GenomeNet

Database: UniProt
Entry: O35632
LinkDB: O35632
Original site: O35632 
ID   HYAL2_MOUSE             Reviewed;         473 AA.
AC   O35632; O35631; Q99MS9; Q99MT0;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 2.
DT   10-APR-2019, entry version 160.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=9790770; DOI=10.1006/geno.1998.5472;
RA   Strobl B., Wechselberger C., Beier D., Lepperdinger G.;
RT   "Structural organization and chromosomal localization of Hyal2, a gene
RT   encoding a lysosomal hyaluronidase.";
RL   Genomics 53:214-219(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/HeJ, and Czech II;
RX   PubMed=11296287; DOI=10.1073/pnas.071572898;
RA   Rai S.K., Duh F.-M., Vigdorovich V., Danilkovitch-Miagkova A.,
RA   Lerman M.I., Miller A.D.;
RT   "Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol
RT   (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus,
RT   the envelope protein of which mediates oncogenic transformation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4443-4448(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Czech II;
RX   PubMed=11960552; DOI=10.1186/1471-2121-3-8;
RA   Chang N.-S.;
RT   "Transforming growth factor-beta1 blocks the enhancement of tumor
RT   necrosis factor cytotoxicity by hyaluronidase Hyal-2 in L929
RT   fibroblasts.";
RL   BMC Cell Biol. 3:8-8(2002).
RN   [4]
RP   REVIEW.
RX   PubMed=11731268; DOI=10.1016/S0945-053X(01)00170-6;
RA   Lepperdinger G., Mullegger J., Kreil G.;
RT   "Hyal2 -- less active, but more versatile?";
RL   Matrix Biol. 20:509-514(2001).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-390.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to
CC       produce an intermediate-sized product which is further hydrolyzed
CC       by sperm hyaluronidase to give small oligosaccharides. Displays
CC       very low levels of activity. Associates with and negatively
CC       regulates MST1R (By similarity). {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   -!- SUBUNIT: Interacts with MST1R. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
CC       GPI-anchor {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. In the brain, expressed
CC       during embryonic stages but expression decreases after birth and
CC       is barely detectable in adult brain. {ECO:0000269|PubMed:9790770}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be lysosomal. {ECO:0000305}.
DR   EMBL; AJ000059; CAA03888.1; -; mRNA.
DR   EMBL; AJ000060; CAA03889.1; -; Genomic_DNA.
DR   EMBL; AF302843; AAK28481.1; -; mRNA.
DR   EMBL; AF302844; AAK28482.1; -; mRNA.
DR   EMBL; AF422177; AAL17823.1; -; mRNA.
DR   CCDS; CCDS23496.1; -.
DR   RefSeq; NP_034619.2; NM_010489.2.
DR   RefSeq; XP_006511706.1; XM_006511643.3.
DR   RefSeq; XP_006511707.1; XM_006511644.3.
DR   RefSeq; XP_006511708.1; XM_006511645.3.
DR   UniGene; Mm.440982; -.
DR   UniGene; Mm.4834; -.
DR   ProteinModelPortal; O35632; -.
DR   SMR; O35632; -.
DR   STRING; 10090.ENSMUSP00000010191; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   iPTMnet; O35632; -.
DR   PhosphoSitePlus; O35632; -.
DR   jPOST; O35632; -.
DR   PaxDb; O35632; -.
DR   PeptideAtlas; O35632; -.
DR   PRIDE; O35632; -.
DR   Ensembl; ENSMUST00000010191; ENSMUSP00000010191; ENSMUSG00000010047.
DR   Ensembl; ENSMUST00000195752; ENSMUSP00000141280; ENSMUSG00000010047.
DR   GeneID; 15587; -.
DR   KEGG; mmu:15587; -.
DR   UCSC; uc009rlu.1; mouse.
DR   CTD; 8692; -.
DR   MGI; MGI:1196334; Hyal2.
DR   eggNOG; ENOG410IECJ; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   GeneTree; ENSGT00950000182708; -.
DR   HOGENOM; HOG000015133; -.
DR   HOVERGEN; HBG052053; -.
DR   InParanoid; O35632; -.
DR   KO; K01197; -.
DR   OMA; WGGEQCQ; -.
DR   OrthoDB; 1096692at2759; -.
DR   PhylomeDB; O35632; -.
