HUGA_APIME
ID HUGA_APIME Reviewed; 382 AA.
AC Q08169;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Hyaluronidase;
DE Short=Hya;
DE EC=3.2.1.35;
DE AltName: Full=Allergen Api m II;
DE AltName: Full=Hyaluronoglucosaminidase;
DE AltName: Allergen=Api m 2;
DE Flags: Precursor;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=7682712; DOI=10.1073/pnas.90.8.3569;
RA Gmachl M., Kreil G.;
RT "Bee venom hyaluronidase is homologous to a membrane protein of mammalian
RT sperm.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3569-3573(1993).
RN [2]
RP PROTEIN SEQUENCE OF 34-64.
RC TISSUE=Venom;
RA Jacobson R.S., Hoffman D.R., Kemeny D.M.;
RT "The cross-reactivity between bee and vespid hyaluronidases has a
RT structural basis.";
RL J. Allergy Clin. Immunol. 89:292-292(1991).
RN [3]
RP GLYCOSYLATION.
RX PubMed=7795417; DOI=10.1007/bf00731872;
RA Kubelka V., Altmann F., Marz L.;
RT "The asparagine-linked carbohydrate of honeybee venom hyaluronidase.";
RL Glycoconj. J. 12:77-83(1995).
RN [4]
RP GLYCOSYLATION AT ASN-263.
RX PubMed=10998264; DOI=10.1006/abio.2000.4737;
RA Kolarich D., Altmann F.;
RT "N-glycan analysis by matrix-assisted laser desorption/ionization mass
RT spectrometry of electrophoretically separated nonmammalian proteins:
RT application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1.";
RL Anal. Biochem. 285:64-75(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 42-362, ACTIVE SITE, AND DISULFIDE
RP BONDS.
RX PubMed=11080624; DOI=10.1016/s0969-2126(00)00511-6;
RA Markovic-Housley Z., Miglierini G., Soldatova L., Rizkallah P.J.,
RA Mueller U., Schirmer T.;
RT "Crystal structure of hyaluronidase, a major allergen of bee venom.";
RL Structure 8:1025-1035(2000).
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 -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in the venom glands of worker bees. It is
CC also detected in the testes of drones but not in the queen-bee venom
CC glands or in pupae.
CC -!- PTM: N-glycosylated. Glycans found include a majority of small
CC oligosaccharides (Man1-3GlcNAc2), most of which are either alpha 1,3-
CC monofucosylated or alpha 1,3-(alpha 1,6-)difucosylated at the innermost
CC GlcNAc residue, approximately 5% of high-mannose type structures, and
CC 8% contains the terminal trisaccharide GalNAc beta 1-4[Fuc alpha 1-
CC 3]GlcNAc beta 1-in beta 1,2-linkage to the core alpha 1,3-mannosyl
CC residue. {ECO:0000269|PubMed:10998264, ECO:0000269|PubMed:7795417}.
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; L10710; AAA27730.1; -; mRNA.
DR PIR; A47477; A47477.
DR RefSeq; NP_001011619.1; NM_001011619.1.
DR PDB; 1FCQ; X-ray; 1.60 A; A=33-382.
DR PDB; 1FCU; X-ray; 2.10 A; A=33-382.
DR PDB; 1FCV; X-ray; 2.65 A; A=33-382.
DR PDB; 2J88; X-ray; 2.60 A; A=33-382.
DR PDBsum; 1FCQ; -.
DR PDBsum; 1FCU; -.
DR PDBsum; 1FCV; -.
DR PDBsum; 2J88; -.
DR AlphaFoldDB; Q08169; -.
DR SMR; Q08169; -.
DR STRING; 7460.GB52775-PA; -.
DR Allergome; 2493; Api m A1-A2.
DR Allergome; 2778; Api m A1-A2-A3.
DR Allergome; 3089; Api m 2.0101.
DR Allergome; 46; Api m 2.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyConnect; 224; 17 N-Linked glycans.
DR iPTMnet; Q08169; -.
DR PaxDb; Q08169; -.
DR ABCD; Q08169; 1 sequenced antibody.
DR EnsemblMetazoa; NM_001011619; NP_001011619; LOC406146.
DR GeneID; 406146; -.
DR KEGG; ame:406146; -.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR PhylomeDB; Q08169; -.
DR BRENDA; 3.2.1.35; 387.
DR EvolutionaryTrace; Q08169; -.
DR Proteomes; UP000005203; Unplaced.
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; Reference proteome; Secreted; Signal;
KW Zymogen.
FT SIGNAL 1..28
FT /note="Or 24"
FT /evidence="ECO:0000255"
FT PROPEP 29..33
FT /evidence="ECO:0000255"
FT /id="PRO_0000012105"
FT CHAIN 34..382
FT /note="Hyaluronidase"
FT /id="PRO_0000012106"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:11080624"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:10998264"
FT DISULFID 54..345
FT /evidence="ECO:0000269|PubMed:11080624"
FT DISULFID 221..233
FT /evidence="ECO:0000269|PubMed:11080624"
FT VARIANT 371
FT /note="D -> S (in clone HYA-2)"
FT CONFLICT 37
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1FCU"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1FCU"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 178..207
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 266..286
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2J88"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:1FCQ"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:1FCQ"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:1FCQ"
SQ SEQUENCE 382 AA; 44260 MW; 3E6822E95CA11856 CRC64;
MSRPLVITEG MMIGVLLMLA PINALLLGFV QSTPDNNKTV REFNVYWNVP TFMCHKYGLR
FEEVSEKYGI LQNWMDKFRG EEIAILYDPG MFPALLKDPN GNVVARNGGV PQLGNLTKHL
QVFRDHLINQ IPDKSFPGVG VIDFESWRPI FRQNWASLQP YKKLSVEVVR REHPFWDDQR
VEQEAKRRFE KYGQLFMEET LKAAKRMRPA ANWGYYAYPY CYNLTPNQPS AQCEATTMQE
NDKMSWLFES EDVLLPSVYL RWNLTSGERV GLVGGRVKEA LRIARQMTTS RKKVLPYYWY
KYQDRRDTDL SRADLEATLR KITDLGADGF IIWGSSDDIN TKAKCLQFRE YLNNELGPAV
KRIALNNNAN DRLTVDVSVD QV
