ID HUGAA_VESVU Reviewed; 331 AA. AC P49370; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 22-FEB-2023, entry version 98. DE RecName: Full=Hyaluronidase A; DE Short=Hya A; DE EC=3.2.1.35; DE AltName: Full=Allergen Ves v II; DE AltName: Full=Hyaluronoglucosaminidase A; DE AltName: Allergen=Ves v 2a; OS Vespula vulgaris (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=7454; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-13; 205-224 AND RP 260-268. RC TISSUE=Venom, and Venom gland; RX PubMed=8828537; DOI=10.1016/s0091-6749(96)70093-3; RA King T.P., Lu G., Gonzalez M., Qian N., Soldatova L.; RT "Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence RT similarity and antigenic cross-reactivity with their hornet and wasp RT homologs and possible implications for clinical allergy."; RL J. Allergy Clin. Immunol. 98:588-600(1996). RN [2] RP CATALYTIC ACTIVITY. RX PubMed=19896717; DOI=10.1016/j.molimm.2009.10.005; RA Seismann H., Blank S., Braren I., Greunke K., Cifuentes L., Grunwald T., RA Bredehorst R., Ollert M., Spillner E.; RT "Dissecting cross-reactivity in hymenoptera venom allergy by circumvention RT of alpha-1,3-core fucosylation."; RL Mol. Immunol. 47:799-808(2010). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-331, PARTIAL PROTEIN SEQUENCE, RP IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-79; ASN-99 AND RP ASN-127, AND DISULFIDE BONDS. RX PubMed=16699186; DOI=10.1107/s0907444906010687; RA Skov L.K., Seppaelae U., Coen J.J.F., Crickmore N., King T.P., Monsalve R., RA Kastrup J.S., Spangfort M.D., Gajhede M.; RT "Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural RT analysis of an allergenic hyaluronidase from wasp venom."; RL Acta Crystallogr. D 62:595-604(2006). 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|PubMed:19896717}; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. 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; L43562; AAB48073.1; -; mRNA. DR PDB; 2ATM; X-ray; 2.00 A; A=1-331. DR PDBsum; 2ATM; -. DR AlphaFoldDB; P49370; -. DR SMR; P49370; -. DR Allergome; 3521; Ves v 2.0101. DR Allergome; 669; Ves v 2. DR CAZy; GH56; Glycoside Hydrolase Family 56. DR iPTMnet; P49370; -. DR EvolutionaryTrace; P49370; -. 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 3D-structure; Allergen; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Glycosidase; Hydrolase; Secreted. FT CHAIN 1..331 FT /note="Hyaluronidase A" FT /id="PRO_0000191286" FT ACT_SITE 109 FT /note="Proton donor" FT /evidence="ECO:0000305" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16699186" FT CARBOHYD 99 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16699186" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16699186" FT CARBOHYD 325 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 19..308 FT /evidence="ECO:0000269|PubMed:16699186" FT DISULFID 185..197 FT /evidence="ECO:0000269|PubMed:16699186" FT CONFLICT 1 FT /note="S -> T (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 9..13 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 16..22 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 29..32 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 80..94 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 120..123 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 124..136 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 142..171 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 175..180 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 199..206 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 230..250 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 256..265 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 268..272 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 275..287 FT /evidence="ECO:0007829|PDB:2ATM" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 299..302 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 305..317 FT /evidence="ECO:0007829|PDB:2ATM" FT HELIX 319..328 FT /evidence="ECO:0007829|PDB:2ATM" SQ SEQUENCE 331 AA; 38933 MW; F800F7C0F19D6AEC CRC64; SERPKRVFNI YWNVPTFMCH QYDLYFDEVT NFNIKRNSKD DFQGDKIAIF YDPGEFPALL SLKDGKYKKR NGGVPQEGNI TIHLQKFIEN LDKIYPNRNF SGIGVIDFER WRPIFRQNWG NMKIHKNFSI DLVRNEHPTW NKKMIELEAS KRFEKYARFF MEETLKLAKK TRKQADWGYY GYPYCFNMSP NNLVPECDVT AMHENDKMSW LFNNQNVLLP SVYVRQELTP DQRIGLVQGR VKEAVRISNN LKHSPKVLSY WWYVYQDETN TFLTETDVKK TFQEIVINGG DGIIIWGSSS DVNSLSKCKR LQDYLLTVLG PIAINVTEAV N //