HUGA_POLAN
ID HUGA_POLAN Reviewed; 367 AA.
AC Q9U6V9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Hyaluronidase;
DE Short=Hya;
DE EC=3.2.1.35;
DE AltName: Full=Hyaluronoglucosaminidase;
DE AltName: Allergen=Pol a 2;
DE Flags: Precursor; Fragment;
OS Polistes annularis (Paper wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Polistinae; Polistini; Polistes.
OX NCBI_TaxID=27505;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA King T.P., Lu G.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in reproduction. {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 -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; AF174528; AAD52616.1; -; mRNA.
DR AlphaFoldDB; Q9U6V9; -.
DR SMR; Q9U6V9; -.
DR Allergome; 3431; Pol a 2.0101.
DR Allergome; 584; Pol a 2.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
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; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Signal;
KW Zymogen.
FT SIGNAL <1..?
FT PROPEP ?..29
FT /id="PRO_0000012107"
FT CHAIN 30..367
FT /note="Hyaluronidase"
FT /id="PRO_0000012108"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..337
FT /evidence="ECO:0000250"
FT DISULFID 214..226
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 367 AA; 43020 MW; 8127056216957562 CRC64;
YVSLSPDSVF NIITDDISHQ ILSRSNCERS KRPKRVFSIY WNVPTFMCHQ YGMNFDEVTD
FNIKHNSKDN FRGETISIYY DPGKFPALMP LKNGNYEERN GGVPQRGNIT IHLQQFNEDL
DKMTPDKNFG GIGVIDFERW KPIFRQNWGN TEIHKKYSIE LVRKEHPKWS ESMIEAEATK
KFEKYARYFM EETLKLAKKT RKRAKWGYYG FPYCYNVTPN NPGPDCDAKA TIENDRLSWM
YNNQEILFPS VYVRHEQKPE ERVYLVQGRI KEAVRISNNL EHSPSVLAYW WYVYQDKMDI
YLSETDVEKT FQEIVTNGGD GIIIWGSSSD VNSLSKCKRL REYLLNTLGP FAVNVTETVN
GRSSLNF