GenomeNet

Database: UniProt
Entry: J3S820
LinkDB: J3S820
Original site: J3S820 
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   05-DEC-2018, entry version 21.
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;
OC   Toxicofera; 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.,
RA   Rokyta D.R.;
RT   "Linking the transcriptome and proteome to characterize the venom of
RT   the eastern diamondback rattlesnake (Crotalus adamanteus).";
RL   J. Proteomics 96:145-158(2014).
CC   -!- FUNCTION: Snake venom endo-hyaluronidase that degrades hyaluronan
CC       to smaller oligosaccharide fragments. In venom, it is not toxic by
CC       itself, but increases the diffusion of other venom proteins by
CC       degrading the extracellular matrix. In addition, it displays
CC       antiedematogenic activity (By similarity). {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: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
DR   EMBL; JU173662; AFJ49188.1; -; mRNA.
DR   SMR; J3S820; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
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       {ECO:0000250}.
FT   CHAIN        24    449       Hyaluronidase.
FT                                /FTId=PRO_0000425658.
FT   DOMAIN      427    438       EGF-like.
FT   ACT_SITE    135    135       Proton donor. {ECO:0000250}.
FT   CARBOHYD     67     67       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    357    357       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     47    340       {ECO:0000250}.
FT   DISULFID    211    227       {ECO:0000250}.
FT   DISULFID    365    376       {ECO:0000250}.
FT   DISULFID    370    427       {ECO:0000250}.
FT   DISULFID    429    438       {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
//
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