ID HUGA_POLAN Reviewed; 367 AA. AC Q9U6V9; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 22-FEB-2023, entry version 77. DE RecName: Full=Hyaluronidase; DE Short=Hya; DE EC=3.2.1.35; DE AltName: Full=Hyaluronoglucosaminidase; DE AltName: Allergen=Pol a 2; DE Flags: Precursor; Fragment; OS Polistes annularis (Paper wasp). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea; OC Vespidae; Polistinae; Polistini; Polistes. OX NCBI_TaxID=27505; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA King T.P., Lu G.; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May play a role in reproduction. {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 -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF174528; AAD52616.1; -; mRNA. DR AlphaFoldDB; Q9U6V9; -. DR SMR; Q9U6V9; -. DR Allergome; 3431; Pol a 2.0101. DR Allergome; 584; Pol a 2. DR CAZy; GH56; Glycoside Hydrolase Family 56. 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; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Signal; KW Zymogen. FT SIGNAL <1..? FT PROPEP ?..29 FT /id="PRO_0000012107" FT CHAIN 30..367 FT /note="Hyaluronidase" FT /id="PRO_0000012108" FT ACT_SITE 138 FT /note="Proton donor" FT /evidence="ECO:0000250" FT CARBOHYD 108 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 354 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 48..337 FT /evidence="ECO:0000250" FT DISULFID 214..226 FT /evidence="ECO:0000250" FT NON_TER 1 SQ SEQUENCE 367 AA; 43020 MW; 8127056216957562 CRC64; YVSLSPDSVF NIITDDISHQ ILSRSNCERS KRPKRVFSIY WNVPTFMCHQ YGMNFDEVTD FNIKHNSKDN FRGETISIYY DPGKFPALMP LKNGNYEERN GGVPQRGNIT IHLQQFNEDL DKMTPDKNFG GIGVIDFERW KPIFRQNWGN TEIHKKYSIE LVRKEHPKWS ESMIEAEATK KFEKYARYFM EETLKLAKKT RKRAKWGYYG FPYCYNVTPN NPGPDCDAKA TIENDRLSWM YNNQEILFPS VYVRHEQKPE ERVYLVQGRI KEAVRISNNL EHSPSVLAYW WYVYQDKMDI YLSETDVEKT FQEIVTNGGD GIIIWGSSSD VNSLSKCKRL REYLLNTLGP FAVNVTETVN GRSSLNF //