ID   HYAL2_TITSE             Reviewed;         403 AA.
AC   W0HFN9;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Hyaluronidase 2;
DE            Short=TsHyal-2;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase;
DE   AltName: Full=Venom spreading factor;
DE   Flags: Precursor;
OS   Tityus serrulatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=6887;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING.
RC   TISSUE=Venom gland;
RX   PubMed=24551256; DOI=10.1371/journal.pntd.0002693;
RA   Horta C.C., Magalhaes B.F., Oliveira-Mendes B.B., do Carmo A.O.,
RA   Duarte C.G., Felicori L.F., Machado-de-Avila R.A., Chavez-Olortegui C.,
RA   Kalapothakis E.;
RT   "Molecular, immunological, and biological characterization of Tityus
RT   serrulatus venom hyaluronidase: new insights into its role in
RT   envenomation.";
RL   PLoS Negl. Trop. Dis. 8:E2693-E2693(2014).
CC   -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC       small oligosaccharides (By similarity). Is an important component of
CC       the venom, since anti-hyaluronidase serum effectively neutralizes the
CC       lethal effet of the venom injected into mice. It may act by increasing
CC       the diffusion of other venom proteins by degrading the extracellular
CC       matrix. {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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KF623284; AHF72516.1; -; mRNA.
DR   AlphaFoldDB; W0HFN9; -.
DR   SMR; W0HFN9; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   BRENDA; 3.2.1.35; 14016.
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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..403
FT                   /note="Hyaluronidase 2"
FT                   /id="PRO_0000429175"
FT   DOMAIN          346..400
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        122
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        39
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        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..325
FT                   /evidence="ECO:0000250"
FT   DISULFID        191..234
FT                   /evidence="ECO:0000250"
FT   DISULFID        198..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        350..361
FT                   /evidence="ECO:0000250"
FT   DISULFID        355..389
FT                   /evidence="ECO:0000250"
FT   DISULFID        391..399
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   403 AA;  46877 MW;  CAC4A5C989731237 CRC64;
     MNPISIFSVV ISVICAVQAE FKVYWEVPSF LCSKRFNINV TQVLTSHKIL VNQGESFNGD
     KIVMFYENQL GKYPYIDSNK VEINGGILQV ADLLKHLKVA KDNITNLVPN PNFNGVGVID
     WESWLPTWDF NWDKMKVYRK KSIDLVKSKH PEWPSHRVEN VAKEEWEKSA KEWMVKTLKL
     AQELRPNAVW CYYSFPDCYN YSRKDEPSPL ACIRKVLVEN DRISWLWKQS TAICPSIHIQ
     ESHITKYSMS QRVWWIDARL REAVRLSMYH RNIPIYPYIN YILPGTNQIV PVMDFKRTLG
     QIASLGLEGA ILWGSSYHLF SESQCKITFD YVKNVIAPTV ATVVLNTNRC SQLICKGRGN
     CIWPAEPFSS WKYLLDPKMP VFKPMKIICK CKHYLGRYCE IPK