HYAL1_PIG
ID HYAL1_PIG Reviewed; 435 AA.
AC Q6RHW4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15218248; DOI=10.1159/000078571;
RA Gatphayak K., Knorr C., Beck J., Brenig B.;
RT "Molecular characterization of porcine hyaluronidase genes 1, 2, and 3
RT clustered on SSC13q21.";
RL Cytogenet. Genome Res. 106:98-106(2004).
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 -!- TISSUE SPECIFICITY: Highly expressed in spleen, kidney, and lung.
CC {ECO:0000269|PubMed:15218248}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; AY497543; AAR91599.1; -; mRNA.
DR RefSeq; NP_999606.1; NM_214441.1.
DR AlphaFoldDB; Q6RHW4; -.
DR SMR; Q6RHW4; -.
DR STRING; 9823.ENSSSCP00000012158; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR PaxDb; Q6RHW4; -.
DR PeptideAtlas; Q6RHW4; -.
DR Ensembl; ENSSSCT00025099366; ENSSSCP00025043731; ENSSSCG00025072252.
DR Ensembl; ENSSSCT00035110453; ENSSSCP00035048195; ENSSSCG00035080541.
DR Ensembl; ENSSSCT00065096081; ENSSSCP00065042049; ENSSSCG00065069969.
DR GeneID; 404698; -.
DR KEGG; ssc:404698; -.
DR CTD; 3373; -.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR InParanoid; Q6RHW4; -.
DR OrthoDB; 1096692at2759; -.
DR BRENDA; 3.2.1.35; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..435
FT /note="Hyaluronidase-1"
FT /id="PRO_0000042625"
FT DOMAIN 418..429
FT /note="EGF-like"
FT ACT_SITE 131
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..333
FT /evidence="ECO:0000250"
FT DISULFID 207..221
FT /evidence="ECO:0000250"
FT DISULFID 358..369
FT /evidence="ECO:0000250"
FT DISULFID 363..418
FT /evidence="ECO:0000250"
FT DISULFID 420..429
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 48507 MW; 5C5B7FB408B70B28 CRC64;
MAAHLLPICT LFLNLLSVAQ GSRDPVVLNR PFTTIWNANT QWCLKRHGVD VDVSVFEVVV
NPGQTFRGPN MTIFYSSQLG TYPYYTSAGE PVFGGLPQNA SLDVHLNRTF KDILAAMPES
NFSGLAVIDW EAWRPRWAFN WDAKDIYRQR SRALVQKQHP DWPAPWVEAA AQDQFQEAAQ
TWMAGTLKLG QTLRPHGLWG FYGFPDCYNY DFQSSNYTGQ CPPGVSAQND QLGWLWGQSR
ALYPSIYLPS ALEGTNKTQL YVQHRVNEAF RVAAAAGDPN LPVLPYAQIF HDMTNRLLSR
EELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQSIKEYV DTTLGPFILN VTSGALLCSQ
AVCSGHGRCV RRPSHTEALP ILNPSSFSIK PTPGGGPLTL QGALSLKDRV QMAEEFQCRC
YPGWRGTWCE QQGTR
