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   03-AUG-2022, entry version 101.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   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 ovary
RT   cells: sequence alignment similarities to bacterial 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 cells:
RT   part I: cloning and expression of soluble sialidase in 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 cells:
RT   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) moieties from glycoproteins, oligosaccharides and gangliosides.
CC       {ECO:0000269|PubMed:11270813}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC         (2->8)- glycosidic linkages of terminal sialic acid residues in
CC         oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC         synthetic substrates.; EC=3.2.1.18;
CC         Evidence={ECO:0000269|PubMed:11270812, ECO:0000269|PubMed:11270813};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR   EMBL; U06143; AAA19746.1; -; mRNA.
DR   PIR; A54961; A54961.
DR   RefSeq; NP_001233664.1; NM_001246735.2.
DR   AlphaFoldDB; Q64393; -.
DR   SMR; Q64393; -.
DR   STRING; 10029.NP_001233664.1; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   Ensembl; ENSCGRT00001030356; ENSCGRP00001026110; ENSCGRG00001023529.
DR   GeneID; 100689301; -.
DR   KEGG; cge:100689301; -.
DR   CTD; 4759; -.
DR   eggNOG; ENOG502QSFT; Eukaryota.
DR   GeneTree; ENSGT00950000182944; -.
DR   OrthoDB; 652179at2759; -.
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; IPR011040; Sialidase.
DR   InterPro; IPR026945; Sialidase-2.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   PANTHER; PTHR10628:SF6; PTHR10628:SF6; 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
FT                   /note="Sialidase-2"
FT                   /id="PRO_0000208898"
FT   REPEAT          127..138
FT                   /note="BNR 1"
FT   REPEAT          197..208
FT                   /note="BNR 2"
FT   MOTIF           20..23
FT                   /note="FRIP motif"
FT   ACT_SITE        46
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000255"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="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