ID HUGA_VESMC Reviewed; 31 AA. AC P0CH89; DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 1. DT 25-MAY-2022, entry version 23. DE RecName: Full=Hyaluronidase; DE Short=Hya; DE EC=3.2.1.35; DE AltName: Full=Hyaluronoglucosaminidase; DE AltName: Allergen=Ves m 2; DE Flags: Fragment; OS Vespula maculifrons (Eastern yellow jacket) (Wasp). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea; OC Vespidae; Vespinae; Vespula. OX NCBI_TaxID=7453; RN [1] RP PROTEIN SEQUENCE. RA Jacobson R.S., Hoffman D.R., Kemeny D.M.; RT "The cross-reactivity between bee and vespid hyaluronidases has a RT structural basis."; RL J. Allergy Clin. Immunol. 89:292-292(1992). 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 -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- PTM: Contains 2 disulfide bonds. {ECO:0000250}. CC -!- PTM: N-glycosylated on at least two Asn residues by identical CC heptasaccharide units composed of Man, GlcNAc, and Fuc residues in the CC molar ration of 3:2:2. {ECO:0000250}. 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 AlphaFoldDB; P0CH89; -. DR Allergome; 3515; Ves m 2.0101. DR Allergome; 662; Ves m 2. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Glycosidase; Hydrolase; Secreted. FT CHAIN 1..>31 FT /note="Hyaluronidase" FT /id="PRO_0000401923" FT NON_TER 31 SQ SEQUENCE 31 AA; 3848 MW; FFF02ACAEF547B89 CRC64; DRCIWPKEGF SIYWNIPTHF CHNFGVYFKE L //