ID   HUGA_VESVE              Reviewed;         341 AA.
AC   C0HLL4;
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 A {ECO:0000303|PubMed:31923175};
DE            EC=3.2.1.35 {ECO:0000305|PubMed:31923175};
DE   AltName: Full=Vesp v 2A {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, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND GLYCOSYLATION AT ASN-3.
RC   TISSUE=Venom {ECO:0000303|PubMed:25896434};
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: May hydrolyze high molecular weight hyaluronic acid to
CC       produce small oligosaccharides. {ECO:0000305|PubMed:31923175}.
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}.
CC   -!- CAUTION: Lacks the typical Glu active site in position 113 that is
CC       replaced by an Asn residue. Some catalytic activity was found but in a
CC       fraction that contained both Hyaluronidase A and Hyaluronidase B.
CC       {ECO:0000305|PubMed:31923175}.
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DR   AlphaFoldDB; C0HLL4; -.
DR   SMR; C0HLL4; -.
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..341
FT                   /note="Hyaluronidase A"
FT                   /id="PRO_0000449970"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:31923175"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        23..311
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   DISULFID        189..201
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
SQ   SEQUENCE   341 AA;  40012 MW;  0CC80360D0880C51 CRC64;
     NLNRTNWPKK IFNIYWNVPT YFCHQHDVYF NELTKFDIKY NPKGNYRGDT ISLFYDPGNF
     PAMVPLKNGT YDIRNEGVPQ KGNITVHLQQ FTKELDEIYP KKISGGIGVI NFNKWRPIFR
     RNVNNLKINK EVSIDLVRKE HPKWDKSMIE TEASNRFEKS ARIFMEKTLK LAKDIRNKNK
     WGYHGYPYCP TASTGNPSFD CDALAMNEND KLSWLFKYQD VLLPSVYVKH VLKPEEKIGL
     VRGSVKEAVR ISKKFEHLPK VLSYWWYAYE DKMDTFLTET DVKNTFREIL INGGDGIIIW
     GTMHDLNKEK CEKLKQYLST ILGPIAFKVM EAVKKRTPLN F