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Database: UniProt
Entry: I0CME8
LinkDB: I0CME8
Original site: I0CME8 
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   05-DEC-2018, entry version 19.
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; 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.,
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 (By similarity). {ECO:0000250}.
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;
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.
CC       {ECO:0000305}.
DR   EMBL; JN697597; AFH78529.1; -; mRNA.
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;
KW   Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   PROPEP       19     33       {ECO:0000250}.
FT                                /FTId=PRO_0000419900.
FT   CHAIN        34   >347       Hyaluronidase conohyal-ad1.
FT                                /FTId=PRO_0000419901.
FT   ACT_SITE    150    150       Proton donor. {ECO:0000250}.
FT   DISULFID     67    343       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   NON_TER     347    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
//
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