ID   HYAL_TITST              Reviewed;          24 AA.
AC   P0C8X3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   11-DEC-2019, entry version 15.
DE   RecName: Full=Hyaluronidase;
DE            EC=3.2.1.35;
DE   AltName: Full=Cysteine-rich venom protein;
DE            Short=CRVP;
DE   AltName: Full=Hyaluronoglucosaminidase A;
DE   Flags: Fragment;
OS   Tityus stigmurus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=50344;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17270501; DOI=10.1016/j.cbpc.2006.12.004;
RA   Batista C.V.F., Roman-Gonzalez S.A., Salas-Castillo S.P., Zamudio F.Z.,
RA   Gomez-Lagunas F., Possani L.D.;
RT   "Proteomic analysis of the venom from the scorpion Tityus stigmurus:
RT   biochemical and physiological comparison with other Tityus species.";
RL   Comp. Biochem. Physiol. 146C:147-157(2007).
CC   -!- FUNCTION: Possesses high activity against hyaluronan in vitro.
CC       {ECO:0000269|PubMed:17270501}.
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=44800.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17270501};
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Secreted.
FT   PEPTIDE         1..>24
FT                   /note="Hyaluronidase"
FT                   /id="PRO_0000366111"
FT   NON_TER         24
SQ   SEQUENCE   24 AA;  2966 MW;  EEC76D5D0426A345 CRC64;
     EHPALYRRYS KEHTFCKTKN QXCN