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I0CME7 (HYAL_CONCN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. 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 conohyal-Cn1

Short name=Hya
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase
OrganismConus consors (Singed cone)
Taxonomic identifier101297 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Catalytic activity

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

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom duct.

Miscellaneous

Found in both injectable (milked) (IV) and dissected venom (DV) (Ref.1).

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainEGF-like domain
Signal
   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

Signal peptide1 – 1818 Potential
Propeptide19 – 3315
PRO_0000419902
Chain34 – 448415Hyaluronidase conohyal-Cn1
PRO_0000419903

Regions

Domain413 – 42412EGF-like

Sites

Active site1511Proton donor By similarity

Amino acid modifications

Glycosylation1411N-linked (GlcNAc...) Ref.1
Glycosylation1691N-linked (GlcNAc...) Probable
Glycosylation3611N-linked (GlcNAc...) Ref.1
Disulfide bond67 ↔ 344 By similarity
Disulfide bond369 ↔ 380 By similarity
Disulfide bond374 ↔ 413 By similarity
Disulfide bond415 ↔ 424 By similarity

Natural variations

Natural variant781D → E. Ref.1

Sequences

Sequence LengthMass (Da)Tools
I0CME7 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 57E4073753DDB803

FASTA44851,427
        10         20         30         40         50         60 
MRAVVVVTGL VVVVVATALS LPNHDVKSAT SSRSSSDYQG SSGDDCDEGL PPPDQPFRVV 

        70         80         90        100        110        120 
WNHPDNCERI KLHLPLDDYG IIFNKLRVFL GEEIQTLYDT GPWPYISETG KFINGGLPQS 

       130        140        150        160        170        180 
FNHPDNDGET QRILKKHRPE NFTGLGVLDF ETWRAIYSTN FGPMTIYQNE SVKLVKEQHP 

       190        200        210        220        230        240 
DYDQKKLTKV AEKEWQQAAK DIMSNKLKIA QEVMPRGHWG YYLYPRTWDN KRDTKFRNDK 

       250        260        270        280        290        300 
INWLWRQSTG LYPSIYIYDF SKTESAITKF VSDTVGEAVR VQKEFSPPNT PIYPYVMFQT 

       310        320        330        340        350        360 
MDNIFHYEDH LKISLGLSAK MGAAGVVLWG TSKHYKESTR QWQCQQLQEH IRTVLGPLVK 

       370        380        390        400        410        420 
NVTQMMTDCS RAICEGHGRC VHNSHDVILG ETESQRLSDL CSTRQSRFRD YHCRCYSAWE 

       430        440 
GACCQTLRPS RCQKREQRNV HGGGDLID 

« 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], PROTEIN SEQUENCE OF 34-43 AND 137-154, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, VARIANT GLU-78, GLYCOSYLATION AT ASN-141 AND ASN-361.
Tissue: Venom and Venom duct.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
JN697596 mRNA. Translation: AFH78528.1.

3D structure databases

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]
PRINTSPR00846. GLHYDRLASE56.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHYAL_CONCN
AccessionPrimary (citable) accession number: I0CME7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: June 13, 2012
Last modified: February 19, 2014
This is version 9 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