HYAL1_MESMA
ID HYAL1_MESMA Reviewed; 410 AA.
AC P86100; D1MBU1; U6BKM8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Hyaluronidase-1 {ECO:0000303|PubMed:18611448};
DE Short=BmHYA1;
DE Short=HYA1 {ECO:0000303|PubMed:18611448};
DE EC=3.2.1.35;
DE AltName: Full=Hyaluronoglucosaminidase-1;
DE AltName: Full=Venom spreading factor;
DE Flags: Precursor;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xue S., Zhao Y., Ma Y., Gui G., Huang C.;
RT "Cloning and molecular characterization of scorpion Buthus martensi venom
RT hyaluronidases: a novel full-length and diversiform no-code stop
RT sequences.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-410.
RX PubMed=20417653; DOI=10.1016/j.toxicon.2010.04.009;
RA Feng L., Gao R., Meng J., Gopalakrishnakone P.;
RT "Cloning and molecular characterization of BmHYA1, a novel hyaluronidase
RT from the venom of Chinese red scorpion Buthus martensi Karsch.";
RL Toxicon 56:474-479(2010).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 26-55, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Venom {ECO:0000269|PubMed:18611448};
RX PubMed=18611448; DOI=10.1016/j.cbpc.2008.06.003;
RA Feng L., Gao R., Gopalakrishnakone P.;
RT "Isolation and characterization of a hyaluronidase from the venom of
RT Chinese red scorpion Buthus martensi.";
RL Comp. Biochem. Physiol. 148C:250-257(2008).
CC -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC small oligosaccharides. In venom, it may participate in the degradation
CC of the extracellular matrix thus allowing a rapid spread of other venom
CC components during the envenomation process.
CC {ECO:0000269|PubMed:18611448}.
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 Evidence={ECO:0000269|PubMed:18611448};
CC -!- ACTIVITY REGULATION: Inhibited by heparin, and to a lesser extent by
CC DTT, Fe(3+) and Cu(2+). Not inhibited by reduced glutathione, L-
CC cysteine, EDTA, Ca(2+) or Mg(2+). {ECO:0000269|PubMed:18611448}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:18611448};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Activity decreases when
CC incubated at temperatures above 24 degrees Celsius for 10 minutes. No
CC activity remains after 10 minutes at 65 degrees Celsius.
CC {ECO:0000269|PubMed:18611448};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18611448}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:18611448}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC {ECO:0000269|PubMed:18611448}.
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DR EMBL; KF588514; AHA36327.1; -; mRNA.
DR EMBL; GU130249; ACY69673.1; -; mRNA.
DR AlphaFoldDB; P86100; -.
DR SMR; P86100; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR PRIDE; P86100; -.
DR BRENDA; 3.2.1.35; 11141.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0033906; F:hyaluronoglucuronidase activity; IDA:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0035821; P:modulation of process of another organism; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000742; EGF-like_dom.
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.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Glycosidase; Hydrolase; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:18611448"
FT CHAIN 26..410
FT /note="Hyaluronidase-1"
FT /id="PRO_0000355081"
FT DOMAIN 352..407
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 48
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 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 199..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 206..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 356..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 361..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 397..406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 48
FT /note="N -> C (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="A -> T (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="W -> G (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="L -> F (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="V -> A (in Ref. 2; ACY69673)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="W -> G (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="E -> G (in Ref. 2; ACY69673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 47433 MW; 4472C474E9E4DF56 CRC64;
MTQNIQMTEM YQIILFASIL AAISATSADF KVVWEVPSIM CSKKFKINVT DLLTSHKILV
NQEETFNGDK IVIFYESQLG KYPHIESHGD INGGMLQVSD LANHLKIARD NISKFIPDPN
FNGVGIIDWE AWRPLWKYNW GRMSEYRDRS KDLVKAKHPD WSPAQIEKVA IEEWENSAKE
WMLKTLKLVE DMRPNAAWCY YLFPDCYNYG GKDQPSEYFC KNDIQEANDK LSWLWKQSTA
LCPSIYMQES HITKYNTSQR AWWIYARLRE TIRLSHPNTL IYPYINYILP GTKKTVPSMD
FKRVLGQIGS LGLDGAIIWG SSYHVNTEEM CKEMKTYVKD VIAPVASTVI QNVNRCSQQI
CKGRGNCVWP EEPYTSWKYL IDPKNPTFKH TNISCKCKGG YTGRYCQIAP
