HYAL_LOXIN
ID HYAL_LOXIN Reviewed; 400 AA.
AC R4J7Z9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Hyaluronidase;
DE EC=3.2.1.35;
DE AltName: Full=Chondroitinase;
DE AltName: Full=Dietrich's hyaluronidase;
DE AltName: Full=Hyaluronoglucosaminidase;
DE AltName: Full=Spreading factor;
DE Flags: Precursor;
OS Loxosceles intermedia (Brown spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX NCBI_TaxID=58218;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOASSAY.
RC TISSUE=Venom gland;
RX PubMed=23658852; DOI=10.1371/journal.pntd.0002206;
RA Ferrer V.P., de Mari T.L., Gremski L.H., Trevisan Silva D.,
RA da Silveira R.B., Gremski W., Chaim O.M., Senff-Ribeiro A., Nader H.B.,
RA Veiga S.S.;
RT "A novel hyaluronidase from brown spider (Loxosceles intermedia) venom
RT (Dietrich's Hyaluronidase): from cloning to functional characterization.";
RL PLoS Negl. Trop. Dis. 7:E2206-E2206(2013).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=17210169; DOI=10.1016/j.toxicon.2006.11.024;
RA da Silveira R.B., Chaim O.M., Mangili O.C., Gremski W., Dietrich C.P.,
RA Nader H.B., Veiga S.S.;
RT "Hyaluronidases in Loxosceles intermedia (Brown spider) venom are endo-
RT beta-N-acetyl-d-hexosaminidases hydrolases.";
RL Toxicon 49:758-768(2007).
CC -!- FUNCTION: Spider venom endo-hyaluronidase that is able to degrade
CC purified hyaluronic acid (HA) and chondroitin sulfate (CS). Has no
CC activity on dermatan sulfate (DS) and heparan sulfate (HS). Also
CC increases the dermonecrotic effect of the dermonecrotic toxin (AC
CC P0CE80), when injected in rabbit skin, supporting the hypothesis that
CC venom hyaluronidases are spreading factors.
CC {ECO:0000269|PubMed:17210169, ECO:0000269|PubMed:23658852}.
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:0000269|PubMed:17210169}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17210169}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; JX402631; AGH25912.1; -; mRNA.
DR AlphaFoldDB; R4J7Z9; -.
DR SMR; R4J7Z9; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR ArachnoServer; AS001899; Hyaluronidase-1-Loxosceles intermedia.
DR BRENDA; 3.2.1.35; 8287.
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; 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.
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..400
FT /note="Hyaluronidase"
FT /id="PRO_0000425845"
FT DOMAIN 340..396
FT /note="EGF-like"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..319
FT /evidence="ECO:0000250"
FT DISULFID 196..209
FT /evidence="ECO:0000250"
FT DISULFID 344..355
FT /evidence="ECO:0000250"
FT DISULFID 349..384
FT /evidence="ECO:0000250"
FT DISULFID 386..395
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 46198 MW; 5B9A3C3DE19350F4 CRC64;
MQTILVLTTF LSAWFLAVGF DVFWNVPSQQ CKKYGMKFVP LLEQYSILVN KEDNFKGDKI
TIFYESQLGL YPHIGANDES FNGGIPQLGD LKAHLEKSAV DIRRDILDKS ATGLRIIDWE
AWRPIWEFNW SSLRKYQDKM KKVVRQFNPT AHESTVAKLA HNEWENSSKS WMLSTLQLGK
QLRPNSVWCY YLFPDCYNYD GNSVQEFQCS EAIRKGNDRL KWLWEESTAV CPSIYIKEGQ
LTNYTLQKRI WFTNGRLQEA LRVAQPKARI YPYINYSIKP GMMVPEVEFW RLIAQIASLG
MDGAVIWGSS ASVGSKNHCA QLMKYIADVL GPATLRIKEN VARCSKQACS GRGRCTWPKD
TSVIAWKFLV EKEDYDFYLG DIECKCVEGY EGRYCEQKTK
