ID   HUGA_TABYA              Reviewed;         349 AA.
AC   E0XKJ9;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Hyaluronidase Tab y 2.0101 {ECO:0000303|PubMed:20608917};
DE            EC=3.2.1.35 {ECO:0000255|RuleBase:RU610713, ECO:0000269|PubMed:20608917};
DE   AltName: Full=Allergen Tab a 2 {ECO:0000303|PubMed:20608917};
DE   AltName: Allergen=Tab y 2.0101 {ECO:0000303|PubMed:20608917};
DE   Flags: Precursor;
OS   Tabanus yao (Horsefly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Tabanomorpha; Tabanoidea;
OC   Tabanidae; Tabanus.
OX   NCBI_TaxID=485572 {ECO:0000312|EMBL:ADM18346.1};
RN   [1] {ECO:0000312|EMBL:ADM18346.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-41; 51-61; 119-131;
RP   195-208; 227-237; 284-294 AND 337-346, FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND ALLERGEN.
RC   TISSUE=Salivary gland {ECO:0000303|PubMed:20608917,
RC   ECO:0000312|EMBL:ADM18346.1};
RX   PubMed=20608917; DOI=10.1111/j.1398-9995.2010.02435.x;
RA   Ma D., Li Y., Dong J., An S., Wang Y., Liu C., Yang X., Yang H., Xu X.,
RA   Lin D., Lai R.;
RT   "Purification and characterization of two new allergens from the salivary
RT   glands of the horsefly, Tabanus yao.";
RL   Allergy 66:101-109(2011).
CC   -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC       small oligosaccharides. {ECO:0000269|PubMed:20608917}.
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:0000255|RuleBase:RU610713,
CC         ECO:0000269|PubMed:20608917};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20608917}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC       {ECO:0000269|PubMed:20608917}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 92% of
CC       the 37 patients tested allergic to horsefly bites. Has some binding
CC       capacity to IgE of patients with V.magnifica wasp sting allergy.
CC       {ECO:0000269|PubMed:20608917}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000255|PIRNR:PIRNR038193, ECO:0000255|RuleBase:RU610713,
CC       ECO:0000305}.
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DR   EMBL; GU321119; ADM18346.1; -; mRNA.
DR   AlphaFoldDB; E0XKJ9; -.
DR   SMR; E0XKJ9; -.
DR   Allergome; 8832; Tab y 2.
DR   Allergome; 9054; Tab y 2.0101.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
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; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:20608917"
FT   CHAIN           26..349
FT                   /note="Hyaluronidase Tab y 2.0101"
FT                   /evidence="ECO:0000305|PubMed:20608917"
FT                   /id="PRO_5003143069"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR038193-1"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        37..328
FT                   /evidence="ECO:0000255|PIRSR:PIRSR038193-3"
FT   DISULFID        205..216
FT                   /evidence="ECO:0000255|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   349 AA;  40318 MW;  6139DB0B3BDA1112 CRC64;
     MKLHQGLVCL SVLILLPTCI LGDRKFEVYW NIPTFMCPDQ NKTIMDLNKK HGVIQNTEDL
     FRGDKISLLY HPGAFPAITR NKTTNTLIYE NGGVPQAGNL SLHLKLLEKD INEQITDKNF
     SGLAVIDFEL WRPIFRQNGG SLSDYQNLSL KLEKDLHPEF NEDQLRKEAE RRIEKFGRSF
     IKQTLIKAKK LRPKAQWGYY AFPYCFNGRR RYVDTCIPSA KIDNDRILYM FENSDVIYPA
     VYLQTDLAQK NQTGLVKGRV DEAVRMAKMV KKPAKPPVLV YHRYVFTDTL EYISKENTTA
     VFKAMKDNGA DGVIIWGSSF DLNSKEKCAK FLDYLREVLW PVIDEVKRS