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Database: UniProt
Entry: Q5REQ1
LinkDB: Q5REQ1
Original site: Q5REQ1 
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   05-DEC-2018, entry version 65.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
CC       cells surrounding the egg by digesting hyaluronic acid. Involved
CC       in induction of the acrosome reaction in the sperm. Involved in
CC       follicular atresia, the breakdown of immature ovarian follicles
CC       that are not selected to ovulate. Induces ovarian granulosa cell
CC       apoptosis, possibly via apoptotic signaling pathway involving
CC       CASP8 and CASP3 activation, and poly(ADP-ribose) polymerase (PARP)
CC       cleavage. Has no hyaluronidase activity in embryonic fibroblasts
CC       in vitro. Has no hyaluronidase activity in granulosa cells in
CC       vitro. {ECO:0000250|UniProtKB:Q8VEI3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-
CC         beta-D-glucosamine and D-glucuronate residues in hyaluronate.;
CC         EC=3.2.1.35; Evidence={ECO:0000250|UniProtKB:Q8VEI3};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8VEI3}.
CC       Cell membrane {ECO:0000250|UniProtKB:Q8VEI3}. Cytoplasmic vesicle,
CC       secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q8VEI3}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8VEI3}. Early
CC       endosome {ECO:0000250|UniProtKB:Q8VEI3}. Note=Mostly present in
CC       low-density vesicles. Low levels in higher density vesicles of
CC       late endosomes and lysosomes. Localized in punctate cytoplasmic
CC       vesicles and in perinuclear structures, but does not colocalize
CC       with LAMP1. Localized on the plasma membrane over the acrosome and
CC       on the surface of the midpiece of the sperm tail.
CC       {ECO:0000250|UniProtKB:Q8VEI3}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8VEI3}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
DR   EMBL; CR857468; CAH89756.1; -; mRNA.
DR   UniGene; Pab.19855; -.
DR   ProteinModelPortal; Q5REQ1; -.
DR   SMR; Q5REQ1; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   HOVERGEN; HBG052053; -.
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; Complete proteome; Cytoplasmic vesicle; Disulfide bond;
KW   EGF-like domain; Endoplasmic reticulum; Endosome; Fertilization;
KW   Glycoprotein; Glycosidase; Hydrolase; Membrane; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    414       Hyaluronidase-3.
FT                                /FTId=PRO_0000248203.
FT   DOMAIN      349    404       EGF-like.
FT   ACT_SITE    129    129       Proton donor.
FT                                {ECO:0000250|UniProtKB:Q12794}.
FT   CARBOHYD     69     69       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    215    215       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     42    328       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    205    220       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    353    364       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    358    392       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    394    403       {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
//
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