ID   HUGA_DOLMA              Reviewed;         331 AA.
AC   P49371;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Hyaluronidase;
DE            Short=Hya;
DE            EC=3.2.1.35;
DE   AltName: Full=Allergen Dol m II;
DE   AltName: Full=Hyaluronoglucosaminidase;
DE   AltName: Allergen=Dol m 2;
OS   Dolichovespula maculata (Bald-faced hornet) (Vespula maculata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Dolichovespula.
OX   NCBI_TaxID=7441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-45.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=7876212; DOI=10.1074/jbc.270.9.4457;
RA   Lu G., Kochoumian L., King T.P.;
RT   "Sequence identity and antigenic cross-reactivity of white face hornet
RT   venom allergen, also a hyaluronidase, with other proteins.";
RL   J. Biol. Chem. 270:4457-4465(1995).
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   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   EMBL; L34548; AAA68279.1; -; mRNA.
DR   PIR; A56090; A56090.
DR   AlphaFoldDB; P49371; -.
DR   SMR; P49371; -.
DR   Allergome; 3273; Dol m 2.0101.
DR   Allergome; 329; Dol m 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; -; 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..331
FT                   /note="Hyaluronidase"
FT                   /id="PRO_0000191285"
FT   ACT_SITE        109
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        19..308
FT                   /evidence="ECO:0000250"
FT   DISULFID        185..197
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  38929 MW;  DD07C11CE7865570 CRC64;
     SERPKRVFNI YWNVPTFMCH QYGLYFDEVT NFNIKHNSKD DFQGDKISIF YDPGEFPALL
     PLKEGNYKIR NGGVPQEGNI TIHLQRFIEN LDKTYPNRNF NGIGVIDFER WRPIFRQNWG
     NMMIHKKFSI DLVRNEHPFW DKKMIELEAS KRFEKYARLF MEETLKLAKK TRKQADWGYY
     GYPYCFNMSP NNLVPDCDAT AMLENDKMSW LFNNQNVLLP SVYIRHELTP DQRVGLVQGR
     VKEAVRISNN LKHSPKVLSY WWYVYQDDTN TFLTETDVKK TFQEIAINGG DGIIIWGSSS
     DVNSLSKCKR LREYLLTVLG PITVNVTETV N