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Database: UniProt
Entry: Q6RHW4
LinkDB: Q6RHW4
Original site: Q6RHW4 
ID   HYAL1_PIG               Reviewed;         435 AA.
AC   Q6RHW4;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 78.
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   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).
CC   -!- FUNCTION: May have a role in promoting tumor progression. May
CC       block the TGFB1-enhanced cell growth (By similarity).
CC       {ECO:0000250}.
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   -!- TISSUE SPECIFICITY: Highly expressed in spleen, kidney, and lung.
CC       {ECO:0000269|PubMed:15218248}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
DR   EMBL; AY497543; AAR91599.1; -; mRNA.
DR   RefSeq; NP_999606.1; NM_214441.1.
DR   UniGene; Ssc.26119; -.
DR   ProteinModelPortal; Q6RHW4; -.
DR   SMR; Q6RHW4; -.
DR   STRING; 9823.ENSSSCP00000012158; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   PaxDb; Q6RHW4; -.
DR   PeptideAtlas; Q6RHW4; -.
DR   PRIDE; Q6RHW4; -.
DR   GeneID; 404698; -.
DR   KEGG; ssc:404698; -.
DR   CTD; 3373; -.
DR   eggNOG; ENOG410IECJ; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   HOGENOM; HOG000015133; -.
DR   HOVERGEN; HBG052053; -.
DR   InParanoid; Q6RHW4; -.
DR   KO; K01197; -.
DR   OrthoDB; 1096692at2759; -.
DR   BRENDA; 3.2.1.35; 6170.
DR   Proteomes; UP000008227; 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; ISS:UniProtKB.
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:0030214; P:hyaluronan catabolic 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     21       {ECO:0000255}.
FT   CHAIN        22    435       Hyaluronidase-1.
FT                                /FTId=PRO_0000042625.
FT   DOMAIN      418    429       EGF-like.
FT   ACT_SITE    131    131       Proton donor. {ECO:0000250}.
FT   CARBOHYD     70     70       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    107    107       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    121    121       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    216    216       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    350    350       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     43    333       {ECO:0000250}.
FT   DISULFID    207    221       {ECO:0000250}.
FT   DISULFID    358    369       {ECO:0000250}.
FT   DISULFID    363    418       {ECO:0000250}.
FT   DISULFID    420    429       {ECO:0000250}.
SQ   SEQUENCE   435 AA;  48507 MW;  5C5B7FB408B70B28 CRC64;
     MAAHLLPICT LFLNLLSVAQ GSRDPVVLNR PFTTIWNANT QWCLKRHGVD VDVSVFEVVV
     NPGQTFRGPN MTIFYSSQLG TYPYYTSAGE PVFGGLPQNA SLDVHLNRTF KDILAAMPES
     NFSGLAVIDW EAWRPRWAFN WDAKDIYRQR SRALVQKQHP DWPAPWVEAA AQDQFQEAAQ
     TWMAGTLKLG QTLRPHGLWG FYGFPDCYNY DFQSSNYTGQ CPPGVSAQND QLGWLWGQSR
     ALYPSIYLPS ALEGTNKTQL YVQHRVNEAF RVAAAAGDPN LPVLPYAQIF HDMTNRLLSR
     EELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQSIKEYV DTTLGPFILN VTSGALLCSQ
     AVCSGHGRCV RRPSHTEALP ILNPSSFSIK PTPGGGPLTL QGALSLKDRV QMAEEFQCRC
     YPGWRGTWCE QQGTR
//
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