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Database: UniProt
Entry: E2R560_CANLF
LinkDB: E2R560_CANLF
Original site: E2R560_CANLF 
ID   E2R560_CANLF            Unreviewed;       476 AA.
AC   E2R560;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 2.
DT   08-MAY-2019, entry version 60.
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=HYAL2 {ECO:0000313|Ensembl:ENSCAFP00000015681,
GN   ECO:0000313|VGNC:VGNC:41843};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000015681, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000015681, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000015681,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000015681}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000015681};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
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}.
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DR   EMBL; AAEX03012222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; E2R560; -.
DR   STRING; 9612.ENSCAFP00000015681; -.
DR   PaxDb; E2R560; -.
DR   Ensembl; ENSCAFT00000016952; ENSCAFP00000015681; ENSCAFG00000010657.
DR   VGNC; VGNC:41843; HYAL2.
DR   eggNOG; ENOG410IECJ; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   GeneTree; ENSGT00950000182708; -.
DR   InParanoid; E2R560; -.
DR   OMA; GGEQCQW; -.
DR   TreeFam; TF321598; -.
DR   Reactome; R-CFA-2160916; Hyaluronan uptake and degradation.
DR   Proteomes; UP000002254; Chromosome 20.
DR   Bgee; ENSCAFG00000010657; Expressed in 3 organ(s), highest expression level in adult mammalian kidney.
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 factor 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:UniProtKB-UniRule.
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:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
DR   GO; GO:2000484; P:positive regulation of interleukin-8 secretion; 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:0019087; P:transformation of host cell by virus; ISS:UniProtKB.
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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
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:UP000002254};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    476       Hyaluronidase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003163075.
FT   ACT_SITE    134    134       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   CARBOHYD    360    360       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000256|PIRSR:PIRSR038193-2}.
FT   DISULFID     46    343       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    210    226       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    368    379       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    373    430       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    432    441       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   476 AA;  53889 MW;  163638D9512E4E71 CRC64;
     MWAGLGPAVT LALVVVAWAA QLKPTAPPIF TGRPFVVAWD VPTQDCGPRL KVPLDLKAFD
     VQASPNEGFV NQNITIFYHD RLGLYPRFSS VGRSVHGGVP QNGSLWAHLK MLQEHVEHYI
     RSQEPAGLAV IDWEDWRPVW VRNWQDKDIY RQSSRQLVAV RHPDWPADRV VKQAQYEFEF
     AARQFMLETL RFVKAVRPRH LWGFYLFPDC YNHDYVQNWE TYTGRCPDVE VSRNDQLAWL
     WAESTALFPS VYLDETLASS THGRNFVSFR VQEALRVAHT HHANHALPVY VFTRPTYSRR
     LTGLSEVQMD LISTIGESAA LGAAGVILWG DAGYTTSTVQ ETCQYLKDYL KRLLVPYVVN
     VSWAAQYCSW AQCHGHGRCV RRDPSANTFL HLSASSFRLV PSHVPGEPQL RPEGELSWAD
     LNHLQTHFRC QCYLGWGGEQ CQWDHTRAAG GARGAWAGSH LTGPLAVAAL VLTWTS
//
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