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Protein

Hyaluronidase conohyal-Cn1

Gene
N/A
Organism
Conus consors (Singed cone)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei151 – 1511Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase conohyal-Cn1 (EC:3.2.1.35)
Short name:
Hya
Alternative name(s):
Hyaluronoglucosaminidase
OrganismiConus consors (Singed cone)
Taxonomic identifieri101297 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 33151 PublicationPRO_0000419902Add
BLAST
Chaini34 – 448415Hyaluronidase conohyal-Cn1PRO_0000419903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 344By similarity
Glycosylationi141 – 1411N-linked (GlcNAc...)1 Publication
Glycosylationi169 – 1691N-linked (GlcNAc...)Curated
Glycosylationi361 – 3611N-linked (GlcNAc...)1 Publication
Disulfide bondi369 ↔ 380By similarity
Disulfide bondi374 ↔ 413By similarity
Disulfide bondi415 ↔ 424By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom duct.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini413 – 42412EGF-likeAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.Curated
Contains 1 EGF-like domain.Curated

Keywords - Domaini

EGF-like domain, Signal

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PRINTSiPR00846. GLHYDRLASE56.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

I0CME7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAVVVVTGL VVVVVATALS LPNHDVKSAT SSRSSSDYQG SSGDDCDEGL
60 70 80 90 100
PPPDQPFRVV WNHPDNCERI KLHLPLDDYG IIFNKLRVFL GEEIQTLYDT
110 120 130 140 150
GPWPYISETG KFINGGLPQS FNHPDNDGET QRILKKHRPE NFTGLGVLDF
160 170 180 190 200
ETWRAIYSTN FGPMTIYQNE SVKLVKEQHP DYDQKKLTKV AEKEWQQAAK
210 220 230 240 250
DIMSNKLKIA QEVMPRGHWG YYLYPRTWDN KRDTKFRNDK INWLWRQSTG
260 270 280 290 300
LYPSIYIYDF SKTESAITKF VSDTVGEAVR VQKEFSPPNT PIYPYVMFQT
310 320 330 340 350
MDNIFHYEDH LKISLGLSAK MGAAGVVLWG TSKHYKESTR QWQCQQLQEH
360 370 380 390 400
IRTVLGPLVK NVTQMMTDCS RAICEGHGRC VHNSHDVILG ETESQRLSDL
410 420 430 440
CSTRQSRFRD YHCRCYSAWE GACCQTLRPS RCQKREQRNV HGGGDLID
Length:448
Mass (Da):51,427
Last modified:June 13, 2012 - v1
Checksum:i57E4073753DDB803
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti78 – 781D → E.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JN697596 mRNA. Translation: AFH78528.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JN697596 mRNA. Translation: AFH78528.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PRINTSiPR00846. GLHYDRLASE56.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiHYAL_CONCN
AccessioniPrimary (citable) accession number: I0CME7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: June 13, 2012
Last modified: January 7, 2015
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.