ID HYAL2_RAT Reviewed; 473 AA. AC Q9Z2Q3; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 24-JAN-2024, entry version 132. DE RecName: Full=Hyaluronidase-2; DE Short=Hyal-2; DE EC=3.2.1.35; DE AltName: Full=Hyaluronoglucosaminidase-2; DE Flags: Precursor; GN Name=Hyal2; 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]. RA Boel P., Mertens-Strijthagen J., Flamion B.; RT "Cloning and expression of the cDNA for a rat hyaluronidase."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to produce CC an intermediate-sized product which is further hydrolyzed by sperm CC hyaluronidase to give small oligosaccharides. Displays very low levels CC of activity. Associates with and negatively regulates MST1R (By CC similarity). {ECO:0000250}. 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 -!- SUBUNIT: Interacts with MST1R. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI- CC anchor {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF034218; AAD01980.1; -; mRNA. DR AlphaFoldDB; Q9Z2Q3; -. DR SMR; Q9Z2Q3; -. DR STRING; 10116.ENSRNOP00000075204; -. DR CAZy; GH56; Glycoside Hydrolase Family 56. DR GlyCosmos; Q9Z2Q3; 3 sites, No reported glycans. DR GlyGen; Q9Z2Q3; 3 sites. DR PhosphoSitePlus; Q9Z2Q3; -. DR PaxDb; 10116-ENSRNOP00000017461; -. DR UCSC; RGD:620321; rat. DR AGR; RGD:620321; -. DR RGD; 620321; Hyal2. DR eggNOG; ENOG502QUYI; Eukaryota. DR InParanoid; Q9Z2Q3; -. DR PhylomeDB; Q9Z2Q3; -. DR BRENDA; 3.2.1.35; 5301. DR Reactome; R-RNO-2160916; Hyaluronan uptake and degradation. DR PRO; PR:Q9Z2Q3; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0009986; C:cell surface; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0005764; C:lysosome; ISS:UniProtKB. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0005902; C:microvillus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD. DR GO; GO:0019899; F:enzyme binding; ISO:RGD. DR GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB. DR GO; GO:0033906; F:hyaluronoglucuronidase activity; IDA:UniProtKB. DR GO; GO:0004415; F:hyalurononglucosaminidase activity; ISS:UniProtKB. DR GO; GO:0030294; F:receptor signaling protein tyrosine kinase inhibitor activity; ISS:UniProtKB. DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD. DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:RGD. DR GO; GO:0001618; F:virus receptor activity; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB. DR GO; GO:0071560; P:cellular response to transforming growth factor beta 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:0051607; P:defense response to virus; ISO:RGD. DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; ISS:UniProtKB. DR GO; GO:0006027; P:glycosaminoglycan catabolic process; ISS:UniProtKB. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD. DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB. DR GO; GO:0001822; P:kidney development; IEP:UniProtKB. DR GO; GO:0042117; P:monocyte activation; ISS:UniProtKB. DR GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; ISO:RGD. DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. DR GO; GO:0010764; P:negative regulation of fibroblast migration; ISS:UniProtKB. DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB. DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:UniProtKB. DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD. DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0035810; P:positive regulation of urine volume; IEP:UniProtKB. DR GO; GO:0070295; P:renal water absorption; IEP:UniProtKB. DR GO; GO:0046677; P:response to antibiotic; ISO:RGD. 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:0048705; P:skeletal system morphogenesis; ISO:RGD. DR GO; GO:0046718; P:viral entry into host cell; IDA:RGD. 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:SF6; HYALURONIDASE-2; 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 Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Glycosidase; KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Receptor; Reference proteome; KW Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..448 FT /note="Hyaluronidase-2" FT /id="PRO_0000012103" FT PROPEP 449..473 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000012104" FT DOMAIN 361..439 FT /note="EGF-like" FT ACT_SITE 135 FT /note="Proton donor" FT /evidence="ECO:0000250" FT LIPID 448 FT /note="GPI-anchor amidated aspartate" FT /evidence="ECO:0000255" FT CARBOHYD 74 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 357 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 47..340 FT /evidence="ECO:0000250" FT DISULFID 211..227 FT /evidence="ECO:0000250" FT DISULFID 365..376 FT /evidence="ECO:0000250" FT DISULFID 370..427 FT /evidence="ECO:0000250" FT DISULFID 429..438 FT /evidence="ECO:0000250" SQ SEQUENCE 473 AA; 53999 MW; 46B90A2F260B0CE4 CRC64; MRAGLGPIIT LALVLEVAWA SELKPTAPPI FTGRPFVVAW NVPTQECAPR HKVPLDLRAF DVEATPNEGF FNQNITTFYY DRLGLYPRFD AAGMSVHGGV PQNGSLCAHL PMLKEAVERY IQTQEPAGLA VIDWEEWRPV WVRNWQEKDV YRQSSRQLVA SRHPDWPSDR IVKQAQYEFE FAARQFMLNT LRYVKAVRPQ HLWGFYLFPD CYNHDYVQNW DSYTGRCPDV EVAQNDQLAW LWAENTALFP SVYLDKTLAS SKHSRNFVSF RVQEALRVAH THHANHALPV YVFTRPTYTR RLTELNQMDL ISTIGESAAL GSAGVIFWGD SVYASSMENC QNLKKYLTQT LVPYIVNVSW ATQYCSWTQC HGHGRCVRRN PSASTFLHLS PSSFRLVPGR TPSEPQLRPE GELSEDDLSY LQMHFRCHCY LGWGGEQCQW NHKRAAGDAS RAWAGAHLAS LLGLVAMTLT WTL //