ID   HUGAB_VESVE             Reviewed;         331 AA.
AC   C0HLL5;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Hyaluronidase B {ECO:0000303|PubMed:31923175};
DE            EC=3.2.1.35 {ECO:0000305|PubMed:31923175};
DE   AltName: Full=Vesp v 2B {ECO:0000303|PubMed:31923175};
OS   Vespa velutina (Asian yellow-legged hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=202808;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland {ECO:0000303|PubMed:25896434};
RX   PubMed=25896434; DOI=10.1038/srep09454;
RA   Liu Z., Chen S., Zhou Y., Xie C., Zhu B., Zhu H., Liu S., Wang W., Chen H.,
RA   Ji Y.;
RT   "Deciphering the venomic transcriptome of killer-wasp Vespa velutina.";
RL   Sci. Rep. 5:9454-9454(2015).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-10, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:31923175};
RX   PubMed=31923175; DOI=10.1371/journal.pone.0225672;
RA   Monsalve R.I., Gutierrez R., Hoof I., Lombardero M.;
RT   "Purification and molecular characterization of phospholipase, antigen 5
RT   and hyaluronidases from the venom of the Asian hornet (Vespa velutina).";
RL   PLoS ONE 15:E0225672-E0225672(2020).
CC   -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC       small oligosaccharides. {ECO:0000250|UniProtKB:E0XKJ9}.
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:0000305|PubMed:31923175};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31923175}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31923175}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLL5; -.
DR   SMR; C0HLL5; -.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Secreted.
FT   CHAIN           1..331
FT                   /note="Hyaluronidase B"
FT                   /id="PRO_0000449971"
FT   ACT_SITE        109
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        19..308
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   DISULFID        185..197
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
SQ   SEQUENCE   331 AA;  39110 MW;  D0AFADC079BDEF7E CRC64;
     SERPKRVFNI YWNVPTFMCH QYGLYFDEVT NFNIKHNSKD NFQGDKIAIF YDPGEFPALL
     PLKYGKYKIR NGGVPQEGNI TIHLQRFIEH LDKTYPNRNF SGIGVIDFER WRPIFRQNWG
     NMKIYKNFSI DLVRKEHPFW NKKMIELEAS KRFEKYARLF MEETLKLAKK TRKQADWGYY
     GYPYCFNMSP TNFVPDCDVT AMRENDEMSW LFNNQNVLLP SVYVRRELTP DQRIGLVQGR
     VKEAVRISNN LKHSPKVFSY WWYVYQDETN TFLTETDVKK TFQEIVINGG DGIIIWGSSS
     DVNSLSKCMR LREYLLTVLG PIAVNVTEAV N