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I0CME8

- HYAL_CONAQ

UniProt

I0CME8 - HYAL_CONAQ

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
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    • History
      Entry version 11 (01 Oct 2014)
      Sequence version 1 (13 Jun 2012)
      Previous versions | rss
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    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.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 donorBy similarity

    GO - Molecular functioni

    1. hyalurononglucosaminidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 3315By similarityPRO_0000419900Add
    BLAST
    Chaini34 – ›347›314Hyaluronidase conohyal-ad1PRO_0000419901Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi67 ↔ 343PROSITE-ProRule annotation

    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

    Belongs to the glycosyl hydrolase 56 family.Curated

    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

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    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

    Experimental Info

    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: October 1, 2014
    This is version 11 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