GenomeNet

Database: UniProt
Entry: Q76HM9
LinkDB: Q76HM9
Original site: Q76HM9 
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   16-JAN-2019, 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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; AB100602; BAD14370.1; -; mRNA.
DR   EMBL; BC097259; AAH97259.1; -; mRNA.
DR   RefSeq; NP_997482.2; NM_207599.2.
DR   UniGene; Rn.229321; -.
DR   ProteinModelPortal; Q76HM9; -.
DR   SMR; Q76HM9; -.
DR   STRING; 10116.ENSRNOP00000021590; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   PaxDb; Q76HM9; -.
DR   PRIDE; Q76HM9; -.
DR   GeneID; 300993; -.
DR   KEGG; rno:300993; -.
DR   CTD; 8372; -.
DR   RGD; 1303334; Hyal3.
DR   eggNOG; ENOG410IH0U; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   HOGENOM; HOG000015133; -.
DR   HOVERGEN; HBG052053; -.
DR   InParanoid; Q76HM9; -.
DR   KO; K01197; -.
DR   OrthoDB; 1096692at2759; -.
DR   PhylomeDB; Q76HM9; -.
DR   TreeFam; TF321598; -.
DR   BRENDA; 3.2.1.35; 5301.
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: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; IPR013032; EGF-like_CS.
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     22       {ECO:0000255}.
FT   CHAIN        23    412       Hyaluronidase-3.
FT                                /FTId=PRO_0000248204.
FT   DOMAIN      353    408       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    216    216       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     42    332       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    206    221       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    357    368       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    362    396       {ECO:0000250|UniProtKB:Q12794}.
FT   DISULFID    398    407       {ECO:0000250|UniProtKB:Q12794}.
FT   CONFLICT     29     29       F -> L (in Ref. 2; AAH97259).
FT                                {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
//
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