NEUR2_RAT
ID NEUR2_RAT Reviewed; 379 AA.
AC Q64627; Q63705;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Sialidase-2;
DE EC=3.2.1.18 {ECO:0000269|PubMed:8253770};
DE AltName: Full=Cytosolic sialidase;
DE AltName: Full=N-acetyl-alpha-neuraminidase 2;
GN Name=Neu2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Skeletal muscle;
RX PubMed=8253770; DOI=10.1016/s0021-9258(19)74333-6;
RA Miyagi T., Konno K., Emori Y., Kawasaki H., Suzuki K., Yasui A., Tsuiki S.;
RT "Molecular cloning and expression of cDNA encoding rat skeletal muscle
RT cytosolic sialidase.";
RL J. Biol. Chem. 268:26435-26440(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8563137; DOI=10.1093/glycob/5.5.511;
RA Sato K., Miyagi T.;
RT "Genomic organization and the 5'-upstream sequence of the rat cytosolic
RT sialidase gene.";
RL Glycobiology 5:511-516(1995).
CC -!- FUNCTION: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of
CC the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan
CC moiety in the catabolism of glycolipids, glycoproteins and
CC oligosacharides. Recognizes sialyl linkage positions of the glycan
CC moiety as well as the supramolecular organization of the
CC sialoglycoconjugate. Displays preference for alpha-(2->3)-sialylated
CC GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both
CC monomeric forms and micelles. Hydrolyzes monomeric GM1 ganglioside, but
CC has no activity toward the miscellar form. Has lower sialidase activity
CC for glycoproteins such as fetuin and TF/transferrin that carry a
CC mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages. Cleaves milk
CC oligosaccharide alpha-(2->3)-sialyllactose, but is inactive toward
CC alpha-(2->6)-sialyllactose isomer. Has no activity toward colominic
CC acid, a homomer of alpha-(2->8)-linked Neu5Ac residues.
CC {ECO:0000250|UniProtKB:Q9Y3R4}.
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:8253770};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD1a + H2O = ganglioside GM1 + N-
CC acetylneuraminate; Xref=Rhea:RHEA:47832, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:82637, ChEBI:CHEBI:82639;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47833;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM1 + H2O = ganglioside GA1 + N-acetylneuraminate;
CC Xref=Rhea:RHEA:47872, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418,
CC ChEBI:CHEBI:82639, ChEBI:CHEBI:88069;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47873;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GT1b + H2O = ganglioside GD1b + N-
CC acetylneuraminate; Xref=Rhea:RHEA:47828, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:82939, ChEBI:CHEBI:82940;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47829;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD1b + H2O = ganglioside GM1 + N-
CC acetylneuraminate; Xref=Rhea:RHEA:47876, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:82639, ChEBI:CHEBI:82939;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47877;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD3 + H2O = ganglioside GM3 + N-acetylneuraminate;
CC Xref=Rhea:RHEA:48120, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418,
CC ChEBI:CHEBI:79210, ChEBI:CHEBI:79214;
CC Evidence={ECO:0000250|UniProtKB:Q9JMH3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48121;
CC Evidence={ECO:0000250|UniProtKB:Q9JMH3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM3 + H2O = beta-D-galactosyl-(1->4)-beta-D-
CC glucosyl-(1<->1)-ceramide + N-acetylneuraminate;
CC Xref=Rhea:RHEA:48136, ChEBI:CHEBI:15377, ChEBI:CHEBI:35418,
CC ChEBI:CHEBI:79208, ChEBI:CHEBI:79210;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48137;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 + H2O = N-acetyl-beta-D-galactosaminyl-(1->4)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-
CC acetylneuraminate; Xref=Rhea:RHEA:48172, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:79218, ChEBI:CHEBI:90085;
CC Evidence={ECO:0000250|UniProtKB:Q9JMH3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48173;
CC Evidence={ECO:0000250|UniProtKB:Q9JMH3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-NeuAc-nLc4Cer(d18:1(4E)) + H2O = a
CC neolactoside nLc4Cer(d18:1(4E)) + N-acetylneuraminate;
CC Xref=Rhea:RHEA:47852, ChEBI:CHEBI:15377, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:58665;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47853;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC (1->4)-D-glucose = lactose + N-acetylneuraminate;
CC Xref=Rhea:RHEA:64640, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716,
CC ChEBI:CHEBI:35418, ChEBI:CHEBI:156068;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64641;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3R4};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Y3R4}.
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle.
CC {ECO:0000269|PubMed:8253770}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR EMBL; D16300; BAA03805.1; -; mRNA.
DR EMBL; D50606; BAA09169.1; -; Genomic_DNA.
DR PIR; A49679; A49679.
DR AlphaFoldDB; Q64627; -.
DR SMR; Q64627; -.
DR STRING; 10116.ENSRNOP00000022818; -.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR PhosphoSitePlus; Q64627; -.
DR PaxDb; Q64627; -.
DR UCSC; RGD:3164; rat.
DR RGD; 3164; Neu2.
DR eggNOG; ENOG502QSFT; Eukaryota.
DR InParanoid; Q64627; -.
DR PhylomeDB; Q64627; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR PRO; PR:Q64627; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; ISO:RGD.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IDA:RGD.
DR GO; GO:0051692; P:cellular oligosaccharide catabolic process; ISO:RGD.
DR GO; GO:0006689; P:ganglioside catabolic process; ISS:UniProtKB.
DR GO; GO:0006516; P:glycoprotein catabolic process; ISO:RGD.
DR GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:RGD.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
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; Reference proteome; Repeat.
FT CHAIN 1..379
FT /note="Sialidase-2"
FT /id="PRO_0000208901"
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; 42382 MW; 55583C7043CA9784 CRC64;
METCPVLQKE TLFHTEVYAY RIPALLYLKK QKTLLAFAEK RASRTDEHAE LIVLRRGSYN
GATNHVKWQP EEVVTQAQLE GHRSMNPCPL YDKQTKTLFL FFIAVPGRVS EQHQLQTRVN
VTRLCRVTST DYGMNWSPVQ DLTETTIGST HQDWATFAVG PGHCLQLRNR AGSLLVPAYA
YRKLHPVHKP TPFAFCFISL DHGHTWELGN FVSENSLECQ VAEVGTGAHR VVYLNARSFI
GARVQAQSPN DGLDFQDNQV VSKLVEPPHG CHGSVVAFHS PTSKPDCLRH VAAYTHPTDS
RNRTNLGVYL NQTPLDPTAW SEPTLLATGT CAYSDLQIWG LGPDGSPQFG CLYESGNYDE
IIFLMFTLKQ AFPTVHGAQ
