ID   HUGA_POLPI              Reviewed;         288 AA.
AC   P86687;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Hyaluronidase {ECO:0000303|Ref.1, ECO:0000303|Ref.2};
DE            Short=Hya {ECO:0000250|UniProtKB:Q08169};
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase {ECO:0000250|UniProtKB:Q08169};
DE   Flags: Fragment;
OS   Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Polistinae; Epiponini; Polybia.
OX   NCBI_TaxID=291283;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND ALLERGEN.
RC   TISSUE=Venom {ECO:0000269|Ref.1};
RA   Pinto J.R.A.S.;
RT   "Molecular characterization of Hyaluronidase allergen from the venom of the
RT   social wasp Polybia paulista (Hymenoptera, Vespidae).";
RL   Thesis (2008), Sao Paulo State University, Brazil.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom {ECO:0000269|Ref.2};
RA   Pinto J.R.A.S., Santos L.D., Arcuri H.A., Dias N.B., Palma M.S.;
RT   "Structural characterization of hyaluronidase isoforms from the venom of
RT   the social wasp Polybia paulista (Hymenoptera, Vespidae).";
RL   Submitted (JUN-2010) to UniProtKB.
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:0000269|Ref.1};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.1}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000269|Ref.1}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 9.5,
CC       its MW is: 44.1 kDa. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000255}.
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DR   AlphaFoldDB; P86687; -.
DR   SMR; P86687; -.
DR   Allergome; 12007; Poly p 2.0101.
DR   Allergome; 8808; Poly p 2.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB.
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; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   InterPro; IPR001329; Venom_Hyaluronidase.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   PRINTS; PR00847; HYALURONDASE.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Secreted.
FT   CHAIN           <1..>288
FT                   /note="Hyaluronidase"
FT                   /id="PRO_0000396653"
FT   ACT_SITE        66
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        142..154
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   DISULFID        ?..265
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
FT   NON_TER         288
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   288 AA;  33746 MW;  ABFF0679F329016F CRC64;
     GETISIYYDP GKFPALMPLK NGNYEERNGG VPQRGNITIH LQQFNEDLDK MTPDKNFGGI
     GVIDFERWKP IFRQNWGNTE IHKKYSIELV RYEHPKWSES MIEAEATKKF EKYARLFMEE
     TLKLAKKTRK RAKWGYYGFP YCYNYTPNNP GPDCDAKAMI ENDRLSWMYN NQEILFPSVY
     VRHELTPDQR VYLVQGRIKE AVRISNNLKH SPKVLSYWWY VYQDKMDIFL SETDVKKTFQ
     EIVTNGGDGI IIWGSSSDVN SLSKCKRLRE YLLNTLGPFA VNVTETVN