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I0CME8

- HYAL_CONAQ

UniProt

I0CME8 - HYAL_CONAQ

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Protein
Hyaluronidase conohyal-ad1
Gene
N/A
Organism
Conus adamsonii (Cone snail)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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 By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei150 – 1501Proton donor By similarity

GO - Molecular functioni

  1. hyalurononglucosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase conohyal-ad1 (EC:3.2.1.35)
Short name:
Hya
Alternative name(s):
Hyaluronoglucosaminidase
OrganismiConus adamsonii (Cone snail)
Taxonomic identifieri1173533 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri5536. conohyal-ad1 precursor.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Propeptidei19 – 3315 By similarity
PRO_0000419900Add
BLAST
Chaini34 – ›347›314Hyaluronidase conohyal-ad1
PRO_0000419901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 343 By similarity

Post-translational modificationi

Contains 4 disulfide bonds By similarity.
Is N-linked glycosylated at three positions By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom duct.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

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.

Sequencei

Sequence statusi: Fragment.

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

I0CME8-1 [UniParc]FASTAAdd to Basket

« Hide

MRAVVVVTGL VVVVVTTTLS LQDHDVKSAS SPLSSSVDQG SSGDDCDEGL    50
PPPDQPFRVV WNHPDNCEKI NLHLPLDEYG IIFNKRRVFL GEEIQTLYDT 100
GPWPYINKTG CFINGGLPQL FNQPDNSETC KILGKNRIED FTGLGVLDFE 150
TWRAIYSTNF GTMENYQIES VNLVRKRHPD YSEKELKMVA EQEWQEAARK 200
IMTDKLAAGQ SLMPRGYWGY YLYPRTWDSK PDTKFRNNKI DWLWRQSTGL 250
YPSIYIYYDV VSKTDSVITK FVSDTVGEAV RVQNDFSPPN TPIYPYVMFQ 300
TMDNVFHKED HMKISLGLSA KMGAAGVILW GSSQNYKDFT TQCSRLQ 347
Length:347
Mass (Da):39,582
Last modified:June 13, 2012 - v1
Checksum:iA114DF88E0043228
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei347 – 3471

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
JN697597 mRNA. Translation: AFH78529.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
JN697597 mRNA. Translation: AFH78529.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ConoServeri 5536. conohyal-ad1 precursor.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view ]
PANTHERi PTHR11769. PTHR11769. 1 hit.
Pfami PF01630. Glyco_hydro_56. 1 hit.
[Graphical view ]
PRINTSi PR00846. GLHYDRLASE56.
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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].
    Tissue: Venom duct.

Entry informationi

Entry nameiHYAL_CONAQ
AccessioniPrimary (citable) accession number: I0CME8
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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