Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q08169

- HUGA_APIME

UniProt

Q08169 - HUGA_APIME

Protein

Hyaluronidase

Gene
N/A
Organism
Apis mellifera (Honeybee)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. hyalurononglucosaminidase activity Source: UniProtKB-EC

    GO - Biological processi

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

    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

    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)2 Publications

    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

    1
    382
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08169.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 56 family.Curated

    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

    Experimental Info

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

    Natural variant

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

    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: October 1, 2014
    This is version 99 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