ID   HUGAB_VESVU             Reviewed;         340 AA.
AC   Q5D7H4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Inactive hyaluronidase B;
DE            Short=Hya B;
DE   AltName: Full=Hyaluronoglucosaminidase B;
DE   AltName: Allergen=Ves v 2b;
OS   Vespula vulgaris (Yellow jacket) (Wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespula.
OX   NCBI_TaxID=7454;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAX14718.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-15; 53-59; 92-99;
RP   129-136; 228-242; 259-281 AND 320-327, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION AT ASN-66 AND ASN-81.
RC   TISSUE=Venom {ECO:0000269|PubMed:16218950}, and
RC   Venom gland {ECO:0000269|PubMed:16218950};
RX   PubMed=16218950; DOI=10.1111/j.1742-4658.2005.04841.x;
RA   Kolarich D., Leonard R., Hemmer W., Altmann F.;
RT   "The N-glycans of yellow jacket venom hyaluronidases and the protein
RT   sequence of its major isoform in Vespula vulgaris.";
RL   FEBS J. 272:5182-5190(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=19896717; DOI=10.1016/j.molimm.2009.10.005;
RA   Seismann H., Blank S., Braren I., Greunke K., Cifuentes L., Grunwald T.,
RA   Bredehorst R., Ollert M., Spillner E.;
RT   "Dissecting cross-reactivity in hymenoptera venom allergy by circumvention
RT   of alpha-1,3-core fucosylation.";
RL   Mol. Immunol. 47:799-808(2010).
CC   -!- FUNCTION: Has no hyaluronidase activity. {ECO:0000269|PubMed:19896717}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16218950}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:16218950}.
CC   -!- PTM: N-glycosylated on at least two Asn residues by identical
CC       heptasaccharide units composed of Man, GlcNAc, and Fuc residues in the
CC       molar ration of 3:2:2. {ECO:0000269|PubMed:16218950}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000255}.
CC   -!- CAUTION: Lacks the typical Glu active site in position 111 that is
CC       replaced by a His residue, preventing the hyaluronidase activity.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY845866; AAX14718.1; -; mRNA.
DR   EMBL; AJ920395; CAI77218.1; -; mRNA.
DR   AlphaFoldDB; Q5D7H4; -.
DR   SMR; Q5D7H4; -.
DR   Allergome; 3522; Ves v 2.0201.
DR   Allergome; 669; Ves v 2.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   iPTMnet; Q5D7H4; -.
DR   PRIDE; Q5D7H4; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:InterPro.
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   Secreted.
FT   CHAIN           1..340
FT                   /note="Inactive hyaluronidase B"
FT                   /id="PRO_0000271764"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16218950"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16218950"
FT   DISULFID        21..310
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   DISULFID        187..199
FT                   /evidence="ECO:0000250|UniProtKB:Q08169"
FT   CONFLICT        10
FT                   /note="F -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   340 AA;  40072 MW;  9E922056BCFC1CA1 CRC64;
     DRTIWPKKGF SIYWNIPTHF CHNFGVYFKE LKQFNIKYNS MNNFRGETIS LFYDPGNFPS
     MVLLKNGTYE IRNEGVPQKG NLTIHLEQFT KELDEIYPKK IAGGIGVIHF HNWRPIFRRN
     VDNLKINKDI SIDLVRKEHP KWDKSMIEKE ASNRFETSAK IFMEKTLKLA KEIRKKTEWG
     YHGYPHCLSG STDKPSFDCD ALSMSENDKM SWLFNNQNVL LPSIYLKNVL KPDEKIHLVQ
     ERLKEAIRIS KNFKHLPKVL PYWWYTYQDK ESIFLTEADV KNTFKEILTN GADGIIIWGV
     SYELTDRKRC EKLKEYLMKI LGPIAFKVTK AVKENTPLNF