ID   HYAL3_CERCE             Reviewed;         449 AA.
AC   A3QVN4;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   22-FEB-2023, entry version 46.
DE   RecName: Full=Hyaluronidase-3;
DE            Short=Hy-3;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase-3;
DE   AltName: Full=Venom spreading factor;
DE   Flags: Precursor;
OS   Cerastes cerastes (Horned desert viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes.
OX   NCBI_TaxID=8697;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17210232; DOI=10.1016/j.gene.2006.10.026;
RA   Harrison R.A., Ibison F., Wilbraham D., Wagstaff S.C.;
RT   "Identification of cDNAs encoding viper venom hyaluronidases: cross-generic
RT   sequence conservation of full-length and unusually short variant
RT   transcripts.";
RL   Gene 392:22-33(2007).
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 {ECO:0000250}.
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; DQ840251; ABI33939.1; -; mRNA.
DR   AlphaFoldDB; A3QVN4; -.
DR   SMR; A3QVN4; -.
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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF9; HYALURONIDASE; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   2: Evidence at transcript 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-3"
FT                   /id="PRO_0000420459"
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;  52616 MW;  264B073EAB9A535A CRC64;
     MYHIWIKFLA AWIFLKKFNG VHVMQAKAPM YRNEPFLVFW NAPTTQCRLR YKVDLDLKTF
     HIVSNANDSL SGSAVTIFYP NHLGVYPHID DRGHFFHGII PQNESLTKHL NKSKSDINRI
     IPLKAFHGLG VIDWENWRPQ WDRNWGSKNV YRNRSIQFAR DLHPELSEDK IRRLAKKEYE
     KAAKSFMRDT LLLAEEMRPD GYWGYYLYSD CQNYDYKTKG DQYTGKCPEI EMSRNDQLLW
     LWRDSTALFP NVYLEIILRS SDNALKFVHH RLKEAMRIAS MAREDYALPV FAYARPFYAY
     TFEPLTQEDL VTTVGETAAM GAAGIVFWGS MQYASTVDSC QKVKKYMNGP LGRYIVNVTT
     AAKICSRVLC RKNGRCVRKH SDSNAFLHLF PESFRIMVYA NATEKKVIVK GKLELENLIY
     LRENFMCQCY QGWKGLYCEE YSIKDIRKI
//