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Q08169 (HUGA_APIME) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Short name=Hya
EC=3.2.1.35
Alternative name(s):
Allergen Api m II
Hyaluronoglucosaminidase
Allergen=Api m 2
OrganismApis mellifera (Honeybee) [Reference proteome]
Taxonomic identifier7460 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
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.

Catalytic activity

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

Subunit structure

Homotetramer.

Subcellular location

Secreted.

Tissue specificity

Expressed in the venom glands of worker bees. It is also detected in the testes of drones but not in the queen-bee venom glands or in pupae.

Post-translational modification

N-glycosylated. Glycans found include a majority of small oligosaccharides (Man1-3GlcNAc2), most of which are either alpha 1,3-monofucosylated or alpha 1,3-(alpha 1,6-)difucosylated at the innermost GlcNAc residue, approximately 5% of high-mannose type structures, and 8% contains the terminal trisaccharide GalNAc beta 1-4[Fuc alpha 1-3]GlcNAc beta 1-in beta 1,2-linkage to the core alpha 1,3-mannosyl residue. Ref.3 Ref.4

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Ontologies

Keywords
   Cellular componentSecreted
   DiseaseAllergen
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response

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 peptide1 – 2828Or 24 Potential
Propeptide29 – 335 Potential
PRO_0000012105
Chain34 – 382349Hyaluronidase
PRO_0000012106

Sites

Active site1451Proton donor Probable

Amino acid modifications

Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation2631N-linked (GlcNAc...) (complex) Ref.4
Disulfide bond54 ↔ 345
Disulfide bond221 ↔ 233

Natural variations

Natural variant3711D → S in clone HYA-2.

Experimental info

Sequence conflict371N → D AA sequence Ref.2

Secondary structure

............................................................ 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08169 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 3E6822E95CA11856

FASTA38244,260
        10         20         30         40         50         60 
MSRPLVITEG MMIGVLLMLA PINALLLGFV QSTPDNNKTV REFNVYWNVP TFMCHKYGLR 

        70         80         90        100        110        120 
FEEVSEKYGI LQNWMDKFRG EEIAILYDPG MFPALLKDPN GNVVARNGGV PQLGNLTKHL 

       130        140        150        160        170        180 
QVFRDHLINQ IPDKSFPGVG VIDFESWRPI FRQNWASLQP YKKLSVEVVR REHPFWDDQR 

       190        200        210        220        230        240 
VEQEAKRRFE KYGQLFMEET LKAAKRMRPA ANWGYYAYPY CYNLTPNQPS AQCEATTMQE 

       250        260        270        280        290        300 
NDKMSWLFES EDVLLPSVYL RWNLTSGERV GLVGGRVKEA LRIARQMTTS RKKVLPYYWY 

       310        320        330        340        350        360 
KYQDRRDTDL SRADLEATLR KITDLGADGF IIWGSSDDIN TKAKCLQFRE YLNNELGPAV 

       370        380 
KRIALNNNAN DRLTVDVSVD QV 

« Hide

References

[1]"Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm."
Gmachl M., Kreil G.
Proc. Natl. Acad. Sci. U.S.A. 90:3569-3573(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"The cross-reactivity between bee and vespid hyaluronidases has a structural basis."
Jacobson R.S., Hoffman D.R., Kemeny D.M.
J. Allergy Clin. Immunol. 89:292-292(1991)
Cited for: PROTEIN SEQUENCE OF 34-64.
Tissue: Venom.
[3]"The asparagine-linked carbohydrate of honeybee venom hyaluronidase."
Kubelka V., Altmann F., Marz L.
Glycoconj. J. 12:77-83(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[4]"N-glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1."
Kolarich D., Altmann F.
Anal. Biochem. 285:64-75(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-263.
[5]"Crystal structure of hyaluronidase, a major allergen of bee venom."
Markovic-Housley Z., Miglierini G., Soldatova L., Rizkallah P.J., Mueller U., Schirmer T.
Structure 8:1025-1035(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 42-362, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10710 mRNA. Translation: AAA27730.1.
PIRA47477.
RefSeqNP_001011619.1. NM_001011619.1.
UniGeneAme.165.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCQX-ray1.60A33-382[»]
1FCUX-ray2.10A33-382[»]
1FCVX-ray2.65A33-382[»]
2J88X-ray2.60A33-382[»]
ProteinModelPortalQ08169.
SMRQ08169. Positions 42-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7460.Q08169.

Protein family/group databases

Allergome2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3089. Api m 2.0101.
46. Api m 2.
CAZyGH56. Glycoside Hydrolase Family 56.

PTM databases

UniCarbKBQ08169.

Proteomic databases

PaxDbQ08169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID406146.
KEGGame:406146.

Phylogenomic databases

eggNOGNOG77606.
InParanoidQ08169.
KOK01197.
PhylomeDBQ08169.

Enzyme and pathway databases

BRENDA3.2.1.35. 387.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001329. Venom_Hyaluronidase.
[Graphical view]
PANTHERPTHR11769. PTHR11769. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PRINTSPR00846. GLHYDRLASE56.
PR00847. HYALURONDASE.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ08169.

Entry information

Entry nameHUGA_APIME
AccessionPrimary (citable) accession number: Q08169
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Allergens

Nomenclature of allergens and list of entries