HYAL1_BOVIN
ID HYAL1_BOVIN Reviewed; 450 AA.
AC Q5E985; Q3T0A8; Q5E9Z4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 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 [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 [2]
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: May have a role in promoting tumor progression. May block the
CC TGFB1-enhanced cell growth (By 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Lysosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX08792.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT020775; AAX08792.1; ALT_FRAME; mRNA.
DR EMBL; BT021035; AAX09052.1; -; mRNA.
DR EMBL; BC102473; AAI02474.1; -; mRNA.
DR RefSeq; NP_001017941.1; NM_001017941.1.
DR AlphaFoldDB; Q5E985; -.
DR SMR; Q5E985; -.
DR STRING; 9913.ENSBTAP00000000611; -.
DR BindingDB; Q5E985; -.
DR ChEMBL; CHEMBL3833905; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR PaxDb; Q5E985; -.
DR PRIDE; Q5E985; -.
DR GeneID; 515397; -.
DR KEGG; bta:515397; -.
DR CTD; 3373; -.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR HOGENOM; CLU_036366_2_1_1; -.
DR InParanoid; Q5E985; -.
DR OrthoDB; 1096692at2759; -.
DR BRENDA; 3.2.1.35; 908.
DR Proteomes; UP000009136; 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:0050501; F:hyaluronan synthase activity; ISS:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase 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: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:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB.
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; -; 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 Disulfide bond; EGF-like domain; Glycoprotein; Glycosidase; Hydrolase;
KW Lysosome; Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..450
FT /note="Hyaluronidase-1"
FT /id="PRO_0000042623"
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 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
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"
FT CONFLICT 333
FT /note="V -> L (in Ref. 2; AAI02474)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="M -> L (in Ref. 2; AAI02474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 50508 MW; 576DD38745585AB5 CRC64;
MRPFSLEVSL HLPWAMAAHL LPVCTLFLNL LSMTQGSRDP VVPNQPFTTI WNANTEWCMK
KHGVDVDISI FDVVTNPGQT FRGPNMTIFY SSQLGTYPYY TSAGEPVFGG LPQNASLNAH
LARTFQDILA AMPEPRFSGL AVIDWEAWRP RWAFNWDTKD IYRQRSRALV QKQHPDWLAP
RVEAAAQDQF EGAAEEWMAG TLKLGQALRP QGLWGFYNFP ECYNYDFKSP NYTGRCPLNI
CAQNDQLGWL WGQSRALYPS IYLPAALEGT KKTQMFVQHR VAEAFRVAAG AGDPKLPVLP
YMQLFYDMTN HFLPAEELEH SLGESAAQGA AGVVLWVSWL STSTKESCQA IKEYVDTTLG
PSILNVTSGA RLCSQVLCSG HGRCARRPSY PKARLILNST SFSIKPTPGG GPLTLQGALS
LEDRLRMAVE FECRCYRGWR GTRCEQWGMW
