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Database: UniProt/SWISS-PROT
Entry: NEUR2_CRIGR
LinkDB: NEUR2_CRIGR
Original site: NEUR2_CRIGR 
ID   NEUR2_CRIGR             Reviewed;         379 AA.
AC   Q64393;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-MAY-2017, entry version 84.
DE   RecName: Full=Sialidase-2;
DE            EC=3.2.1.18;
DE   AltName: Full=Cytosolic sialidase;
DE   AltName: Full=N-acetyl-alpha-neuraminidase 2;
GN   Name=NEU2;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=7949662; DOI=10.1093/glycob/4.3.367;
RA   Ferrari J., Harris R., Warner T.G.;
RT   "Cloning and expression of a soluble sialidase from Chinese hamster
RT   ovary cells: sequence alignment similarities to bacterial
RT   sialidases.";
RL   Glycobiology 4:367-373(1994).
RN   [2]
RP   CATALYTIC ACTIVITY.
RX   PubMed=11270812; DOI=10.1016/S0008-6215(00)00294-9;
RA   Burg M., Muthing J.;
RT   "Characterization of cytosolic sialidase from Chinese hamster ovary
RT   cells: part I: cloning and expression of soluble sialidase in
RT   Escherichia coli.";
RL   Carbohydr. Res. 330:335-346(2001).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11270813; DOI=10.1016/S0008-6215(00)00295-0;
RA   Muthing J., Burg M.;
RT   "Characterization of cytosolic sialidase from Chinese hamster ovary
RT   cells: part II. Substrate specificity for gangliosides.";
RL   Carbohydr. Res. 330:347-356(2001).
CC   -!- FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic
CC       acid) moities from glycoproteins, oligosaccharides and
CC       gangliosides. {ECO:0000269|PubMed:11270813}.
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. {ECO:0000269|PubMed:11270812,
CC       ECO:0000269|PubMed:11270813}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000305}.
DR   EMBL; U06143; AAA19746.1; -; mRNA.
DR   PIR; A54961; A54961.
DR   RefSeq; NP_001233664.1; NM_001246735.2.
DR   ProteinModelPortal; Q64393; -.
DR   SMR; Q64393; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   GeneID; 100689301; -.
DR   KEGG; cge:100689301; -.
DR   CTD; 4759; -.
DR   HOVERGEN; HBG052608; -.
DR   KO; K12357; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006689; P:ganglioside catabolic process; ISS:UniProtKB.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB.
DR   InterPro; IPR026945; Sialidase-2.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR011040; Sialidases.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   PANTHER; PTHR10628:SF27; PTHR10628:SF27; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Repeat.
FT   CHAIN         1    379       Sialidase-2.
FT                                /FTId=PRO_0000208898.
FT   REPEAT      127    138       BNR 1.
FT   REPEAT      197    208       BNR 2.
FT   MOTIF        20     23       FRIP motif.
FT   ACT_SITE     46     46       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE    333    333       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    354    354       {ECO:0000255}.
FT   BINDING      21     21       Substrate. {ECO:0000250}.
FT   BINDING      41     41       Substrate. {ECO:0000250}.
FT   BINDING     179    179       Substrate. {ECO:0000250}.
FT   BINDING     181    181       Substrate. {ECO:0000250}.
FT   BINDING     218    218       Substrate. {ECO:0000250}.
FT   BINDING     237    237       Substrate. {ECO:0000255}.
FT   BINDING     303    303       Substrate. {ECO:0000250}.
SQ   SEQUENCE   379 AA;  41962 MW;  B5AFFBC6B6BE88B1 CRC64;
     MATCPVLQKE TLFQTGDYAY RIPALIYLSK QKTLLAFAEK RLTKTDEHAD LFVLRRGSYN
     ADTHQVQWQA EEVVTQAYLE GHRSMSPCPL YDKQTRTLFL FFIAVRGQIS EHHQLQTGVN
     VTRLCHITST DHGKTWSAVQ DLTDTTIGST HQDWATFGVG PGHCLQLRNT AGSLLVPAYA
     YRKQPPIHAP APSAFCFLSH DHGSTWELGH FVSQNSLECQ VAEVGTGAER VVYLNARSCL
     GARVQAQSPN SGLDFQDNQV VSKLVEPPKG CHGSVIAFPN PTSKADALDV WLLYTHPTDS
     RKRTNLGVYL NQKPLDPTTW SAPTLLATGI CAYSDLQNMG HGPDGSPQFG CLYESNNYEE
     IVFLMFTLKQ AFPAVFGAQ
//
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