HUGAA_VESVU
ID HUGAA_VESVU Reviewed; 331 AA.
AC P49370;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Hyaluronidase A;
DE Short=Hya A;
DE EC=3.2.1.35;
DE AltName: Full=Allergen Ves v II;
DE AltName: Full=Hyaluronoglucosaminidase A;
DE AltName: Allergen=Ves v 2a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-13; 205-224 AND
RP 260-268.
RC TISSUE=Venom, and Venom gland;
RX PubMed=8828537; DOI=10.1016/s0091-6749(96)70093-3;
RA King T.P., Lu G., Gonzalez M., Qian N., Soldatova L.;
RT "Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence
RT similarity and antigenic cross-reactivity with their hornet and wasp
RT homologs and possible implications for clinical allergy.";
RL J. Allergy Clin. Immunol. 98:588-600(1996).
RN [2]
RP CATALYTIC ACTIVITY.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-331, PARTIAL PROTEIN SEQUENCE,
RP IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-79; ASN-99 AND
RP ASN-127, AND DISULFIDE BONDS.
RX PubMed=16699186; DOI=10.1107/s0907444906010687;
RA Skov L.K., Seppaelae U., Coen J.J.F., Crickmore N., King T.P., Monsalve R.,
RA Kastrup J.S., Spangfort M.D., Gajhede M.;
RT "Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural
RT analysis of an allergenic hyaluronidase from wasp venom.";
RL Acta Crystallogr. D 62:595-604(2006).
CC -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC small oligosaccharides. {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 Evidence={ECO:0000269|PubMed:19896717};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {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; L43562; AAB48073.1; -; mRNA.
DR PDB; 2ATM; X-ray; 2.00 A; A=1-331.
DR PDBsum; 2ATM; -.
DR AlphaFoldDB; P49370; -.
DR SMR; P49370; -.
DR Allergome; 3521; Ves v 2.0101.
DR Allergome; 669; Ves v 2.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR iPTMnet; P49370; -.
DR EvolutionaryTrace; P49370; -.
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 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Secreted.
FT CHAIN 1..331
FT /note="Hyaluronidase A"
FT /id="PRO_0000191286"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16699186"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16699186"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16699186"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 19..308
FT /evidence="ECO:0000269|PubMed:16699186"
FT DISULFID 185..197
FT /evidence="ECO:0000269|PubMed:16699186"
FT CONFLICT 1
FT /note="S -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 142..171
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 230..250
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:2ATM"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 305..317
FT /evidence="ECO:0007829|PDB:2ATM"
FT HELIX 319..328
FT /evidence="ECO:0007829|PDB:2ATM"
SQ SEQUENCE 331 AA; 38933 MW; F800F7C0F19D6AEC CRC64;
SERPKRVFNI YWNVPTFMCH QYDLYFDEVT NFNIKRNSKD DFQGDKIAIF YDPGEFPALL
SLKDGKYKKR NGGVPQEGNI TIHLQKFIEN LDKIYPNRNF SGIGVIDFER WRPIFRQNWG
NMKIHKNFSI DLVRNEHPTW NKKMIELEAS KRFEKYARFF MEETLKLAKK TRKQADWGYY
GYPYCFNMSP NNLVPECDVT AMHENDKMSW LFNNQNVLLP SVYVRQELTP DQRIGLVQGR
VKEAVRISNN LKHSPKVLSY WWYVYQDETN TFLTETDVKK TFQEIVINGG DGIIIWGSSS
DVNSLSKCKR LQDYLLTVLG PIAINVTEAV N
