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Database: UniProt
Entry: HUGA_APIME
LinkDB: HUGA_APIME
Original site: 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   08-MAY-2019, entry version 121.
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;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Apoidea; Apidae; 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
RT   mammalian 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
RT   1.";
RL   Anal. Biochem. 285:64-75(2000).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 42-362, AND ACTIVE SITE.
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
CC       produce small oligosaccharides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-
CC         beta-D-glucosamine and D-glucuronate residues in hyaluronate.;
CC         EC=3.2.1.35;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in the venom glands of worker bees.
CC       It is also detected in the testes of drones but not in the queen-
CC       bee venom 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
CC       1,3-monofucosylated or alpha 1,3-(alpha 1,6-)difucosylated at the
CC       innermost GlcNAc residue, approximately 5% of high-mannose type
CC       structures, and 8% contains the terminal trisaccharide GalNAc beta
CC       1-4[Fuc alpha 1-3]GlcNAc beta 1-in beta 1,2-linkage to the core
CC       alpha 1,3-mannosyl residue. {ECO:0000269|PubMed:10998264,
CC       ECO:0000269|PubMed:7795417}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
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   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; -.
DR   iPTMnet; Q08169; -.
DR   UniCarbKB; Q08169; -.
DR   PaxDb; Q08169; -.
DR   PRIDE; Q08169; -.
DR   GeneID; 406146; -.
DR   KEGG; ame:406146; -.
DR   eggNOG; ENOG410IECJ; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   KO; K01197; -.
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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL        1     28       Or 24. {ECO:0000255}.
FT   PROPEP       29     33       {ECO:0000255}.
FT                                /FTId=PRO_0000012105.
FT   CHAIN        34    382       Hyaluronidase.
FT                                /FTId=PRO_0000012106.
FT   ACT_SITE    145    145       Proton donor.
FT                                {ECO:0000305|PubMed:11080624}.
FT   CARBOHYD    115    115       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    263    263       N-linked (GlcNAc...) (complex)
FT                                asparagine.
FT                                {ECO:0000269|PubMed:10998264}.
FT   DISULFID     54    345
FT   DISULFID    221    233
FT   VARIANT     371    371       D -> S (in clone HYA-2).
FT   CONFLICT     37     37       N -> D (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND       44     49       {ECO:0000244|PDB:1FCQ}.
FT   HELIX        51     57       {ECO:0000244|PDB:1FCQ}.
FT   HELIX        63     66       {ECO:0000244|PDB:1FCQ}.
FT   HELIX        74     76       {ECO:0000244|PDB:1FCQ}.
FT   STRAND       78     88       {ECO:0000244|PDB:1FCQ}.
FT   STRAND       94     97       {ECO:0000244|PDB:1FCU}.
FT   STRAND      103    106       {ECO:0000244|PDB:1FCU}.
FT   HELIX       111    113       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       116    130       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      138    143       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       151    153       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       156    158       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       159    172       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       178    207       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      211    216       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      225    227       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      230    232       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       235    242       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       245    248       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      252    255       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      262    264       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       266    286       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      288    290       {ECO:0000244|PDB:2J88}.
FT   STRAND      297    302       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      305    309       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       312    324       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      328    333       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       336    338       {ECO:0000244|PDB:1FCQ}.
FT   STRAND      339    341       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       342    354       {ECO:0000244|PDB:1FCQ}.
FT   HELIX       356    361       {ECO:0000244|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
//
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