HYAL3_RAT
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 25-MAY-2022, entry version 104.
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}.
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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 GlyGen; Q76HM9; 3 sites.
DR PaxDb; Q76HM9; -.
DR PRIDE; Q76HM9; -.
DR GeneID; 300993; -.
DR KEGG; rno:300993; -.
DR CTD; 8372; -.
DR RGD; 1303334; Hyal3.
DR eggNOG; ENOG502QTXP; Eukaryota.
DR InParanoid; Q76HM9; -.
DR OrthoDB; 1096692at2759; -.
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; -; 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; PTHR11769; 1.
DR PANTHER; PTHR11769:SF19; PTHR11769:SF19; 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; SSF51445; 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
