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Database: UniProt
Entry: I0CME7
LinkDB: I0CME7
Original site: I0CME7 
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   05-DEC-2018, entry version 21.
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; 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
RP   GLU-78, 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.,
RA   Dutertre S., Noguier F., Ducancel F., Stocklin R., Krizaj I.,
RA   Favreau P.;
RT   "Recruitment of glycosyl hydrolase proteins in a cone snail venomous
RT   arsenal: further insights into biomolecular features of Conus
RT   venoms.";
RL   Mar. Drugs 10:258-280(2012).
CC   -!- FUNCTION: Hyaluronidase catalyzes the hydrolysis of hyaluronic
CC       acid (HA), an anionic, nonsulfated glycosaminoglycan distributed
CC       widely throughout connective, epithelial, and neural tissues. In
CC       venom, they are known to enhance diffusion of the venom by
CC       degrading the extracellular matrix.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-
CC         beta-D-glucosamine and D-glucuronate residues in hyaluronate.;
CC         EC=3.2.1.35; 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
CC       dissected venom (DV). {ECO:0000305|PubMed:22412800}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
DR   EMBL; JN697596; AFH78528.1; -; mRNA.
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; -; 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   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00022; EGF_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   PROPEP       19     33       {ECO:0000269|PubMed:22412800}.
FT                                /FTId=PRO_0000419902.
FT   CHAIN        34    448       Hyaluronidase conohyal-Cn1.
FT                                /FTId=PRO_0000419903.
FT   DOMAIN      413    424       EGF-like.
FT   ACT_SITE    151    151       Proton donor. {ECO:0000250}.
FT   CARBOHYD    141    141       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:22412800}.
FT   CARBOHYD    169    169       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000305}.
FT   CARBOHYD    361    361       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:22412800}.
FT   DISULFID     67    344       {ECO:0000250}.
FT   DISULFID    369    380       {ECO:0000250}.
FT   DISULFID    374    413       {ECO:0000250}.
FT   DISULFID    415    424       {ECO:0000250}.
FT   VARIANT      78     78       D -> E. {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
//
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