ID   HYAL1_OLIMR             Reviewed;         410 AA.
AC   P86100; D1MBU1; U6BKM8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   02-SEP-2026, entry version 33.
DE   RecName: Full=Hyaluronidase HYA1 {ECO:0000303|PubMed:18611448};
DE            Short=BmHYA1 {ECO:0000303|PubMed:20417653};
DE            EC=3.2.1.35 {ECO:0000269|PubMed:18611448};
DE   AltName: Full=Hyaluronidase BmHYI {ECO:0000303|PubMed:24973698};
DE   AltName: Full=Hyaluronoglucosaminidase {ECO:0000305};
DE   AltName: Full=Venom spreading factor {ECO:0000303|PubMed:18611448, ECO:0000303|PubMed:24973698, ECO:0000305};
DE   Flags: Precursor;
OS   Olivierus martensii (Manchurian scorpion) (Mesobuthus martensii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Olivierus.
OX   NCBI_TaxID=34649;
RN   [1] {ECO:0000312|EMBL:AHA36327.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=24973698; DOI=10.1016/j.gene.2014.06.045;
RA   Xia X., Liu R., Li Y., Xue S., Liu Q., Jiang X., Zhang W., Ding K.;
RT   "Cloning and molecular characterization of scorpion Buthus martensi venom
RT   hyaluronidases: a novel full-length and diversiform noncoding isoforms.";
RL   Gene 547:338-345(2014).
RN   [2] {ECO:0000312|EMBL:ACY69673.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-410.
RC   TISSUE=Venom gland;
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]
RP   PROTEIN SEQUENCE OF 26-55, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
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: Scorpion venom endo-hyaluronidase that degrades hyaluronic
CC       acid to produce small oligosaccharides. May act as a venom spreading
CC       factor by degrading the extracellular matrix.
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:0000305|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   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; EXP:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0044523; P:venom-mediated disruption of extracellular matrix in another organism; TAS:UniProtKB.
DR   FunFam; 3.20.20.70:FF:000065; Hyaluronidase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF35; 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.
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 HYA1"
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:0000255|PIRSR:PIRSR038193-1"
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:0000250|UniProtKB:Q12794"
FT   DISULFID        199..242
FT                   /evidence="ECO:0000305"
FT   DISULFID        206..220
FT                   /evidence="ECO:0000250|UniProtKB:Q12794"
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
//