NEUR1_BOVIN
ID NEUR1_BOVIN Reviewed; 415 AA.
AC A6BMK7; A4IFG6; Q5D0G1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Sialidase-1;
DE EC=3.2.1.18;
DE AltName: Full=Acetylneuraminyl hydrolase;
DE AltName: Full=Lysosomal sialidase;
DE AltName: Full=N-acetyl-alpha-neuraminidase 1;
DE Flags: Precursor;
GN Name=NEU1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Masoudi A.A., Yamato O., Kunieda T.;
RT "Evaluation of PPGB and NEU1 genes as candidates for the lysosomal storage
RT disorder in Japanese black cattle.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-205.
RA Heaton M.P., Clawson M.L., Snelling W.M., Keele J.W., Harhay G.P.,
RA Wiedmann R.T., Bennett G.L., Smith T.P.L., Stone R.T., Freking B.A.,
RA Van Tassell C.P., Sonstegard T.S., Gasbarre L.C., Carr J., DiBello P.,
RA Kumar M., Lee M.S., Murthy J., Otto J., Salisbury B., Schulz V., Tracy R.,
RA Hawk D.A., Kalbfleisch T., Laegreid W.W.;
RT "Estimating probability of parentage in U.S. beef and dairy cattle with
RT single nucleotide polymorphisms.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
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 -!- 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:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Lysosome
CC lumen {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Note=Localized not only on the inner side of the
CC lysosomal membrane and in the lysosomal lumen, but also on the plasma
CC membrane and in intracellular vesicles. {ECO:0000250}.
CC -!- DOMAIN: A C-terminal internalization signal (YGTL) appears to allow the
CC targeting of plasma membrane proteins to endosomes. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylation of tyrosine within the internalization signal
CC results in inhibition of sialidase internalization and blockage on the
CC plasma membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR EMBL; AB327106; BAF64705.1; -; Genomic_DNA.
DR EMBL; BC134571; AAI34572.1; -; mRNA.
DR EMBL; AY937242; AAX14675.1; -; Genomic_DNA.
DR RefSeq; NP_001077111.1; NM_001083642.1.
DR AlphaFoldDB; A6BMK7; -.
DR SMR; A6BMK7; -.
DR STRING; 9913.ENSBTAP00000007454; -.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR PaxDb; A6BMK7; -.
DR Ensembl; ENSBTAT00000007454; ENSBTAP00000007454; ENSBTAG00000005674.
DR GeneID; 505554; -.
DR KEGG; bta:505554; -.
DR CTD; 4758; -.
DR VEuPathDB; HostDB:ENSBTAG00000005674; -.
DR VGNC; VGNC:50230; NEU1.
DR eggNOG; ENOG502QSIT; Eukaryota.
DR GeneTree; ENSGT00950000182944; -.
DR HOGENOM; CLU_024620_3_0_1; -.
DR InParanoid; A6BMK7; -.
DR OrthoDB; 652179at2759; -.
DR TreeFam; TF331063; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000005674; Expressed in ileocecal valve and 105 other tissues.
DR ExpressionAtlas; A6BMK7; baseline.
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; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript 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..47
FT /evidence="ECO:0000250"
FT CHAIN 48..415
FT /note="Sialidase-1"
FT /id="PRO_0000304726"
FT REPEAT 112..123
FT /note="BNR 1"
FT REPEAT 172..183
FT /note="BNR 2"
FT REPEAT 231..242
FT /note="BNR 3"
FT REPEAT 347..358
FT /note="BNR 4"
FT MOTIF 77..80
FT /note="FRIP motif"
FT MOTIF 412..415
FT /note="Internalization signal"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 370
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 410
FT /note="S -> G (in Ref. 1; BAF64705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45433 MW; F670909AF7046428 CRC64;
MTEEGPGIVS LGKLRRPRML RLWGICRVQI FSAIFMLMSP AGVGAGAKDD FSLVHPLVTM
EQLLWVSGKQ IGSVDTFRIP LITTTPRGTL LAFAEARKMS TSDKGAKFIA LRRSMDQGST
WSPTAFIVDD GETPDGLNLG AVVSDTTTGV VFLFYSLCAH KAGCQVASTM LVWSKDDGVS
WSSPRNLSLD IGTEMFAPGP GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGVSW
RYGGGVSGIP YGQPKRENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IILRSYDACD
TLRPRDVTFD TELVDPVVAA GAVATSSGIV FFSNPAHPEF RVNLTLRWSF SNGTSWRKET
VQLWPGPSGY SSLTTLEGNV DGKDEAPQLY VLYEKGRNQY MESISLVKVS VYGTL
