSW QVRDHRDFLP YSSAPEQTWT GFYTSQSGLK 

       370        380        390        400        410        420 
RLARRASALL YAGESLFTRY MLSAAHRFLD PAWALTQLQQ LRWAVSEVQH HDGITGTHIL 

       430        440        450        460        470        480 
AVRDMFVEHL TTGMAGVRKL MDSIAQDMPL THSGPEPGGH VAMVYNPLAW TVTTVITLTV 

       490        500        510        520        530        540 
SFPEVSVTDE SGRPVLAQVQ DSKETPSAYD LHVLTTIPGL SYQHYIIKPI RKAREDSQEA 

       550        560        570        580        590        600 
AATVPSTIQF GLKLRRQDGQ VGRNLVPVKN SCYTVFLDKD TNLMHSIWER QSNRTVRMSQ 

       610        620        630        640        650        660 
EFLAYRSVYG YEEAVTSDNY LFTPNGTAEP AWAAVRMEVV EGQLLSEIRQ YFYRQANDSD 

       670        680        690        700        710        720 
HTYAIYSRLA HGPQDSAGEL LCHRIEQEYR VGPLELNHEV VLRTSTSLNT GLVLYSDNNG 

       730        740        750        760        770        780 
YQMQRRTYRH DRNNSVSLNY YPMAQSAFIQ DGGSRLVLLS EQAHGVSSQG NGQVEVMLHR 

       790        800        810        820        830        840 
RLWNKLEWTL QYNLTHDVTS VVRPVLWLLL GPRTLTTGLR QRSGLELQHR PVVLFRELGG 

       850        860        870        880        890        900 
TVQNGPGPRK QEPVTLPPSL HLQILSIPGW KYSSNHTVHL KNLQKGHYRR AKADFRRVLL 

       910        920        930        940        950        960 
RLHHLYEAGE HQALSRPVTL NLQSVLRGLG SVVAVEERSL TGTWDVNSLH RWSWKTEDGH 

       970        980        990 
HHRGSSRRPL PPLRGPNVTI HPKEIRTFFI HFQEQ 

« Hide

References

[1]"Cloning of complementary DNA encoding a 135-kilodalton protein secreted from porcine corpus epididymis and its identification as an epididymis-specific alpha-mannosidase."
Okamura N., Tamba M., Liao H.-J., Onoe S., Sugita Y., Dacheux F., Dacheux J.-L.
Mol. Reprod. Dev. 42:141-148(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Epididymis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28521 mRNA. Translation: BAA05877.1. Different initiation.
PIRT42762.
RefSeqNP_999014.1. NM_213849.1.
UniGeneSsc.14529.

3D structure databases

ProteinModelPortalQ28949.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396847.
KEGGssc:396847.

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_PIG
AccessionPrimary (citable) accession number: Q28949
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 16, 2001
Last modified: June 11, 2014
This is version 88 of the entry and version 2 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