ID   HUGA_VESMG              Reviewed;         357 AA.
AC   P86875; E7BBB9;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=Hyaluronidase;
DE            Short=Hya {ECO:0000250|UniProtKB:Q08169};
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase {ECO:0000250|UniProtKB:Q08169};
DE   AltName: Allergen=Vesp ma 2;
DE   Flags: Precursor;
OS   Vespa magnifica (Hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=202807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-54; 73-91; 125-135;
RP   200-220; 283-304 AND 339-357, SUBCELLULAR LOCATION, AND ALLERGEN.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=22384100; DOI=10.1371/journal.pone.0031920;
RA   An S., Chen L., Wei J.F., Yang X., Ma D., Xu X., Xu X., He S., Lu J.,
RA   Lai R.;
RT   "Purification and characterization of two new allergens from the venom of
RT   Vespa magnifica.";
RL   PLoS ONE 7:E31920-E31920(2012).
CC   -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC       small oligosaccharides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC         glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC         Evidence={ECO:0000250|UniProtKB:Q08169};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q08169,
CC       ECO:0000269|PubMed:22384100}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:22384100}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000255}.
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DR   EMBL; FR749885; CBY83816.1; -; mRNA.
DR   AlphaFoldDB; P86875; -.
DR   SMR; P86875; -.
DR   Allergome; 9454; Vesp ma 2.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   InterPro; IPR001329; Venom_Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF35; HYALURONIDASE; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   PRINTS; PR00847; HYALURONDASE.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:22384100"
FT   CHAIN           27..357
FT                   /note="Hyaluronidase"
FT                   /id="PRO_0000405128"
FT   ACT_SITE        135
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..334
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   DISULFID        211..223
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   CONFLICT        160
FT                   /note="R -> P (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="E -> G (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="N -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        335
FT                   /note="T -> M (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  41948 MW;  709A79B50DEE9A53 CRC64;
     MLLVTLFLFF LQALVNGDSC GSNCEKSERP KRVFNIYWNV PTFMCHQYGL YFDEVTNFNI
     KHNSKDNFQG DKIAIFYDPG EFPALLPLNY GKYKIRNGGV PQEGNITIHL QRFIEYLDKT
     YPNRNFSGIG VIDFERWRPI FRQNWGNMKI YKNFSIDLVR KEHPFWNKKM IELEASKRFE
     KYARLFMEET LKLAKKTRKQ ADWGYYGYPY CFNMSPTNFV PDCDVTARDE NNEMSWLFNN
     QNVLLPSVYI RRELTPDQRI GLVQGRVKEA VRISNKLKHS PKVFSYWWYV YQDETNTFLT
     ETDVKKTFQE IVINGGDGII IWGSSSDVNS LSKCTRLREY LLTVLGPIAV NVTEAVN
//