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
//
