HYAL3_PONAB
ID HYAL3_PONAB Reviewed; 414 AA.
AC Q5REQ1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 68.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857468; CAH89756.1; -; mRNA.
DR AlphaFoldDB; Q5REQ1; -.
DR SMR; Q5REQ1; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR InParanoid; Q5REQ1; -.
DR Proteomes; UP000001595; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..414
FT /note="Hyaluronidase-3"
FT /id="PRO_0000248203"
FT DOMAIN 349..404
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..328
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 205..220
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 353..364
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 358..392
FT /evidence="ECO:0000250|UniProtKB:Q12794"
FT DISULFID 394..403
FT /evidence="ECO:0000250|UniProtKB:Q12794"
SQ SEQUENCE 414 AA; 46114 MW; CBE2FB0A6F8633A8 CRC64;
MTTRLGPALV LGVALCLGCG QPLPQVPERP FSVLWNVPSA HCKSRFGVHL PLNALGIIAN
RGQHFHGQNM TIFYKNQLGL YPYFGPKGTA HNGGIPQALP LDRHLALAAY QIHHSLRPGF
AGPAVLDWEE WCPLWAGNWG RRRAYQAASW AWAQQVFPDL DPQEQLYKAY TGFEQAARAL
MEDTLRVAQA LRPHGLWGFY HYPACGNGWH SMASNYTGRC HAATLARNTQ LHWLWAASSA
LFPSIYLPPR LPPAHHQAFV RHRLEEAFRV ALVGHLPVLA YVRLTHRRSG RFLSQDDLVQ
TIGVSAALGA AGVVLWGDLS LSSSEEECWH LHDYLVDTLG PYGINVTRAA MACSHQRCHG
HGRCARRDPG QMEAFLHLWP DGSLGDWKSF SCHCYWGWAG PTCQEPRLGP KEAV
