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Q29548 (HEXB_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. 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:
Beta-hexosaminidase subunit beta

EC=3.2.1.52
Alternative name(s):
65 kDa epididymal boar protein
Beta-N-acetylhexosaminidase subunit beta
Short name=Hexosaminidase subunit B
N-acetyl-beta-glucosaminidase subunit beta
Gene names
Name:HEXB
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues By similarity.

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Sequence caution

The sequence CAA63123.1 differs from that shown. Reason: Frameshift at positions 3 and 16.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 531510Beta-hexosaminidase subunit beta
PRO_0000012007

Sites

Active site3291Proton donor By similarity

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Disulfide bond67 ↔ 111 By similarity
Disulfide bond283 ↔ 334 By similarity
Disulfide bond508 ↔ 525 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29548 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: F55D62D6937E51C5

FASTA53161,050
        10         20         30         40         50         60 
MEVLPGLLRL LAALVVAERW ARDTSGAESL GLWPLPFAVD ISPRSLHLSP NNFFFGHSPT 

        70         80         90        100        110        120 
SKAGSSCEIL QEAFRRYYDF IFGFYKWHQG SYQLCFGTEL QQLQVHVESE CDTFPSISSN 

       130        140        150        160        170        180 
ESYVLHVKGP EALLRANTVW GALRGLETFS QLIYQDSYGT FTVNESEIID FPRFPHRGIL 

       190        200        210        220        230        240 
IDTGRHFLSV KTIFKTLDAM AFNKFNVLHW HIVDDQSFPY QSINFGVLSS KGSYSLSHVY 

       250        260        270        280        290        300 
TPNDVRMVIE YARIRGIRVM PEFDTPGHSR SWGKGQKDLL TPCYRKQVLS GTFGPINPIL 

       310        320        330        340        350        360 
NTTYNFLSKF FKEISTVFPD EFIHIGGDEV DFDCWASNSE ILQFMQEKGF SQISLNSNLC 

       370        380        390        400        410        420 
TVFKISNMIS AMKKRPIVWQ EAFDGRDKFM PGTVVQVWKI EDYKWEQSLI TKAGFPVILS 

       430        440        450        460        470        480 
APWYLDLISY GQDWKNYYEV EPQDFPGSDK ERKRVLGGEA CLWGEYVDAT NLTPRLWPRA 

       490        500        510        520        530 
SAVGERLWSH KDVRDIHDAY SRLTIHRCRM VRRGIAAEPL FTGYCNHEHR M 

« Hide

References

[1]"Purification, cloning and sequencing analysis of B-N-acetyl-hexosaminidase from epididymal boar."
Syntin P., Okamura N., Guillou F., Dacheux F., Dacheux J.-L.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Epididymis.
[2]"Characterization and identification of proteins secreted in the various regions of the adult boar epididymis."
Syntin P., Dacheux F., Druart X., Gatti J.L., Okamura N., Dacheux J.-L.
Biol. Reprod. 55:956-974(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Epididymis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92379 mRNA. Translation: CAA63123.1. Frameshift.
RefSeqNP_999086.1. NM_213921.1.
UniGeneSsc.3196.

3D structure databases

ProteinModelPortalQ29548.
SMRQ29548. Positions 31-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000014965.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PaxDbQ29548.
PRIDEQ29548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396958.
KEGGssc:396958.

Organism-specific databases

CTD3074.

Phylogenomic databases

eggNOGCOG3525.
HOGENOMHOG000157972.
HOVERGENHBG005961.
KOK12373.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEXB_PIG
AccessionPrimary (citable) accession number: Q29548
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 10, 2005
Last modified: November 13, 2013
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