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Protein

Hyaluronidase

Gene
N/A
Organism
Apis mellifera (Honeybee)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides.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 sitei145 – 1451Proton donor1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.35. 387.

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase (EC:3.2.1.35)
Short name:
Hya
Alternative name(s):
Allergen Api m II
Hyaluronoglucosaminidase
Allergen: Api m 2
OrganismiApis mellifera (Honeybee)
Taxonomic identifieri7460 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis
ProteomesiUP000005203 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3089. Api m 2.0101.
46. Api m 2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Or 24Sequence AnalysisAdd
BLAST
Propeptidei29 – 335Sequence AnalysisPRO_0000012105
Chaini34 – 382349HyaluronidasePRO_0000012106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 345
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi221 ↔ 233
Glycosylationi263 – 2631N-linked (GlcNAc...) (complex)1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ08169.

PTM databases

UniCarbKBiQ08169.

Expressioni

Tissue specificityi

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.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi7460.GB18543-PA.

Structurei

Secondary structure

1
382
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 496Combined sources
Helixi51 – 577Combined sources
Helixi63 – 664Combined sources
Helixi74 – 763Combined sources
Beta strandi78 – 8811Combined sources
Beta strandi94 – 974Combined sources
Beta strandi103 – 1064Combined sources
Helixi111 – 1133Combined sources
Helixi116 – 13015Combined sources
Beta strandi138 – 1436Combined sources
Helixi151 – 1533Combined sources
Helixi156 – 1583Combined sources
Helixi159 – 17214Combined sources
Helixi178 – 20730Combined sources
Beta strandi211 – 2166Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi230 – 2323Combined sources
Helixi235 – 2428Combined sources
Helixi245 – 2484Combined sources
Beta strandi252 – 2554Combined sources
Beta strandi262 – 2643Combined sources
Helixi266 – 28621Combined sources
Beta strandi288 – 2903Combined sources
Beta strandi297 – 3026Combined sources
Beta strandi305 – 3095Combined sources
Helixi312 – 32413Combined sources
Beta strandi328 – 3336Combined sources
Helixi336 – 3383Combined sources
Beta strandi339 – 3413Combined sources
Helixi342 – 35413Combined sources
Helixi356 – 3616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCQX-ray1.60A33-382[»]
1FCUX-ray2.10A33-382[»]
1FCVX-ray2.65A33-382[»]
2J88X-ray2.60A33-382[»]
ProteinModelPortaliQ08169.
SMRiQ08169. Positions 42-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08169.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77606.
KOiK01197.
PhylomeDBiQ08169.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001329. Venom_Hyaluronidase.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
PR00847. HYALURONDASE.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q08169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPLVITEG MMIGVLLMLA PINALLLGFV QSTPDNNKTV REFNVYWNVP
60 70 80 90 100
TFMCHKYGLR FEEVSEKYGI LQNWMDKFRG EEIAILYDPG MFPALLKDPN
110 120 130 140 150
GNVVARNGGV PQLGNLTKHL QVFRDHLINQ IPDKSFPGVG VIDFESWRPI
160 170 180 190 200
FRQNWASLQP YKKLSVEVVR REHPFWDDQR VEQEAKRRFE KYGQLFMEET
210 220 230 240 250
LKAAKRMRPA ANWGYYAYPY CYNLTPNQPS AQCEATTMQE NDKMSWLFES
260 270 280 290 300
EDVLLPSVYL RWNLTSGERV GLVGGRVKEA LRIARQMTTS RKKVLPYYWY
310 320 330 340 350
KYQDRRDTDL SRADLEATLR KITDLGADGF IIWGSSDDIN TKAKCLQFRE
360 370 380
YLNNELGPAV KRIALNNNAN DRLTVDVSVD QV
Length:382
Mass (Da):44,260
Last modified:October 1, 1994 - v1
Checksum:i3E6822E95CA11856
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371N → D AA sequence (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti371 – 3711D → S in clone HYA-2.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10710 mRNA. Translation: AAA27730.1.
PIRiA47477.
RefSeqiNP_001011619.1. NM_001011619.1.
UniGeneiAme.165.

Genome annotation databases

GeneIDi406146.
KEGGiame:406146.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10710 mRNA. Translation: AAA27730.1.
PIRiA47477.
RefSeqiNP_001011619.1. NM_001011619.1.
UniGeneiAme.165.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCQX-ray1.60A33-382[»]
1FCUX-ray2.10A33-382[»]
1FCVX-ray2.65A33-382[»]
2J88X-ray2.60A33-382[»]
ProteinModelPortaliQ08169.
SMRiQ08169. Positions 42-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7460.GB18543-PA.

Protein family/group databases

Allergomei2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3089. Api m 2.0101.
46. Api m 2.
CAZyiGH56. Glycoside Hydrolase Family 56.

PTM databases

UniCarbKBiQ08169.

Proteomic databases

PaxDbiQ08169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi406146.
KEGGiame:406146.

Phylogenomic databases

eggNOGiNOG77606.
KOiK01197.
PhylomeDBiQ08169.

Enzyme and pathway databases

BRENDAi3.2.1.35. 387.

Miscellaneous databases

EvolutionaryTraceiQ08169.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001329. Venom_Hyaluronidase.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
PR00847. HYALURONDASE.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiHUGA_APIME
AccessioniPrimary (citable) accession number: Q08169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 24, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.