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Database: UniProt
Entry: E2RCK6_CANLF
LinkDB: E2RCK6_CANLF
Original site: E2RCK6_CANLF 
ID   E2RCK6_CANLF            Unreviewed;       541 AA.
AC   E2RCK6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 2.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Hyaluronidase {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|PIRNR:PIRNR038193, ECO:0000256|RuleBase:RU610713};
GN   Name=SPAM1 {ECO:0000313|Ensembl:ENSCAFP00000002566,
GN   ECO:0000313|VGNC:VGNC:46700};
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:ENSCAFP00000002566, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000002566, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000002566,
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:ENSCAFP00000002566}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000002566};
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|PIRNR:PIRNR038193,
CC         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; AAEX03009283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005628499.1; XM_005628442.2.
DR   RefSeq; XP_005628500.1; XM_005628443.1.
DR   RefSeq; XP_532443.1; XM_532443.5.
DR   SMR; E2RCK6; -.
DR   STRING; 9612.ENSCAFP00000002566; -.
DR   PaxDb; E2RCK6; -.
DR   Ensembl; ENSCAFT00000002767; ENSCAFP00000002566; ENSCAFG00000001765.
DR   GeneID; 475211; -.
DR   KEGG; cfa:475211; -.
DR   CTD; 6677; -.
DR   VGNC; VGNC:46700; SPAM1.
DR   eggNOG; ENOG410IECJ; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   GeneTree; ENSGT00950000182708; -.
DR   InParanoid; E2RCK6; -.
DR   KO; K01197; -.
DR   OMA; RNNELNW; -.
DR   OrthoDB; 1096692at2759; -.
DR   TreeFam; TF321598; -.
DR   Reactome; R-CFA-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR   Proteomes; UP000002254; Chromosome 14.
DR   Bgee; ENSCAFG00000001765; Expressed in 1 organ(s), highest expression level in liver.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 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|PIRNR:PIRNR038193,
KW   ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038193,
KW   ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254}.
FT   CARBOHYD    369    369       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000256|PIRSR:PIRSR038193-2}.
FT   DISULFID     60    352       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    224    238       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    377    388       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    382    436       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    438    444       {ECO:0000256|PIRSR:PIRSR038193-3}.
SQ   SEQUENCE   541 AA;  61746 MW;  7ED061BCFD7AF35B CRC64;
     MGVLRFQNIF FRSFLGSSGT TQALFIFLLI PCCLTQEFRA PPFIPGVSFL WGWNAPTELC
     AKRFNVQLDL NLFSLIGSPL KGVIGQGIAL FYSDRLGYYP HINKTTGKIV NGGIPQLGSL
     KKHLDKAKKD ISHYIETDSV GLAVIDWDCW RPNWERNWRP KHIYKEQSID LAQQQHIHLN
     LTEVTKIAKA DFEKAGKCFM QETLKLGKFL RPNYLWGFYL YPDCYNYNYK SPNYNGSCFD
     IEQRRNDEIN WLWKESTALF PSIYLNSKLK SSPFAALYVR NRVLEAIRVS KVKNVKHPLP
     IFVYARPVFT DVLLKYLTEE DLVNTIGESV SLGVSGMVMW GSLNLTQNVQ ICTELDAYIK
     NKLNPYIINV TLAAKMCSQV LCQDQGVCIR KHWNSNDYLH LNPVNFAIQL ERSGRYTVQG
     KPTLEDLQLF SKKFYCACYA NTQCKERVDL TDIHTVKVCV GEDVCIDVYL NSVPSGHPSD
     WKGKYVTSSN IFSAMPPPAT GPPCVPGRDL NRCLKARFIV EDNSKTTQTG YQSIHIKNKK
     Q
//
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