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HYAL1_RAT
ID   HYAL1_RAT               Reviewed;         449 AA.
AC   Q76HN1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
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   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].
RC   STRAIN=Wistar;
RA   Hanaki A., Ueno Y., Nakasa T., Okinaka O.;
RT   "Expression and activity of rat hyaluronidase.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=12397638; DOI=10.1002/ijc.10683;
RA   Jacobson A., Rahmanian M., Rubin K., Heldin P.;
RT   "Expression of hyaluronan synthase 2 or hyaluronidase 1 differentially
RT   affect the growth rate of transplantable colon carcinoma cell tumors.";
RL   Int. J. Cancer 102:212-219(2002).
CC   -!- FUNCTION: May have a role in promoting tumor progression. May block the
CC       TGFB1-enhanced cell growth (By similarity). Overexpression of HYAL1
CC       suppressed the growth rate of colon carcinoma cell tumors in an
CC       experimental model. {ECO:0000250, ECO:0000269|PubMed:12397638}.
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}.
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DR   EMBL; AB100600; BAD14368.1; -; mRNA.
DR   RefSeq; NP_997499.1; NM_207616.1.
DR   AlphaFoldDB; Q76HN1; -.
DR   SMR; Q76HN1; -.
DR   STRING; 10116.ENSRNOP00000021408; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   GlyGen; Q76HN1; 5 sites.
DR   PaxDb; Q76HN1; -.
DR   GeneID; 367166; -.
DR   KEGG; rno:367166; -.
DR   UCSC; RGD:1303060; rat.
DR   CTD; 3373; -.
DR   RGD; 1303060; Hyal1.
DR   eggNOG; ENOG502QTUU; Eukaryota.
DR   InParanoid; Q76HN1; -.
DR   OrthoDB; 1096692at2759; -.
DR   PhylomeDB; Q76HN1; -.
DR   BRENDA; 3.2.1.35; 5301.
DR   Reactome; R-RNO-2024101; CS/DS degradation.
DR   Reactome; R-RNO-2160916; Hyaluronan uptake and degradation.
DR   PRO; PR:Q76HN1; -.
DR   Proteomes; UP000002494; 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; ISO:RGD.
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; ISO:RGD.
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: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:0060272; P:embryonic skeletal joint morphogenesis; ISO:RGD.
DR   GO; GO:0030213; P:hyaluronan biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0030214; P:hyaluronan catabolic process; ISO:RGD.
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..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..449
FT                   /note="Hyaluronidase-1"
FT                   /id="PRO_0000042626"
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        114
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        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
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"
SQ   SEQUENCE   449 AA;  50645 MW;  EEF42E46758398EE CRC64;
     MKPFSPEVSP DPCPATAAHL LRTYTLFLTL LELAQGCRGS MVSNRPFITV WNADTHWCLK
     DHGVDVDVSV FDVVANKEQN FQGPNMTIFY REELGTYPYY TPTGEPVFGG LPQNASLVTH
     LAHAFQDIKA AMPEPDFSGL AVIDWEAWRP RWAFNWDSKD IYQQRSMELV RAEHPDWPET
     LVEAEAQGQF QEAAEAWMAG TLQLGQVLRP RGLWGYYGFP DCYNYDFLSP NYTGQCSLSI
     HDQNDQLGWL WNQSYALYPS IYLPAALMGT GKSQMYVRYR VQEAFRLALV SRDPHVPIMP
     YVQIFYEKTD YLLPLEELEH SLGESAAQGA AGAVLWISSE KTSTKESCQA IKAYMDSTLG
     PFILNVTSAA LLCSEALCSG RGRCVRHPSY PEALLTLSPA SFSIEPTHDG RPLSLKGTLS
     LKDRAQMAMK FKCRCYRGWS GEWCKKQDM
 
 
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