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I0CME8 (HYAL_CONAQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 10. 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 conohyal-ad1

Short name=Hya
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase
OrganismConus adamsonii (Cone snail)
Taxonomic identifier1173533 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Protein attributes

Sequence length347 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hyaluronidase catalyzes the hydrolysis of hyaluronic acid (HA), an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues. In venom, they are known to enhance diffusion of the venom by degrading the extracellular matrix By similarity.

Catalytic activity

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

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom duct.

Post-translational modification

Contains 4 disulfide bonds By similarity.

Is N-linked glycosylated at three positions By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
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

Signal peptide1 – 1818 Potential
Propeptide19 – 3315 By similarity
PRO_0000419900
Chain34 – ›347›314Hyaluronidase conohyal-ad1
PRO_0000419901

Sites

Active site1501Proton donor By similarity

Amino acid modifications

Disulfide bond67 ↔ 343 By similarity

Experimental info

Non-terminal residue3471

Sequences

Sequence LengthMass (Da)Tools
I0CME8 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: A114DF88E0043228

FASTA34739,582
        10         20         30         40         50         60 
MRAVVVVTGL VVVVVTTTLS LQDHDVKSAS SPLSSSVDQG SSGDDCDEGL PPPDQPFRVV 

        70         80         90        100        110        120 
WNHPDNCEKI NLHLPLDEYG IIFNKRRVFL GEEIQTLYDT GPWPYINKTG CFINGGLPQL 

       130        140        150        160        170        180 
FNQPDNSETC KILGKNRIED FTGLGVLDFE TWRAIYSTNF GTMENYQIES VNLVRKRHPD 

       190        200        210        220        230        240 
YSEKELKMVA EQEWQEAARK IMTDKLAAGQ SLMPRGYWGY YLYPRTWDSK PDTKFRNNKI 

       250        260        270        280        290        300 
DWLWRQSTGL YPSIYIYYDV VSKTDSVITK FVSDTVGEAV RVQNDFSPPN TPIYPYVMFQ 

       310        320        330        340 
TMDNVFHKED HMKISLGLSA KMGAAGVILW GSSQNYKDFT TQCSRLQ 

« Hide

References

[1]"Recruitment of glycosyl hydrolase proteins in a cone snail venomous arsenal: further insights into biomolecular features of Conus venoms."
Violette A., Leonardi A., Piquemal D., Terrat Y., Biass D., Dutertre S., Noguier F., Ducancel F., Stocklin R., Krizaj I., Favreau P.
Mar. Drugs 10:258-280(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom duct.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
JN697597 mRNA. Translation: AFH78529.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ConoServer5536. conohyal-ad1 precursor.

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]
PRINTSPR00846. GLHYDRLASE56.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHYAL_CONAQ
AccessionPrimary (citable) accession number: I0CME8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: June 13, 2012
Last modified: February 19, 2014
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries