ID HYAL_PHOKE Reviewed; 32 AA. AC P86274; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 07-OCT-2020, entry version 20. DE RecName: Full=Hyaluronidase-Pk1a {ECO:0000250|UniProtKB:Q08169}; DE Short=Hya {ECO:0000303|Ref.1}; DE EC=3.2.1.35; DE AltName: Full=Hyaluronoglucosaminidase {ECO:0000250|UniProtKB:Q08169}; DE Flags: Fragment; OS Phoneutria keyserlingi (Brazilian wandering spider) (Ctenus keyserlingii). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae; OC Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Phoneutria. OX NCBI_TaxID=272754; RN [1] RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Venom {ECO:0000269|Ref.1}; RA Richardson M., Borges M.H., Souza I.A., Cordeiro M.N.; RT "Hyaluronidase enzyme in venom of spider P.keyserlinigi (wandering)."; RL Submitted (APR-2009) to UniProtKB. 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|Ref.1}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.1}. CC -!- MISCELLANEOUS: On the 2D-gel the MW of this protein is: 37 kDa. CC {ECO:0000269|Ref.1}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000255}. 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 ArachnoServer; AS001206; Hyaluronidase-Pk1a (fragment). DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Secreted. FT CHAIN 1..>32 FT /note="Hyaluronidase-Pk1a" FT /id="PRO_0000376024" FT CARBOHYD 23 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 12..? FT /evidence="ECO:0000250|UniProtKB:Q08169" FT NON_TER 32 FT /evidence="ECO:0000303|Ref.1" SQ SEQUENCE 32 AA; 3879 MW; 6CC71A1D7F06AB76 CRC64; FEVYWNVPTL QCRAVYKMIF KLNRTYGIQX NA //