Q812F3 · HYAL5_MOUSE

  • Protein
    Hyaluronidase-5
  • Gene
    Hyal5
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the hydrolysis of hyaluronan into smaller oligosaccharide fragments (PubMed:16330764, PubMed:16925524, PubMed:19605784).
Does not appear to be essential for fertilization (PubMed:19605784).

Catalytic activity

  • Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.
    EC:3.2.1.35 (UniProtKB | ENZYME | Rhea)

pH Dependence

Optimum pH is 5-7.

Features

Showing features for active site.

152650100150200250300350400450500
TypeIDPosition(s)Description
Active site147Proton donor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentacrosomal membrane
Cellular Componentacrosomal vesicle
Cellular Componentexternal side of plasma membrane
Cellular Componentextracellular region
Cellular Componentplasma membrane
Molecular Functionhyalurononglucosaminidase activity
Biological Processcarbohydrate metabolic process
Biological Processfusion of sperm to egg plasma membrane involved in single fertilization
Biological Processhyaluronan catabolic process
Biological Processpenetration of zona pellucida

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Hyaluronidase-5
  • EC number
  • Short names
    Hyal-5
  • Alternative names
    • Hyaluronoglucosaminidase-5

Gene names

    • Name
      Hyal5

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 129/SvJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q812F3

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Lipid-anchor, GPI-anchor
Secreted
Note: Located on the plasma and acrosomal membranes of acrosome-intact (AI) sperm and released during the acrosome reaction.

Keywords

Phenotypes & Variants

Disruption phenotype

No visible phenotype. Viable and fertile.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-35
ChainPRO_000044163636-526Hyaluronidase-5
Disulfide bond60↔351
Glycosylation165N-linked (GlcNAc...) asparagine
Glycosylation179N-linked (GlcNAc...) asparagine
Disulfide bond223↔237
Disulfide bond376↔387
Disulfide bond381↔435
Disulfide bond437↔443

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in testis, epididymal sperm and epididymides (at protein level) (PubMed:16330764, PubMed:19605784).
Expressed at highest levels in testis with lesser amounts in epididymal sperm (PubMed:16330764, PubMed:16925524, PubMed:19605784).

Developmental stage

Detected in the developing testis at postnatal day 20, with increasing levels through development.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    526
  • Mass (Da)
    60,808
  • Last updated
    2003-06-01 v1
  • Checksum
    94DF140035DB52C9
MRVLYFKHSFFRSLLKSNGLPQTLLVFLLIPCYLTVDFRAPPLIPDVPFLWAWNAPTESCFTRFNQPLDLGLFSLVGSPRKSATGQPVTIFYSDRLGLYPYIDDSQLIFNGGLPQLVSLKSHLEVAKTDILHYMPIDNVGLAVIDWEEWRPTWARNWKPKDIYRNKSIELVQQQNILLNFTEAVKWAKEEFEEAARHFMEETLRLGKSLRPNHLWGFYLFPDCYNNKFQVADYKGECPDIEKHRNDALFWIWEESTALYPSIYLKSSLKSSPQAALYVRNRVQEAIRVSKVKDPRNPLPIFVYFRIVFTDLTYQYLYEDDLVNTIGETIALGTSGMVMWGTLSLSQTMKSCLDLHDYLKTILNPYIINVTLAAKMCSQTLCQNQGVCSRKDWNSNDYLHLNPQNFQIHFVKHGKYEIRGNPTLENLLYFSQKFRCSCFAHLNCQERADIESVSTVSVCTLEDICINSLVISDKSELPKDWNRPYFVNSNQSDITSSATVSPCVPRKDVSGYLVVLSLYSQHLKYSL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB085680
EMBL· GenBank· DDBJ
BAC55071.1
EMBL· GenBank· DDBJ
Genomic DNA
AK133387
EMBL· GenBank· DDBJ
BAE21628.1
EMBL· GenBank· DDBJ
mRNA
AC127559
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH466533
EMBL· GenBank· DDBJ
EDL13813.1
EMBL· GenBank· DDBJ
Genomic DNA
BC145992
EMBL· GenBank· DDBJ
AAI45993.1
EMBL· GenBank· DDBJ
mRNA
BC145994
EMBL· GenBank· DDBJ
AAI45995.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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