NEUR1_RAT
ID NEUR1_RAT Reviewed; 409 AA.
AC Q99PW3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sialidase-1;
DE EC=3.2.1.18;
DE AltName: Full=Lysosomal sialidase;
DE AltName: Full=N-acetyl-alpha-neuraminidase 1;
DE Flags: Precursor;
GN Name=Neu1;
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], FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
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 development.";
RL Biochem. Biophys. Res. Commun. 280:726-732(2001).
CC -!- FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic
CC acid) moieties from glycoproteins and glycolipids. To be active, it is
CC strictly dependent on its presence in the multienzyme complex. Appears
CC to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.
CC {ECO:0000269|PubMed:11162581}.
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:11162581};
CC -!- SUBUNIT: Interacts with cathepsin A (protective protein), beta-
CC galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a
CC multienzyme complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:11162581};
CC Peripheral membrane protein {ECO:0000269|PubMed:11162581}; Lumenal side
CC {ECO:0000269|PubMed:11162581}. Lysosome lumen
CC {ECO:0000269|PubMed:11162581}. Cell membrane
CC {ECO:0000269|PubMed:11162581}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:11162581}. Note=Localized not only on the inner
CC side of the lysosomal membrane and in the lysosomal lumen, but also on
CC the plasma membrane and in intracellular vesicles.
CC -!- DOMAIN: A C-terminal internalization signal (YGTL) appears to allow the
CC targeting of plasma membrane proteins to endosomes.
CC -!- PTM: N-glycosylated. {ECO:0000305}.
CC -!- PTM: Phosphorylation of tyrosine within the internalization signal
CC results in inhibition of sialidase internalization and blockage on the
CC plasma membrane.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR EMBL; AB035722; BAB21443.1; -; mRNA.
DR AlphaFoldDB; Q99PW3; -.
DR SMR; Q99PW3; -.
DR IntAct; Q99PW3; 1.
DR STRING; 10116.ENSRNOP00000050614; -.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR GlyGen; Q99PW3; 4 sites.
DR PaxDb; Q99PW3; -.
DR UCSC; RGD:3163; rat.
DR RGD; 3163; Neu1.
DR eggNOG; ENOG502QSIT; Eukaryota.
DR InParanoid; Q99PW3; -.
DR PhylomeDB; Q99PW3; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q99PW3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016997; F:alpha-sialidase activity; ISO:RGD.
DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
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:0004308; F:exo-alpha-sialidase activity; IDA:RGD.
DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:2000291; P:regulation of myoblast proliferation; IMP:RGD.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR10628; PTHR10628; 1.
DR Pfam; PF13088; BNR_2; 1.
DR SUPFAM; SSF50939; SSF50939; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Cytoplasmic vesicle; Glycoprotein;
KW Glycosidase; Hydrolase; Lipid degradation; Lipid metabolism; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..409
FT /note="Sialidase-1"
FT /id="PRO_0000012028"
FT REPEAT 106..117
FT /note="BNR 1"
FT REPEAT 166..177
FT /note="BNR 2"
FT REPEAT 225..236
FT /note="BNR 3"
FT REPEAT 341..352
FT /note="BNR 4"
FT MOTIF 71..74
FT /note="FRIP motif"
FT MOTIF 406..409
FT /note="Internalization signal"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 258
FT /evidence="ECO:0000255"
FT ACT_SITE 364
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /evidence="ECO:0000255"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 409 AA; 44695 MW; F912FA1E1F0991A9 CRC64;
MVGAEPSRPP GPPSYWTGRR GQGLAAIFLL LVSAAGSEAR TEDDFSLVQP LVTMEQLLWV
SGKQIGSVDT FRIPLITATP RGTLLAFAEA RKKSASDEGA KFIAMRRSTD QGSTWSSTAF
IVDDGEASDG LNLGAVVNDV DTGVVFLIYT LCAHKVNCQV ASTMLVWSKD DGVSWSPPRN
LSVDIGTEMF APGPGSGIQK QREPWKGRLI VCGHGTLERD GVFCLLSDDH GASWHYGTGV
SGIPFGQPKH DHDFNPDECQ PYELPDGSVI INARNQNNYH CRCRIVLRSY DACDTLRPRD
VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEYRVNLTL RWSFSNGTFW QKERVQLWPG
PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM VKISVYGTL
