ID   HYAL1_TITSE             Reviewed;         385 AA.
AC   P85841; W0HJY6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=Hyaluronidase 1;
DE            Short=TsHyal-1;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase;
DE   AltName: Full=Venom spreading factor;
DE   Flags: Precursor; Fragment;
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).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-35, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   VARIANT GLN-2.
RC   TISSUE=Venom {ECO:0000269|Ref.2};
RA   Richardson M., Borges M.H., Cordeiro M.N., Pimenta A.M.C., de Lima M.E.,
RA   Rates B.;
RT   "Hyaluronidase from venom of Brazilian scorpion Tityus serrulatus.";
RL   Submitted (MAY-2008) to UniProtKB.
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:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000255}.
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DR   EMBL; KF623285; AHF72517.1; -; mRNA.
DR   AlphaFoldDB; P85841; -.
DR   SMR; P85841; -.
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; 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: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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          <1..1
FT   CHAIN           2..385
FT                   /note="Hyaluronidase 1"
FT                   /id="PRO_0000343459"
FT   DOMAIN          328..382
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        14..307
FT                   /evidence="ECO:0000250"
FT   DISULFID        173..216
FT                   /evidence="ECO:0000250"
FT   DISULFID        180..194
FT                   /evidence="ECO:0000250"
FT   DISULFID        332..343
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        373..381
FT                   /evidence="ECO:0000250"
FT   VARIANT         2
FT                   /note="D -> Q"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CONFLICT        2
FT                   /note="D -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="N -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   385 AA;  44618 MW;  E0D2D508C5C3C35B CRC64;
     ADFKVYWEVP SFLCSKRFKI NVTEVLTSHE ILVNQGESFN GDKIVIFYEN QLGKYPHIDS
     NNVEINGGIL QVADLAKHLK VAKDNITKFV PNPNFNGVGV IDWEAWRPSW EFNWGKLKVY
     KEKSIDLVKS KHPEWPSDRV EKVAKEEWEE SAKEWMVKTL KLAQEMRPNA VWCYYLFPDC
     YNYFGKDQPS QFSCSSRIQK ENSRLSWLWN QSTAICLSIY IQESHVTKYN MSQRTWWIDA
     RLREAIRVSE HRPNIPIYPY INYILPGTNQ TVPAMDFKRT LGQIASLGLD GALLWGSSYH
     VLTESQCKIT SDYVKSVIAP TVATVVLNTN RCSQIICKGR GNCVWPEEPF SSWKYLVDPK
     MPVFKPTNIH CKCKGYLGRY CEIPK
//