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 24-JAN-2024, entry version 104.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 tumors.";
RL Int. J. Cancer 102:212-219(2002).
CC -!- FUNCTION: May have a role in promoting tumor progression. May block the
CC TGFB1-enhanced cell growth (By similarity). Overexpression of HYAL1
CC suppressed the growth rate of colon carcinoma cell tumors in an
CC experimental model. {ECO:0000250, ECO:0000269|PubMed:12397638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Lysosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; AB100600; BAD14368.1; -; mRNA.
DR RefSeq; NP_997499.1; NM_207616.1.
DR AlphaFoldDB; Q76HN1; -.
DR SMR; Q76HN1; -.
DR STRING; 10116.ENSRNOP00000021408; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyCosmos; Q76HN1; 5 sites, No reported glycans.
DR GlyGen; Q76HN1; 5 sites.
DR PhosphoSitePlus; Q76HN1; -.
DR PaxDb; 10116-ENSRNOP00000021408; -.
DR GeneID; 367166; -.
DR KEGG; rno:367166; -.
DR UCSC; RGD:1303060; rat.
DR AGR; RGD:1303060; -.
DR CTD; 3373; -.
DR RGD; 1303060; Hyal1.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR InParanoid; Q76HN1; -.
DR OrthoDB; 5344684at2759; -.
DR PhylomeDB; Q76HN1; -.
DR BRENDA; 3.2.1.35; 5301.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR Reactome; R-RNO-2160916; Hyaluronan uptake and degradation.
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:0052757; F:chondroitin hydrolase activity; ISO:RGD.
DR GO; GO:0050501; F:hyaluronan synthase activity; ISS:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; ISO:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:RGD.
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:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR GO; GO:0030207; P:chondroitin sulfate catabolic process; ISO:RGD.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; ISO:RGD.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030214; P:hyaluronan catabolic process; ISO:RGD.
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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR PANTHER; PTHR11769; HYALURONIDASE; 1.
DR PANTHER; PTHR11769:SF23; HYALURONIDASE-1; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Glycosidase; Hydrolase;
KW Lysosome; Reference proteome; Secreted; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..449
FT /note="Hyaluronidase-1"
FT /id="PRO_0000042626"
FT DOMAIN 433..444
FT /note="EGF-like"
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..348
FT /evidence="ECO:0000250"
FT DISULFID 222..236
FT /evidence="ECO:0000250"
FT DISULFID 373..384
FT /evidence="ECO:0000250"
FT DISULFID 378..433
FT /evidence="ECO:0000250"
FT DISULFID 435..444
FT /evidence="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
//
