ID   HYAL_CRODU              Reviewed;          44 AA.
AC   B3EWP2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Hyaluronidase CdtHya1;
DE            Short=Hya {ECO:0000250|UniProtKB:P86274};
DE            EC=3.2.1.35 {ECO:0000250|UniProtKB:P86274};
DE   AltName: Full=Hyaluronoglucosaminidase {ECO:0000250|UniProtKB:P86274};
DE   AltName: Full=Venom spreading factor;
DE   Flags: Fragment;
OS   Crotalus durissus terrificus (South American rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8732;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   SUBCELLULAR LOCATION, GLYCOSYLATION, AND DISULFIDE BONDS.
RC   TISSUE=Venom {ECO:0000269|Ref.1};
RA   Bordon K.C.F.;
RT   "Functional and structural characterization of hyaluronidase isolated from
RT   Crotalus durissus terrificus snake venom.";
RL   Thesis (2012), University of Sao Paulo, Brazil.
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   SUBCELLULAR LOCATION, GLYCOSYLATION, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=22940594; DOI=10.1016/j.biochi.2012.08.014;
RA   Bordon K.C.F., Perino M.G., Giglio J.R., Arantes E.C.;
RT   "Isolation, enzymatic characterization and antiedematogenic activity of the
RT   first reported rattlesnake hyaluronidase from Crotalus durissus terrificus
RT   venom.";
RL   Biochimie 94:2740-2748(2012).
CC   -!- FUNCTION: Snake venom endo-hyaluronidase that degrades hyaluronan to
CC       smaller oligosaccharide fragments. In venom, it is not toxic by itself,
CC       but increases the diffusion of other venom proteins such as crotoxin (a
CC       neurotoxic and myotoxic PLA2) by degrading the extracellular matrix. In
CC       addition, it displays antiedematogenic activity, since it significantly
CC       diminishes the oedematogenic activity of crotoxin (probably by direct
CC       substrate hydrolysis, since hyaluronan possesses strong water-binding
CC       capacity). {ECO:0000269|PubMed:22940594, ECO:0000269|Ref.1}.
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:0000250|UniProtKB:P86274};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:22940594, ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:22940594, ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22940594, ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22940594,
CC       ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- PTM: Contains disulfide bonds.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:22940594, ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000255}.
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DR   AlphaFoldDB; B3EWP2; -.
DR   SMR; B3EWP2; -.
DR   BRENDA; 3.2.1.35; 1711.
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   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Secreted.
FT   CHAIN           1..>44
FT                   /note="Hyaluronidase CdtHya1"
FT                   /id="PRO_0000419017"
FT   DISULFID        24..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         44
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   44 AA;  5212 MW;  DFD6932D5E3988B0 CRC64;
     MQAKAPMYPN EPFLVFWNAP TTQCRLRYKV DLDLNTFHIV TNAR