ID   HYAL_CONCN              Reviewed;         448 AA.
AC   I0CME7;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=Hyaluronidase conohyal-Cn1;
DE            Short=Hya;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase;
DE   Flags: Precursor;
OS   Conus consors (Singed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-43 AND 137-154,
RP   CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, VARIANT GLU-78,
RP   AND GLYCOSYLATION AT ASN-141 AND ASN-361.
RC   TISSUE=Venom, and 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.
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:22412800};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- MISCELLANEOUS: Found in both injectable (milked) (IV) and dissected
CC       venom (DV). {ECO:0000305|PubMed:22412800}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR   EMBL; JN697596; AFH78528.1; -; mRNA.
DR   AlphaFoldDB; I0CME7; -.
DR   SMR; I0CME7; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   iPTMnet; I0CME7; -.
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   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00022; EGF_1; 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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..33
FT                   /evidence="ECO:0000269|PubMed:22412800"
FT                   /id="PRO_0000419902"
FT   CHAIN           34..448
FT                   /note="Hyaluronidase conohyal-Cn1"
FT                   /id="PRO_0000419903"
FT   DOMAIN          413..424
FT                   /note="EGF-like"
FT   REGION          26..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        151
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22412800"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22412800"
FT   DISULFID        67..344
FT                   /evidence="ECO:0000250"
FT   DISULFID        369..380
FT                   /evidence="ECO:0000250"
FT   DISULFID        374..413
FT                   /evidence="ECO:0000250"
FT   DISULFID        415..424
FT                   /evidence="ECO:0000250"
FT   VARIANT         78
FT                   /note="D -> E"
FT                   /evidence="ECO:0000269|PubMed:22412800"
SQ   SEQUENCE   448 AA;  51427 MW;  57E4073753DDB803 CRC64;
     MRAVVVVTGL VVVVVATALS LPNHDVKSAT SSRSSSDYQG SSGDDCDEGL PPPDQPFRVV
     WNHPDNCERI KLHLPLDDYG IIFNKLRVFL GEEIQTLYDT GPWPYISETG KFINGGLPQS
     FNHPDNDGET QRILKKHRPE NFTGLGVLDF ETWRAIYSTN FGPMTIYQNE SVKLVKEQHP
     DYDQKKLTKV AEKEWQQAAK DIMSNKLKIA QEVMPRGHWG YYLYPRTWDN KRDTKFRNDK
     INWLWRQSTG LYPSIYIYDF SKTESAITKF VSDTVGEAVR VQKEFSPPNT PIYPYVMFQT
     MDNIFHYEDH LKISLGLSAK MGAAGVVLWG TSKHYKESTR QWQCQQLQEH IRTVLGPLVK
     NVTQMMTDCS RAICEGHGRC VHNSHDVILG ETESQRLSDL CSTRQSRFRD YHCRCYSAWE
     GACCQTLRPS RCQKREQRNV HGGGDLID
//