ID   HYAL_CONAQ              Reviewed;         347 AA.
AC   I0CME8;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Hyaluronidase conohyal-ad1;
DE            Short=Hya;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase;
DE   Flags: Precursor; Fragment;
OS   Conus adamsonii (Cone snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Textilia.
OX   NCBI_TaxID=1173533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=22412800; DOI=10.3390/md10020258;
RA   Violette A., Leonardi A., Piquemal D., Terrat Y., Biass D., Dutertre S.,
RA   Noguier F., Ducancel F., Stocklin R., Krizaj I., Favreau P.;
RT   "Recruitment of glycosyl hydrolase proteins in a cone snail venomous
RT   arsenal: further insights into biomolecular features of Conus venoms.";
RL   Mar. Drugs 10:258-280(2012).
CC   -!- FUNCTION: Hyaluronidase catalyzes the hydrolysis of hyaluronic acid
CC       (HA), an anionic, nonsulfated glycosaminoglycan distributed widely
CC       throughout connective, epithelial, and neural tissues. In venom, they
CC       are known to enhance diffusion of the venom by degrading the
CC       extracellular matrix (By similarity). {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 duct.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000250}.
CC   -!- PTM: Is N-linked glycosylated at three positions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   EMBL; JN697597; AFH78529.1; -; mRNA.
DR   AlphaFoldDB; I0CME8; -.
DR   SMR; I0CME8; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   ConoServer; 5536; conohyal-ad1 precursor.
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; Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..33
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000419900"
FT   CHAIN           34..>347
FT                   /note="Hyaluronidase conohyal-ad1"
FT                   /id="PRO_0000419901"
FT   REGION          27..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        150
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..343
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   NON_TER         347
SQ   SEQUENCE   347 AA;  39582 MW;  A114DF88E0043228 CRC64;
     MRAVVVVTGL VVVVVTTTLS LQDHDVKSAS SPLSSSVDQG SSGDDCDEGL PPPDQPFRVV
     WNHPDNCEKI NLHLPLDEYG IIFNKRRVFL GEEIQTLYDT GPWPYINKTG CFINGGLPQL
     FNQPDNSETC KILGKNRIED FTGLGVLDFE TWRAIYSTNF GTMENYQIES VNLVRKRHPD
     YSEKELKMVA EQEWQEAARK IMTDKLAAGQ SLMPRGYWGY YLYPRTWDSK PDTKFRNNKI
     DWLWRQSTGL YPSIYIYYDV VSKTDSVITK FVSDTVGEAV RVQNDFSPPN TPIYPYVMFQ
     TMDNVFHKED HMKISLGLSA KMGAAGVILW GSSQNYKDFT TQCSRLQ