ID   HYAL_CROAD              Reviewed;         449 AA.
AC   J3S820;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Hyaluronidase;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase;
DE   AltName: Full=Venom spreading factor;
DE   Flags: Precursor;
OS   Crotalus adamanteus (Eastern diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT   "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT   (Crotalus adamanteus).";
RL   BMC Genomics 13:312-312(2012).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=24231107; DOI=10.1016/j.jprot.2013.11.001;
RA   Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K., Rokyta D.R.;
RT   "Linking the transcriptome and proteome to characterize the venom of the
RT   eastern diamondback rattlesnake (Crotalus adamanteus).";
RL   J. Proteomics 96:145-158(2014).
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 by degrading the
CC       extracellular matrix. In addition, it displays antiedematogenic
CC       activity (By similarity). {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: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   EMBL; JU173662; AFJ49188.1; -; mRNA.
DR   AlphaFoldDB; J3S820; -.
DR   SMR; J3S820; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   PRIDE; J3S820; -.
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   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..449
FT                   /note="Hyaluronidase"
FT                   /id="PRO_0000425658"
FT   DOMAIN          427..438
FT                   /note="EGF-like"
FT   ACT_SITE        135
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..340
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..227
FT                   /evidence="ECO:0000250"
FT   DISULFID        365..376
FT                   /evidence="ECO:0000250"
FT   DISULFID        370..427
FT                   /evidence="ECO:0000250"
FT   DISULFID        429..438
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  52484 MW;  E32733657EA4B5B5 CRC64;
     MYHLWIKCLA AWIFLKRFNG VHVMQAKAPM YPNEPFLVFW NAPTTQCRLR YKVDLDLNTF
     HIVTNANDSL SGSAVTIFYP THLGFYPHID GRGHFFNGII PQNESLAKHL NKSKSDINRM
     IPLRTFHGLG VIDWENWRPQ WDRNWGSKNV YRNRSIQFAR DLHPELSEDE IKRLAKQEYE
     KAAKSFMRDT LLLAEEMRPY GYWGYYLYPD CQNYNYKTKP DQYTGECPDI EITRNNQLLW
     LWRDSTALFP NIYLETVLRS SDNALKFVHH RLKESMRIAS MARKDYALPV FPYARPFYAY
     TFEPLTEEDL VNTVGETAAM GAAGIVFWGS MQYASTVDSC RKVKDYIDGP LGRYIVNVTT
     AAKICSHFLC KKHGRCVRKH SDSNAFLHLF PDSFRILVHG NATEKKVIVK GKLELENLIF
     LINNFMCQCY QGWKGLYCEK HSIKDIRKI