ID HYAL3_RAT Reviewed; 412 AA. AC Q76HM9; Q4V8Q0; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 08-NOV-2023, entry version 109. DE RecName: Full=Hyaluronidase-3; DE Short=Hyal-3; DE EC=3.2.1.35; DE AltName: Full=Hyaluronoglucosaminidase-3; DE Flags: Precursor; GN Name=Hyal3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; RA Hanaki A., Ueno Y., Nakasa T., Okinaka O.; RT "Expression and activity of rat hyaluronidase."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Facilitates sperm penetration into the layer of cumulus cells CC surrounding the egg by digesting hyaluronic acid. Involved in induction CC of the acrosome reaction in the sperm. Involved in follicular atresia, CC the breakdown of immature ovarian follicles that are not selected to CC ovulate. Induces ovarian granulosa cell apoptosis, possibly via CC apoptotic signaling pathway involving CASP8 and CASP3 activation, and CC poly(ADP-ribose) polymerase (PARP) cleavage. Has no hyaluronidase CC activity in embryonic fibroblasts in vitro. Has no hyaluronidase CC activity in granulosa cells in vitro. {ECO:0000250|UniProtKB:Q8VEI3}. 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:0000250|UniProtKB:Q8VEI3}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8VEI3}. Cell CC membrane {ECO:0000250|UniProtKB:Q8VEI3}. Cytoplasmic vesicle, secretory CC vesicle, acrosome {ECO:0000250|UniProtKB:Q8VEI3}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:Q8VEI3}. Early endosome CC {ECO:0000250|UniProtKB:Q8VEI3}. Note=Mostly present in low-density CC vesicles. Low levels in higher density vesicles of late endosomes and CC lysosomes. Localized in punctate cytoplasmic vesicles and in CC perinuclear structures, but does not colocalize with LAMP1. Localized CC on the plasma membrane over the acrosome and on the surface of the CC midpiece of the sperm tail. {ECO:0000250|UniProtKB:Q8VEI3}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8VEI3}. 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 EMBL; AB100602; BAD14370.1; -; mRNA. DR EMBL; BC097259; AAH97259.1; -; mRNA. DR RefSeq; NP_997482.2; NM_207599.2. DR AlphaFoldDB; Q76HM9; -. DR SMR; Q76HM9; -. DR STRING; 10116.ENSRNOP00000021590; -. DR CAZy; GH56; Glycoside Hydrolase Family 56. DR GlyCosmos; Q76HM9; 2 sites, No reported glycans. DR GlyGen; Q76HM9; 2 sites. DR PaxDb; 10116-ENSRNOP00000021590; -. DR GeneID; 300993; -. DR KEGG; rno:300993; -. DR AGR; RGD:1303334; -. DR CTD; 8372; -. DR RGD; 1303334; Hyal3. DR eggNOG; ENOG502QTXP; Eukaryota. DR InParanoid; Q76HM9; -. DR OrthoDB; 5344684at2759; -. DR PhylomeDB; Q76HM9; -. DR TreeFam; TF321598; -. DR BRENDA; 3.2.1.35; 5301. DR Reactome; R-RNO-2024101; CS/DS degradation. DR Reactome; R-RNO-2160916; Hyaluronan uptake and degradation. DR PRO; PR:Q76HM9; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB. DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB. DR GO; GO:0033906; F:hyaluronoglucuronidase activity; ISO:RGD. DR GO; GO:0004415; F:hyalurononglucosaminidase activity; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0051216; P:cartilage development; ISO:RGD. DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:RGD. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD. DR GO; GO:0071493; P:cellular response to UV-B; ISO:RGD. DR GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; ISO:RGD. DR GO; GO:2000355; P:negative regulation of ovarian follicle development; ISS:UniProtKB. DR GO; GO:0001552; P:ovarian follicle atresia; ISS:UniProtKB. DR GO; GO:0007341; P:penetration of zona pellucida; ISS:UniProtKB. DR GO; GO:2000368; P:positive regulation of acrosomal vesicle exocytosis; ISS:UniProtKB. DR GO; GO:0046677; P:response to antibiotic; ISO:RGD. DR GO; GO:0009615; P:response to virus; ISO:RGD. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR018155; Hyaluronidase. DR InterPro; IPR027260; Hyaluronidase-3. DR PANTHER; PTHR11769; HYALURONIDASE; 1. DR PANTHER; PTHR11769:SF19; HYALURONIDASE-3; 1. DR Pfam; PF01630; Glyco_hydro_56; 1. DR PIRSF; PIRSF038193; Hyaluronidase; 1. DR PIRSF; PIRSF500776; Hyaluronidase_3; 1. DR PRINTS; PR00846; GLHYDRLASE56. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 2: Evidence at transcript level; KW Cell membrane; Cytoplasmic vesicle; Disulfide bond; EGF-like domain; KW Endoplasmic reticulum; Endosome; Fertilization; Glycoprotein; Glycosidase; KW Hydrolase; Membrane; Reference proteome; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..412 FT /note="Hyaluronidase-3" FT /id="PRO_0000248204" FT DOMAIN 353..408 FT /note="EGF-like" FT ACT_SITE 129 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q12794" FT CARBOHYD 69 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 216 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 42..332 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT DISULFID 206..221 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT DISULFID 357..368 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT DISULFID 362..396 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT DISULFID 398..407 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT CONFLICT 29 FT /note="F -> L (in Ref. 2; AAH97259)" FT /evidence="ECO:0000305" SQ SEQUENCE 412 AA; 46207 MW; BB4949AADE4FB270 CRC64; MITQLGLTLV VGLTLCLVHV QALLQVPEFP FSVLWNVPSA RCKTRFGVHL PLDALGIIAN HGQRFHGQNI TIFYKNQFGL YPYFGPRGTA HNGGIPQAVS LDHHLAQAAH QILHNLGSSF AGLAVLDWEE WYPLWAGNWG THRQVYQAAS WAWAQQMFPD LNPQEQLHKA QTGFEQAARA LMEHTLRLGQ MLRPHGLWGF YRYPVCGNGW HNMASNYTGH CHPAIITRNT QLRWLWAASS ALFPSIYLPP RLPPAYHQTF VRHRLEEAFR VALTGHAHPL PVLAYVRLTH RSSGRFLSLD DLMQTIGVSA ALGAAGVVLW GDLSVSSSEE ECWRLHDYLV GTLGPYVINV TKAATACSHQ RCHGHGRCSW KDPGQMEAFL HLQPDDNLGA WKSFRCRCYL GWSGPTCLEP KP //