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Database: UniProt/SWISS-PROT
Entry: NEUR3_RAT
LinkDB: NEUR3_RAT
Original site: NEUR3_RAT 
ID   NEUR3_RAT               Reviewed;         418 AA.
AC   Q99PW5; Q497C0;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   22-NOV-2017, entry version 109.
DE   RecName: Full=Sialidase-3;
DE            EC=3.2.1.18;
DE   AltName: Full=Ganglioside sialidase;
DE   AltName: Full=Membrane sialidase;
DE   AltName: Full=N-acetyl-alpha-neuraminidase 3;
GN   Name=Neu3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=11162581; DOI=10.1006/bbrc.2000.4186;
RA   Hasegawa T., Feijoo Carnero C., Wada T., Itoyama Y., Miyagi T.;
RT   "Differential expression of three sialidase genes in rat
RT   development.";
RL   Biochem. Biophys. Res. Commun. 280:726-732(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in modulating the ganglioside content of
CC       the lipid bilayer at the level of membrane-bound sialyl
CC       glycoconjugates. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
CC       alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
CC       in oligosaccharides, glycoproteins, glycolipids, colominic acid
CC       and synthetic substrates.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, cardiac muscle and weakly
CC       in liver.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000305}.
DR   EMBL; AB026841; BAB32440.1; -; mRNA.
DR   EMBL; BC100625; AAI00626.1; -; mRNA.
DR   PIR; JC7588; JC7588.
DR   RefSeq; NP_446462.1; NM_054010.1.
DR   RefSeq; XP_008757887.1; XM_008759665.2.
DR   UniGene; Rn.67067; -.
DR   ProteinModelPortal; Q99PW5; -.
DR   SMR; Q99PW5; -.
DR   STRING; 10116.ENSRNOP00000024420; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   PhosphoSitePlus; Q99PW5; -.
DR   PaxDb; Q99PW5; -.
DR   PRIDE; Q99PW5; -.
DR   Ensembl; ENSRNOT00000024420; ENSRNOP00000024420; ENSRNOG00000018106.
DR   GeneID; 117185; -.
DR   KEGG; rno:117185; -.
DR   UCSC; RGD:619881; rat.
DR   CTD; 10825; -.
DR   RGD; 619881; Neu3.
DR   eggNOG; ENOG410IFVF; Eukaryota.
DR   eggNOG; ENOG410Y74Z; LUCA.
DR   GeneTree; ENSGT00390000011171; -.
DR   HOGENOM; HOG000233778; -.
DR   HOVERGEN; HBG052608; -.
DR   InParanoid; Q99PW5; -.
DR   KO; K12357; -.
DR   OMA; HSLMIYS; -.
DR   OrthoDB; EOG091G08BI; -.
DR   PhylomeDB; Q99PW5; -.
DR   TreeFam; TF331063; -.
DR   Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-RNO-4085001; Sialic acid metabolism.
DR   PRO; PR:Q99PW5; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018106; -.
DR   Genevisible; Q99PW5; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016997; F:alpha-sialidase activity; ISO:RGD.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; ISS:UniProtKB.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; ISS:UniProtKB.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; ISO:RGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISO:RGD.
DR   GO; GO:0006689; P:ganglioside catabolic process; ISS:UniProtKB.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; ISO:RGD.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026944; Sialidase-3.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   PANTHER; PTHR10628:SF23; PTHR10628:SF23; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; SSF50939; 2.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell membrane; Complete proteome;
KW   Glycosidase; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Repeat.
FT   CHAIN         1    418       Sialidase-3.
FT                                /FTId=PRO_0000208905.
FT   REPEAT      129    140       BNR 1.
FT   REPEAT      201    212       BNR 2.
FT   REPEAT      252    263       BNR 3.
FT   MOTIF        24     27       FRIP motif.
FT   ACT_SITE     50     50       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE    369    369       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    386    386       {ECO:0000255}.
FT   BINDING      25     25       Substrate. {ECO:0000250}.
FT   BINDING      45     45       Substrate. {ECO:0000250}.
FT   BINDING     179    179       Substrate. {ECO:0000250}.
FT   BINDING     181    181       Substrate. {ECO:0000250}.
FT   BINDING     223    223       Substrate. {ECO:0000250}.
FT   BINDING     243    243       Substrate. {ECO:0000255}.
FT   BINDING     339    339       Substrate. {ECO:0000250}.
SQ   SEQUENCE   418 AA;  46980 MW;  7CC46F2E5952E240 CRC64;
     MEEVSSCSLR STLFQQEEQN RITYRIPALL YIPPTHTFLA FAEMRTSSRD EDAVYLVFRR
     GVMKGCSVEW GPQQPLMEAT LPGHRTMSPC PVWEKNTGRV YLFFICVQGH VSERWQLLWG
     RNAARLCFLY SEDSGCSWGE VKDLTEEVVG SEMKHWATFA VGPGHGIQLQ SGRLLIPAYA
     YLISCWFLCF PCSVKPHSLM FYSDDLGVTW HCGKFIKPQV TGECQVAEVP GKAGNLVLYC
     SARTPNKFRA EAFSTDSGDC FQKPTLNQQL CEPRGGCQGS VVSTRPLKMP YTCQDSSGKD
     VPSTQKCPLM DRSLEVEEGA GAPSGTWLLY SHPTNKKKRM NLGIYYNQNP LEVNYWSRPW
     ILNRGPSGYS DLAVVEGQGL FACLFECGER HEDEKIDFCL FSDQEVLSCD DCTSPSSN
//
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