GenomeNet

Database: UniProt
Entry: Q6RHW2
LinkDB: Q6RHW2
Original site: Q6RHW2 
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   16-JAN-2019, entry version 86.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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
RT   by 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
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   -!- TISSUE SPECIFICITY: Highly expressed in bladder, spleen and liver.
CC       Expressed at low levels in the kidney.
CC       {ECO:0000269|PubMed:15218248}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8VEI3}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
DR   EMBL; AY497545; AAR91601.1; -; mRNA.
DR   EMBL; AY472019; AAR33037.1; -; Genomic_DNA.
DR   RefSeq; NP_999604.1; NM_214439.1.
DR   UniGene; Ssc.19656; -.
DR   UniGene; Ssc.94538; -.
DR   ProteinModelPortal; Q6RHW2; -.
DR   SMR; Q6RHW2; -.
DR   STRING; 9823.ENSSSCP00000012156; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   PaxDb; Q6RHW2; -.
DR   PRIDE; Q6RHW2; -.
DR   GeneID; 404696; -.
DR   KEGG; ssc:404696; -.
DR   CTD; 8372; -.
DR   eggNOG; ENOG410IH0U; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   HOGENOM; HOG000015133; -.
DR   HOVERGEN; HBG052053; -.
DR   InParanoid; Q6RHW2; -.
DR   KO; K01197; -.
DR   OrthoDB; 1096692at2759; -.
DR   BRENDA; 3.2.1.35; 6170.
DR   Proteomes; UP000008227; 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     16       {ECO:0000255}.
FT   CHAIN        17    419       Hyaluronidase-3.
FT                                /FTId=PRO_0000248202.
FT   DOMAIN      352    407       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    331       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    205    220       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    356    367       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    361    395       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    397    406       {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
//
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