HYAL2_RAT
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 25-MAY-2022, entry version 126.
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}.
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DR EMBL; AF034218; AAD01980.1; -; mRNA.
DR AlphaFoldDB; Q9Z2Q3; -.
DR SMR; Q9Z2Q3; -.
DR STRING; 10116.ENSRNOP00000017461; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyGen; Q9Z2Q3; 3 sites.
DR PaxDb; Q9Z2Q3; -.
DR UCSC; RGD:620321; rat.
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:0031362; C:anchored component of external side of plasma membrane; ISO:RGD.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
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: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: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:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0060586; P:multicellular organismal 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 protein kinase B signaling; 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; -; 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 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
