HYAL_CONPU
ID HYAL_CONPU Reviewed; 458 AA.
AC C0HKM3;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Hyaluronidase conohyal-P1 {ECO:0000303|PubMed:28479398};
DE EC=3.2.1.35 {ECO:0000269|PubMed:28479398};
DE AltName: Full=Hyaluronoglucosaminidase {ECO:0000250|UniProtKB:I0CME7};
DE Flags: Precursor;
OS Conus purpurascens (Purple cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX NCBI_TaxID=41690 {ECO:0000303|PubMed:28479398};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 89-109; 220-228; 330-353
RP AND 418-430, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP GLYCOSYLATION AT ASN-141; ASN-261; ASN-337 AND ASN-359.
RC TISSUE=Venom {ECO:0000303|PubMed:28479398}, and
RC Venom duct {ECO:0000303|PubMed:28479398};
RX PubMed=28479398; DOI=10.1016/j.jprot.2017.05.002;
RA Moeller C., Clark E., Safavi-Hemani H., DeCaprio A., Mari F.;
RT "Isolation and characterization of Conohyal-P1, a hyaluronidase from the
RT injected venom of Conus purpurascens.";
RL J. Proteomics 164:73-84(2017).
CC -!- FUNCTION: Hyaluronidase catalyzes the hydrolysis of hyaluronic acid
CC (HA), an anionic, nonsulfated glycosaminoglycan distributed widely
CC throughout connective, epithelial, and neural tissues
CC (PubMed:28479398). In venom, they are known to enhance diffusion of the
CC venom by degrading the extracellular matrix (Probable).
CC {ECO:0000269|PubMed:28479398, ECO:0000305}.
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:28479398};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28479398}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:28479398}.
CC -!- MASS SPECTROMETRY: Mass=60409.14; Method=MALDI; Note=Glycosylated.;
CC Evidence={ECO:0000269|PubMed:28479398};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; C0HKM3; -.
DR SMR; C0HKM3; -.
DR iPTMnet; C0HKM3; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB.
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; Glycoprotein;
KW Glycosidase; Hydrolase; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:28479398"
FT CHAIN 19..458
FT /note="Hyaluronidase conohyal-P1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440946"
FT DOMAIN 363..434
FT /note="EGF-like"
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT REGION 24..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28479398"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28479398"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28479398"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28479398"
FT DISULFID 68..342
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 367..378
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 372..411
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 413..422
FT /evidence="ECO:0000250|UniProtKB:Q12794"
SQ SEQUENCE 458 AA; 51891 MW; 651670CBDD3C5A1A CRC64;
MRVVVVVTGL VVVVVATALS LPDHDVKSAS SPLSSSSVYQ GSSGDDCDEG LPPPDRPFYV
VWNHPDTCKR NRIPLHLDHY GFIFNKNRLF LGEEIQTLYN TGLWPNISET GEFFNGGLPQ
LFTHHDYSET VEILGRYRTE NFTGLGILDF EEWRAIYDTN FGIMRKYQDE SIKLAKQRYP
SYNKKELTMV AEQEWDQAAR EIMSTKLAIG QALMPGGHWG YYGYPRTWGS KRNTQLRNNR
IDWLWRQSTG LYPSIYIKDP NMTESAIAEF VSGNVEEAVR VQDEFSPPNT PIYPYAMLQS
GDHIFFQVDH LKISLGLPAK MGTSGVILWA SSNRYKNATR QCSRMRVHID NVLGPYVENL
TQVMADCSTT LCGGHGRCVH NSHDVLLGET DSQRLSGLCT PRHSRFRDYH CRCYSDWEGA
CCQTVRPSRC HKQQQGNVHE GGDLQEGHVV NVVNPLIG
