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Database: UniProt
Entry: Q76HN1
LinkDB: Q76HN1
Original site: Q76HN1 
ID   HYAL1_RAT               Reviewed;         449 AA.
AC   Q76HN1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 91.
DE   RecName: Full=Hyaluronidase-1;
DE            Short=Hyal-1;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase-1;
DE   Flags: Precursor;
GN   Name=Hyal1;
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   FUNCTION.
RX   PubMed=12397638; DOI=10.1002/ijc.10683;
RA   Jacobson A., Rahmanian M., Rubin K., Heldin P.;
RT   "Expression of hyaluronan synthase 2 or hyaluronidase 1 differentially
RT   affect the growth rate of transplantable colon carcinoma cell
RT   tumors.";
RL   Int. J. Cancer 102:212-219(2002).
CC   -!- FUNCTION: May have a role in promoting tumor progression. May
CC       block the TGFB1-enhanced cell growth (By similarity).
CC       Overexpression of HYAL1 suppressed the growth rate of colon
CC       carcinoma cell tumors in an experimental model. {ECO:0000250,
CC       ECO:0000269|PubMed:12397638}.
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;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Lysosome
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
DR   EMBL; AB100600; BAD14368.1; -; mRNA.
DR   RefSeq; NP_997499.1; NM_207616.1.
DR   UniGene; Rn.124438; -.
DR   ProteinModelPortal; Q76HN1; -.
DR   SMR; Q76HN1; -.
DR   STRING; 10116.ENSRNOP00000021408; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   PaxDb; Q76HN1; -.
DR   PRIDE; Q76HN1; -.
DR   GeneID; 367166; -.
DR   KEGG; rno:367166; -.
DR   UCSC; RGD:1303060; rat.
DR   CTD; 3373; -.
DR   RGD; 1303060; Hyal1.
DR   eggNOG; ENOG410IECJ; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   HOGENOM; HOG000015133; -.
DR   HOVERGEN; HBG052053; -.
DR   InParanoid; Q76HN1; -.
DR   KO; K01197; -.
DR   OrthoDB; 1096692at2759; -.
DR   PhylomeDB; Q76HN1; -.
DR   BRENDA; 3.2.1.35; 5301.
DR   PRO; PR:Q76HN1; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0036117; C:hyaluranon cable; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0050501; F:hyaluronan synthase activity; ISS:UniProtKB.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR   GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR   GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR   GO; GO:0030213; P:hyaluronan biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0030212; P:hyaluronan metabolic process; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0045927; P:positive regulation of growth; ISS:UniProtKB.
DR   GO; GO:1900106; P:positive regulation of hyaluranon cable assembly; ISS:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; ISS:UniProtKB.
DR   GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:GOC.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 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   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Glycosidase; Hydrolase; Lysosome; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL        1     39       {ECO:0000255}.
FT   CHAIN        40    449       Hyaluronidase-1.
FT                                /FTId=PRO_0000042626.
FT   DOMAIN      433    444       EGF-like.
FT   ACT_SITE    146    146       Proton donor. {ECO:0000250}.
FT   CARBOHYD     85     85       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    114    114       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    231    231       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    252    252       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    365    365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     58    348       {ECO:0000250}.
FT   DISULFID    222    236       {ECO:0000250}.
FT   DISULFID    373    384       {ECO:0000250}.
FT   DISULFID    378    433       {ECO:0000250}.
FT   DISULFID    435    444       {ECO:0000250}.
SQ   SEQUENCE   449 AA;  50645 MW;  EEF42E46758398EE CRC64;
     MKPFSPEVSP DPCPATAAHL LRTYTLFLTL LELAQGCRGS MVSNRPFITV WNADTHWCLK
     DHGVDVDVSV FDVVANKEQN FQGPNMTIFY REELGTYPYY TPTGEPVFGG LPQNASLVTH
     LAHAFQDIKA AMPEPDFSGL AVIDWEAWRP RWAFNWDSKD IYQQRSMELV RAEHPDWPET
     LVEAEAQGQF QEAAEAWMAG TLQLGQVLRP RGLWGYYGFP DCYNYDFLSP NYTGQCSLSI
     HDQNDQLGWL WNQSYALYPS IYLPAALMGT GKSQMYVRYR VQEAFRLALV SRDPHVPIMP
     YVQIFYEKTD YLLPLEELEH SLGESAAQGA AGAVLWISSE KTSTKESCQA IKAYMDSTLG
     PFILNVTSAA LLCSEALCSG RGRCVRHPSY PEALLTLSPA SFSIEPTHDG RPLSLKGTLS
     LKDRAQMAMK FKCRCYRGWS GEWCKKQDM
//
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