HYAL_ECHOC
ID HYAL_ECHOC Reviewed; 449 AA.
AC A3QVN2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 47.
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 ocellatus (Ocellated saw-scaled viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=99586;
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; DQ840249; ABI33937.1; -; mRNA.
DR AlphaFoldDB; A3QVN2; -.
DR SMR; A3QVN2; -.
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 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_0000420456"
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 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; 52543 MW; 4AA76609010C0660 CRC64;
MYHLWIKCLA AWIFLKRFNG VHVMHAKAPM YPNEPFLVFW NAPTTQCRLR YKVDLDLKTF
HIVANANDTL SGSAVTIFYP THLGIYPHID DRGHFFHGII PQNESLTKHL DKSKSDINRI
IPLKTFHGLG VIDWENWRPQ WDRNWGNKNV YRNRSIQFAR DLHPELSENK IRRLAKAEYE
KAAKSFMRDT LLLAEEMRPD GYWGYYLYPD CQNYDYKTKG DQYTGKCPDI EMSRNDQLLW
LWRESTALFP NVYLEIILRS SDNALKFVHH RLKESMRIAS MAREDYALPV FVYARPFYAY
TFEPLTQEDL VTTVGETAAM GAAGIVFWGS MQYASTVDSC QKVKKYMNGP LGRYIINVTT
AAKICSHALC RKNGRCVRKH SDSNAFLHLF PESFRIMVHA NATEKKVIVK GKLELENLIY
LRENFMCQCY QGWQGLYCEE YSIKDIRKI