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P85841 (HYAL1_TITSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 14. 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 1

Short name=TsHyal-1
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase
Venom spreading factor
OrganismTityus serrulatus (Brazilian scorpion)
Taxonomic identifier6887 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeTityus

Protein attributes

Sequence length385 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subcellular location

Secreted Ref.1 Ref.2.

Tissue specificity

Expressed by the venom gland. Ref.1 Ref.2

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 peptide‹1›1 Ref.2
Chain2 – 385384Hyaluronidase 1
PRO_0000343459

Regions

Domain328 – 38255EGF-like By similarity

Sites

Active site1041Proton donor By similarity

Amino acid modifications

Glycosylation211N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Disulfide bond14 ↔ 307 By similarity
Disulfide bond173 ↔ 216 By similarity
Disulfide bond180 ↔ 194 By similarity
Disulfide bond332 ↔ 343 By similarity
Disulfide bond337 ↔ 371 By similarity
Disulfide bond373 ↔ 381 By similarity

Natural variations

Natural variant21D → Q. Ref.2

Experimental info

Sequence conflict21D → K AA sequence Ref.2
Sequence conflict211N → C AA sequence Ref.2
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P85841 [UniParc].

Last modified May 14, 2014. Version 2.
Checksum: E0D2D508C5C3C35B

FASTA38544,618
        10         20         30         40         50         60 
ADFKVYWEVP SFLCSKRFKI NVTEVLTSHE ILVNQGESFN GDKIVIFYEN QLGKYPHIDS 

        70         80         90        100        110        120 
NNVEINGGIL QVADLAKHLK VAKDNITKFV PNPNFNGVGV IDWEAWRPSW EFNWGKLKVY 

       130        140        150        160        170        180 
KEKSIDLVKS KHPEWPSDRV EKVAKEEWEE SAKEWMVKTL KLAQEMRPNA VWCYYLFPDC 

       190        200        210        220        230        240 
YNYFGKDQPS QFSCSSRIQK ENSRLSWLWN QSTAICLSIY IQESHVTKYN MSQRTWWIDA 

       250        260        270        280        290        300 
RLREAIRVSE HRPNIPIYPY INYILPGTNQ TVPAMDFKRT LGQIASLGLD GALLWGSSYH 

       310        320        330        340        350        360 
VLTESQCKIT SDYVKSVIAP TVATVVLNTN RCSQIICKGR GNCVWPEEPF SSWKYLVDPK 

       370        380 
MPVFKPTNIH CKCKGYLGRY CEIPK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
KF623285 mRNA. Translation: AHF72517.1.

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]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHYAL1_TITSE
AccessionPrimary (citable) accession number: P85841
Secondary accession number(s): W0HJY6
Entry history
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 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