ID   HYAL_ECHPL              Reviewed;         449 AA.
AC   A3QVN6;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   22-FEB-2023, entry version 49.
DE   RecName: Full=Hyaluronidase;
DE            Short=Hy;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase;
DE   AltName: Full=Venom spreading factor;
DE   Flags: Precursor;
OS   Echis pyramidum leakeyi (Leakey's carpet viper) (Echis carinatus leakeyi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=38415;
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; DQ840253; ABI33941.1; -; mRNA.
DR   AlphaFoldDB; A3QVN6; -.
DR   SMR; A3QVN6; -.
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; 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"
FT                   /id="PRO_0000420457"
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;  52688 MW;  FF069A91DD9CE460 CRC64;
     MYHIWIKFLA AWIFLKRFNG VHVMQAKAPM YRNEPFLVFW NAPTTQCRLR YKVDLDLKTF
     HIVSNANDSL SGSAVTIFYP NHLGVYPHID DRGHFFHGII PQNESLTKHL NKSKSDINRI
     IPLKAFHGLG VIDWENWRPQ WDRNWGSKNV YRNRSIQFAR DLHPELSEDK IRRLAKKEYE
     KAAKSFMRDT LLLAEEMRPD GYWGYYLYPD CQNYDYKTKG DQYTGKCPEI EMSRNDQLLW
     LWRDSTALFP NVYLEIILRS SDNALKFVHH RLKEAMRIAS MAREDYALPV FAYARPFYAY
     TFEPLTQEDL VTTVGETAAM GAAGIVFWGS MQYASTVDSC QKVKKYMNGP LGRYIVNVTT
     AAKICSRVFC RKNGRCVRKH SDSNAFLHLF PESFRIMVYA NATEKKVIVK GKLELENLIY
     LRENFMCQCY QGWKGLYCEE YSIKDIRKI
//