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P85841

- HYAL1_TITSE

UniProt

P85841 - HYAL1_TITSE

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Protein
Hyaluronidase 1
Gene
N/A
Organism
Tityus serrulatus (Brazilian scorpion)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides By similarity. Is an important component of the venom, since anti-hyaluronidase serum effectively neutralizes the lethal effet of the venom injected into mice. It may act by increasing the diffusion of other venom proteins 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Proton 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 1 (EC:3.2.1.35)
Short name:
TsHyal-1
Alternative name(s):
Hyaluronoglucosaminidase
Venom spreading factor
OrganismiTityus serrulatus (Brazilian scorpion)
Taxonomic identifieri6887 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeTityus

Subcellular locationi

Secreted 2 Publications

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 peptidei‹1 – 1›11 Publication
Chaini2 – 385384Hyaluronidase 1
PRO_0000343459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi14 ↔ 307 By similarity
Glycosylationi21 – 211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi85 – 851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi173 ↔ 216 By similarity
Disulfide bondi180 ↔ 194 By similarity
Glycosylationi210 – 2101N-linked (GlcNAc...) Reviewed prediction
Glycosylationi230 – 2301N-linked (GlcNAc...) Reviewed prediction
Glycosylationi269 – 2691N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi332 ↔ 343 By similarity
Disulfide bondi337 ↔ 371 By similarity
Disulfide bondi373 ↔ 381 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.2 Publications

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini328 – 38255EGF-like By similarity
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

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]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Fragment.

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

P85841-1 [UniParc]FASTAAdd to Basket

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ADFKVYWEVP SFLCSKRFKI NVTEVLTSHE ILVNQGESFN GDKIVIFYEN    50
QLGKYPHIDS NNVEINGGIL QVADLAKHLK VAKDNITKFV PNPNFNGVGV 100
IDWEAWRPSW EFNWGKLKVY KEKSIDLVKS KHPEWPSDRV EKVAKEEWEE 150
SAKEWMVKTL KLAQEMRPNA VWCYYLFPDC YNYFGKDQPS QFSCSSRIQK 200
ENSRLSWLWN QSTAICLSIY IQESHVTKYN MSQRTWWIDA RLREAIRVSE 250
HRPNIPIYPY INYILPGTNQ TVPAMDFKRT LGQIASLGLD GALLWGSSYH 300
VLTESQCKIT SDYVKSVIAP TVATVVLNTN RCSQIICKGR GNCVWPEEPF 350
SSWKYLVDPK MPVFKPTNIH CKCKGYLGRY CEIPK 385
Length:385
Mass (Da):44,618
Last modified:May 14, 2014 - v2
Checksum:iE0D2D508C5C3C35B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21D → Q.1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21D → K AA sequence 1 Publication
Sequence conflicti21 – 211N → C AA sequence 1 Publication

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
KF623285 mRNA. Translation: AHF72517.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
KF623285 mRNA. Translation: AHF72517.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 ]
PIRSFi PIRSF038193. Hyaluronidase. 1 hit.
PRINTSi PR00846. GLHYDRLASE56.
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Molecular, immunological, and biological characterization of Tityus serrulatus venom hyaluronidase: new insights into its role in envenomation."
    Horta C.C., Magalhaes B.F., Oliveira-Mendes B.B., do Carmo A.O., Duarte C.G., Felicori L.F., Machado-de-Avila R.A., Chavez-Olortegui C., Kalapothakis E.
    PLoS Negl. Trop. Dis. 8:E2693-E2693(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING.
    Tissue: Venom gland.
  2. "Hyaluronidase from venom of Brazilian scorpion Tityus serrulatus."
    Richardson M., Borges M.H., Cordeiro M.N., Pimenta A.M.C., de Lima M.E., Rates B.
    Submitted (MAY-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-35, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT GLN-2.
    Tissue: Venom.

Entry informationi

Entry nameiHYAL1_TITSE
AccessioniPrimary (citable) accession number: P85841
Secondary accession number(s): W0HJY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: May 14, 2014
Last modified: June 11, 2014
This is version 14 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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

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