ID A0A3P8XRN6_ESOLU Unreviewed; 472 AA.
AC A0A3P8XRN6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN Name=HYAL2 {ECO:0000313|Ensembl:ENSELUP00000005933.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000005933.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000005933.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000005933.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce
CC an intermediate-sized product which is further hydrolyzed by sperm
CC hyaluronidase to give small oligosaccharides. Displays very low levels
CC of activity. Associates with and negatively regulates MST1R.
CC {ECO:0000256|ARBA:ARBA00037675}.
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:0000256|ARBA:ARBA00000251,
CC ECO:0000256|RuleBase:RU610713};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|PIRNR:PIRNR038193,
CC ECO:0000256|RuleBase:RU610713}.
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 RefSeq; XP_010894375.1; XM_010896073.2.
DR RefSeq; XP_010894377.1; XM_010896075.3.
DR RefSeq; XP_010894378.1; XM_010896076.1.
DR AlphaFoldDB; A0A3P8XRN6; -.
DR STRING; 8010.ENSELUP00000005933; -.
DR GlyCosmos; A0A3P8XRN6; 1 site, No reported glycans.
DR Ensembl; ENSELUT00000009803.2; ENSELUP00000005933.1; ENSELUG00000006901.2.
DR GeneID; 105025417; -.
DR GeneTree; ENSGT01020000230364; -.
DR InParanoid; A0A3P8XRN6; -.
DR OMA; TKNRESC; -.
DR OrthoDB; 5344684at2759; -.
DR Proteomes; UP000265140; LG17.
DR Bgee; ENSELUG00000006901; Expressed in spleen and 14 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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:SF6; HYALURONIDASE-2; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR038193-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU610713};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..472
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030079061"
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 52..345
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 217..233
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 370..381
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 375..429
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 431..440
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 472 AA; 53831 MW; 34DFFD8E1ED0659A CRC64;
MLHWTVLADW KVLLLVTLTW ECFCDEELKP TRWPLYPQKP LVLAWNAPTE ECRPRHSIIF
QLDQFQIVAS PNEGFVRQNL TIFYKDRLGL YPYYDEHDGT AMNGGLPQVT SLTQHLSKVP
DGIQYYIREA EAKGLAVIDW EEWRPLWIRN WDVKNVYRSR SKQLVAQKNP TWPSERVAKV
AQQEFEMSAR RFMLETLRLA KSLRPNQLWG FYLFPDCYNH DYKITLENYT GRCPDVEVAR
NEKLKWLWTE STALFPSVYM GTMLRSLPSG RQFVRNRVKE GMRLASSGEG LARPVFVYAK
PTYVNVLDLL TETDLVSTIG ESVALGAAGI ILWGDHTYAG SKASCKNLNE YLRGPLGRYL
LNVSTAAELC SQTLCGSRGR CLRRHADTDT YLHLSPHNHS IEALANGTLR IQGQLGEEEA
AGFRRDFWCQ CYAGFKGGGC SQKDPLQQRG SAPPSMNSRG SCVLVLLVTL LF
//
