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Q08169

- HUGA_APIME

UniProt

Q08169 - HUGA_APIME

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Protein
Hyaluronidase
Gene
N/A
Organism
Apis mellifera (Honeybee)
Status
Reviewed - 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 donor Inferred

GO - Molecular functioni

  1. hyalurononglucosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. defense response Source: InterPro
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: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
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 24 Reviewed prediction
Add
BLAST
Propeptidei29 – 335 Reviewed prediction
PRO_0000012105
Chaini34 – 382349Hyaluronidase
PRO_0000012106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 345
Glycosylationi115 – 1151N-linked (GlcNAc...) Reviewed prediction
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.Q08169.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ08169.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77606.
InParanoidiQ08169.
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]
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

MSRPLVITEG MMIGVLLMLA PINALLLGFV QSTPDNNKTV REFNVYWNVP    50
TFMCHKYGLR FEEVSEKYGI LQNWMDKFRG EEIAILYDPG MFPALLKDPN 100
GNVVARNGGV PQLGNLTKHL QVFRDHLINQ IPDKSFPGVG VIDFESWRPI 150
FRQNWASLQP YKKLSVEVVR REHPFWDDQR VEQEAKRRFE KYGQLFMEET 200
LKAAKRMRPA ANWGYYAYPY CYNLTPNQPS AQCEATTMQE NDKMSWLFES 250
EDVLLPSVYL RWNLTSGERV GLVGGRVKEA LRIARQMTTS RKKVLPYYWY 300
KYQDRRDTDL SRADLEATLR KITDLGADGF IIWGSSDDIN TKAKCLQFRE 350
YLNNELGPAV KRIALNNNAN DRLTVDVSVD QV 382
Length:382
Mass (Da):44,260
Last modified:October 1, 1994 - v1
Checksum:i3E6822E95CA11856
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L10710 mRNA. Translation: AAA27730.1 .
PIRi A47477.
RefSeqi NP_001011619.1. NM_001011619.1.
UniGenei Ame.165.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FCQ X-ray 1.60 A 33-382 [» ]
1FCU X-ray 2.10 A 33-382 [» ]
1FCV X-ray 2.65 A 33-382 [» ]
2J88 X-ray 2.60 A 33-382 [» ]
ProteinModelPortali Q08169.
SMRi Q08169. Positions 42-365.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7460.Q08169.

Protein family/group databases

Allergomei 2493. Api m A1-A2.
2778. Api m A1-A2-A3.
3089. Api m 2.0101.
46. Api m 2.
CAZyi GH56. Glycoside Hydrolase Family 56.

PTM databases

UniCarbKBi Q08169.

Proteomic databases

PaxDbi Q08169.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 406146.
KEGGi ame:406146.

Phylogenomic databases

eggNOGi NOG77606.
InParanoidi Q08169.
KOi K01197.
PhylomeDBi Q08169.

Enzyme and pathway databases

BRENDAi 3.2.1.35. 387.

Miscellaneous databases

EvolutionaryTracei Q08169.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001329. Venom_Hyaluronidase.
[Graphical view ]
PANTHERi PTHR11769. PTHR11769. 1 hit.
Pfami PF01630. Glyco_hydro_56. 1 hit.
[Graphical view ]
PRINTSi PR00846. GLHYDRLASE56.
PR00847. HYALURONDASE.
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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 11, 2014
This is version 98 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

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