HYAL3_PIG
ID HYAL3_PIG Reviewed; 419 AA.
AC Q6RHW2; Q6S3P5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15218248; DOI=10.1159/000078571;
RA Gatphayak K., Knorr C., Beck J., Brenig B.;
RT "Molecular characterization of porcine hyaluronidase genes 1, 2, and 3
RT clustered on SSC13q21.";
RL Cytogenet. Genome Res. 106:98-106(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 127-247.
RX PubMed=14619892; DOI=10.1159/000074181;
RA Gatphayak K., Knorr C., Habermann F., Fries R., Brenig B.;
RT "Assignment of the porcine hyaluronidase-3 (HYAL3) gene to SSC13-->q21 by
RT FISH and confirmation by hybrid panel analyses.";
RL Cytogenet. Genome Res. 101:178-178(2003).
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 -!- TISSUE SPECIFICITY: Highly expressed in bladder, spleen and liver.
CC Expressed at low levels in the kidney. {ECO:0000269|PubMed:15218248}.
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; AY497545; AAR91601.1; -; mRNA.
DR EMBL; AY472019; AAR33037.1; -; Genomic_DNA.
DR RefSeq; NP_999604.1; NM_214439.1.
DR AlphaFoldDB; Q6RHW2; -.
DR SMR; Q6RHW2; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR PaxDb; Q6RHW2; -.
DR GeneID; 404696; -.
DR KEGG; ssc:404696; -.
DR CTD; 8372; -.
DR eggNOG; ENOG502QTXP; Eukaryota.
DR InParanoid; Q6RHW2; -.
DR BRENDA; 3.2.1.35; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB.
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 Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..419
FT /note="Hyaluronidase-3"
FT /id="PRO_0000248202"
FT DOMAIN 352..407
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 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..331
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 205..220
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 356..367
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 361..395
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 397..406
FT /evidence="ECO:0000250|UniProtKB:Q12794"
SQ SEQUENCE 419 AA; 46393 MW; 8035CDE3D04324AC CRC64;
MTMQLGLALV LGVAMCLGCG QPLLRAPERP FCVLWNVPSA RCKARFGVHL PLEALGITAN
HGQRFHGQNI TIFYKSQLGL YPYFGPRGTA HNGGIPQAVS LDHHLARAAY QIHRSLRPGF
TGLAVLDWEE WCPLWAGNWG RRQAYQAASC AWAQRVYPNL DPQEQLCKAR AGFEEAARAL
MEDTLRLGRM LRPHGLWGFY HYPACGNGWH GTASNYTGHC HAAALARNTQ LYWLWAASSA
LFPSIYLPPG LPPAYHQAFV RYRLEEAFRV ALVGHPHPLP VLAYARLTHR NSGRFLSQDE
LVQTIGVSAA LGASGVVLWG DLSFSSSEEE CWHLRGYLVG TLGPYVINVT RAAMACSHQR
CHGHGRCAWQ DPGQLKVFLH LHPGGSPGAW ESFSCRCYWG WAGPTCQEPR PELGPEEAT
