GenomeNet

Database: UniProt
Entry: G5BZZ2_HETGA
LinkDB: G5BZZ2_HETGA
Original site: G5BZZ2_HETGA 
ID   G5BZZ2_HETGA            Unreviewed;       448 AA.
AC   G5BZZ2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   08-MAY-2019, entry version 40.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
DE   AltName: Full=Hyaluronoglucosaminidase {ECO:0000256|RuleBase:RU610713};
GN   Name=HYAL1 {ECO:0000313|EMBL:JAN98609.1};
GN   ORFNames=GW7_19947 {ECO:0000313|EMBL:EHB14834.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Bathyergidae; Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB14834.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB14834.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L.,
RA   Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L.,
RA   Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of
RT   the naked mole rat.";
RL   Nature 479:223-227(2011).
RN   [2] {ECO:0000313|EMBL:JAN98609.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:JAN98609.1};
RA   Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA   Platzer M., Szafranski K.;
RT   "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; JH172617; EHB14834.1; -; Genomic_DNA.
DR   EMBL; GEBF01005023; JAN98609.1; -; Transcribed_RNA.
DR   InParanoid; G5BZZ2; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
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:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR   GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IEA:Ensembl.
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   GO; GO:0046718; P:viral entry into host cell; IEA:GOC.
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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006813};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     36       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        37    448       Hyaluronidase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007661008.
FT   ACT_SITE    145    145       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   CARBOHYD    364    364       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000256|PIRSR:PIRSR038193-2}.
FT   DISULFID     57    347       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    221    235       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    372    383       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    377    432       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    434    443       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   448 AA;  49935 MW;  71C23CE099642716 CRC64;
     MKPFSPEVSP HPPHVITAHL LQICTLFLIL LDMTSSRGPV VPNQPFTTIW NADTQRCLKN
     YSVDVDVSIF DVVANPGQTF HGPNMTIFYS SELGTYPYYT ATGEPVFGGL PQNASLSEHL
     AYTFHDIQAA MPAPDFSGLV VIDWEAWRPR WAFNWDTKDI YRERSQALIQ AQHPDWPESR
     VKTVAKDQFQ EAARAWMAGT LQLGQTLRPH GLWGFYGLPD CYNYDFKSPN YTGQCPLGIL
     PENDQLGWLW NQSRALYPSI YIPAALIGTG MTQKYVRHRV GEAFRVARTA SNPSLPVLPY
     IQIFYDTTNH LLPLEELEHT LGESAAQGAA GVVFWVSSED TNSKESCQAI KEYMDTTLGP
     FILNVTSGAL LCSQALCSGH GRCARHPNHP EALLILNPAS FSIQFTPGGK PLTLKGGPSL
     EDQAQMAMKF RCRCYRGWRG AFCGQPDV
//
DBGET integrated database retrieval system