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B3EWP2 (HYAL_CRODU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 9. 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:
Hyaluronidase CdtHya1

Short name=Hya
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase
Venom spreading factor
OrganismCrotalus durissus terrificus (South American rattlesnake)
Taxonomic identifier8732 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

Protein attributes

Sequence length44 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Snake venom endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. In venom, it is not toxic by itself, but increases the diffusion of other venom proteins such as crotoxin (a neurotoxic and myotoxic PLA2) by degrading the extracellular matrix. In addition, it displays antiedematogenic activity, since it significantly diminishes the oedematogenic activity of crotoxin (probably by direct substrate hydrolysis, since hayluronan possesses strong water-binding capacity). Ref.1 Ref.2

Catalytic activity

Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate. UniProtKB P86274

Subunit structure

Monomer. Ref.1 Ref.2

Subcellular location

Secreted Ref.1 Ref.2.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

Contains disulfide bonds.

Glycosylated. Ref.1 Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Ref.1 Ref.2

Temperature dependence:

Optimum temperature is 37 degrees Celsius. Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhyalurononglucosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›44›44Hyaluronidase CdtHya1
PRO_0000419017

Amino acid modifications

Disulfide bond24 ↔ ? By similarity

Experimental info

Non-terminal residue441

Sequences

Sequence LengthMass (Da)Tools
B3EWP2 [UniParc].

Last modified September 5, 2012. Version 1.
Checksum: DFD6932D5E3988B0

FASTA445,212
        10         20         30         40 
MQAKAPMYPN EPFLVFWNAP TTQCRLRYKV DLDLNTFHIV TNAR 

« Hide

References

[1]"Functional and structural characterization of hyaluronidase isolated from Crotalus durissus terrificus snake venom."
Bordon K.C.F.
Thesis (2012), University of Sao Paulo, Brazil
Cited for: PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, DISULFIDE BONDS.
Tissue: Venom.
[2]"Isolation, enzymatic characterization and antiedematogenic activity of the first reported rattlesnake hyaluronidase from Crotalus durissus terrificus venom."
Bordon K.C.F., Perino M.G., Giglio J.R., Arantes E.C.
Biochimie 94:2740-2748(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, DISULFIDE BONDS.
Tissue: Venom.

Cross-references

3D structure databases

ProteinModelPortalB3EWP2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERPTHR11769. PTHR11769. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHYAL_CRODU
AccessionPrimary (citable) accession number: B3EWP2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: September 5, 2012
Last modified: October 16, 2013
This is version 9 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