HYAL2_BOVIN
ID HYAL2_BOVIN Reviewed; 473 AA.
AC Q8SQG8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11836391; DOI=10.1128/jvi.76.5.2141-2149.2002;
RA Dirks C., Duh F.-M., Rai S.K., Lerman M.I., Miller A.D.;
RT "Mechanism of cell entry and transformation by enzootic nasal tumor
RT virus.";
RL J. Virol. 76:2141-2149(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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; AF411973; AAL78385.1; -; mRNA.
DR EMBL; BT021810; AAX46657.1; -; mRNA.
DR EMBL; BT026155; ABG66994.1; -; mRNA.
DR EMBL; BC102042; AAI02043.1; -; mRNA.
DR RefSeq; NP_776772.1; NM_174347.2.
DR RefSeq; XP_010815967.1; XM_010817665.2.
DR RefSeq; XP_010815968.1; XM_010817666.2.
DR AlphaFoldDB; Q8SQG8; -.
DR SMR; Q8SQG8; -.
DR STRING; 9913.ENSBTAP00000000612; -.
DR BindingDB; Q8SQG8; -.
DR ChEMBL; CHEMBL3833905; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR PaxDb; Q8SQG8; -.
DR PRIDE; Q8SQG8; -.
DR Ensembl; ENSBTAT00000000612; ENSBTAP00000000612; ENSBTAG00000000484.
DR Ensembl; ENSBTAT00000052079; ENSBTAP00000051198; ENSBTAG00000000484.
DR Ensembl; ENSBTAT00000069832; ENSBTAP00000060743; ENSBTAG00000000484.
DR Ensembl; ENSBTAT00000070191; ENSBTAP00000061533; ENSBTAG00000000484.
DR GeneID; 281838; -.
DR KEGG; bta:281838; -.
DR CTD; 8692; -.
DR VEuPathDB; HostDB:ENSBTAG00000000484; -.
DR VGNC; VGNC:30011; HYAL2.
DR eggNOG; ENOG502QUYI; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_0_0_1; -.
DR InParanoid; Q8SQG8; -.
DR OMA; FHCHCYQ; -.
DR OrthoDB; 1096692at2759; -.
DR TreeFam; TF321598; -.
DR Reactome; R-BTA-2160916; Hyaluronan uptake and degradation.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000000484; Expressed in bone marrow and 106 other tissues.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
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:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS: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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
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 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..451
FT /note="Hyaluronidase-2"
FT /id="PRO_0000296276"
FT PROPEP 452..473
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000296277"
FT DOMAIN 364..442
FT /note="EGF-like"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 451
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..343
FT /evidence="ECO:0000250"
FT DISULFID 214..230
FT /evidence="ECO:0000250"
FT DISULFID 368..379
FT /evidence="ECO:0000250"
FT DISULFID 373..430
FT /evidence="ECO:0000250"
FT DISULFID 432..441
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 53881 MW; BC3D1E5DD120622E CRC64;
MWTGLGPAVT LALVLVVAWA TELKPTAPPI FTGRPFVVAW DVPTQDCGPR HKMPLDPKDM
KAFDVQASPN EGFVNQNITI FYRDRLGMYP HFNSVGRSVH GGVPQNGSLW VHLEMLKGHV
EHYIRTQEPA GLAVIDWEDW RPVWVRNWQD KDVYRRLSRH LVAIRHPDWP PERVAKEAQY
EFEFAARQFM LETLRFVKAF RPRHLWGFYL FPDCYNHDYV QNWETYTGRC PDVEVSRNDQ
LAWLWAESTA LFPSVYLEET LASSTHGRNF VSFRVQEALR VADVHHANHA LPVYVFTRPT
YSRGLTGLSE MDLISTIGES AALGAAGVIL WGDAGFTTSN ETCRRLKDYL TRSLVPYVVN
VSWAAQYCSW AQCHGHGRCV RRDPNAHTFL HLSASSFRLV PSHAPDEPRL RPEGELSWAD
RNHLQMHFRC QCYLGWGGEQ CQWDRRRAAG GASGAWAGSH LTGLLAVAVL AFT