DR   TreeFam; TF321598; -.
DR   BRENDA; 3.2.1.35; 3474.
DR   Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
DR   PRO; PR:O35632; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000010047; Expressed in 225 organ(s), highest expression level in dorsal pancreas.
DR   ExpressionAtlas; O35632; baseline and differential.
DR   Genevisible; O35632; MM.
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; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; ISS: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 factor complex; IDA:BHF-UCL.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR   GO; GO:0033906; F:hyaluronoglucuronidase activity; ISS: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:MGI.
DR   GO; GO:0050431; F:transforming growth factor beta binding; IPI:BHF-UCL.
DR   GO; GO:0001618; F:virus receptor activity; IDA: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; IDA:BHF-UCL.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
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; IMP:MGI.
DR   GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB.
DR   GO; GO:0042117; P:monocyte activation; ISS:UniProtKB.
DR   GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR   GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP:MGI.
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; IDA:MGI.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
DR   GO; GO:2000484; P:positive regulation of interleukin-8 secretion; ISS:UniProtKB.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR   GO; GO:0070295; P:renal water absorption; ISS:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0019087; P:transformation of host cell by virus; ISS:UniProtKB.
DR   GO; GO:0046718; P:viral entry into host cell; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein;
KW   Membrane; Receptor; Reference proteome; Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    448       Hyaluronidase-2.
FT                                /FTId=PRO_0000012101.
FT   PROPEP      449    473       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000012102.
FT   DOMAIN      361    439       EGF-like.
FT   ACT_SITE    135    135       Proton donor. {ECO:0000250}.
FT   LIPID       448    448       GPI-anchor amidated asparagine;
FT                                alternate. {ECO:0000255}.
FT   CARBOHYD     74     74       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    357    357       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    390    390       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD    448    448       N-linked (GlcNAc...) asparagine;
FT                                alternate. {ECO:0000255}.
FT   DISULFID     47    340       {ECO:0000250}.
FT   DISULFID    211    227       {ECO:0000250}.
FT   DISULFID    365    376       {ECO:0000250}.
FT   DISULFID    370    427       {ECO:0000250}.
FT   DISULFID    429    438       {ECO:0000250}.
FT   CONFLICT     26     27       TA -> KP (in Ref. 1; CAA03888/CAA03889).
FT                                {ECO:0000305}.
FT   CONFLICT    193    199       YVKAVRP -> LRQGSQT (in Ref. 1; CAA03888).
FT                                {ECO:0000305}.
FT   CONFLICT    250    250       Missing (in Ref. 1; CAA03888).
FT                                {ECO:0000305}.
FT   CONFLICT    269    272       SFRV -> RFGG (in Ref. 1; CAA03888).
FT                                {ECO:0000305}.
FT   CONFLICT    355    355       I -> V (in Ref. 2; AAK28481).
FT                                {ECO:0000305}.
FT   CONFLICT    383    383       A -> V (in Ref. 1; CAA03888/CAA03889).
FT                                {ECO:0000305}.
FT   CONFLICT    416    422       ADLNYLQ -> RDRQLPE (in Ref. 1; CAA03888).
FT                                {ECO:0000305}.
SQ   SEQUENCE   473 AA;  53618 MW;  DD433C9FFCF8147C CRC64;
     MRAGLGPIIT LALVLEVAWA GELKPTAPPI FTGRPFVVAW NVPTQECAPR HKVPLDLRAF
     DVKATPNEGF FNQNITTFYY DRLGLYPRFD AAGTSVHGGV PQNGSLCAHL PMLKESVERY
     IQTQEPGGLA VIDWEEWRPV WVRNWQEKDV YRQSSRQLVA SRHPDWPSDR VMKQAQYEFE
     FAARQFMLNT LRYVKAVRPQ HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW
     LWAESTALFP SVYLDETLAS SVHSRNFVSF RVREALRVAH THHANHALPV YVFTRPTYTR
     GLTGLSQVDL ISTIGESAAL GSAGVIFWGD SEDASSMETC QYLKNYLTQL LVPYIVNVSW
     ATQYCSWTQC HGHGRCVRRN PSANTFLHLN ASSFRLVPGH TPSEPQLRPE GQLSEADLNY
     LQKHFRCQCY LGWGGEQCQR NYKGAAGNAS RAWAGSHLTS LLGLVAVALT WTL
//
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