NEUR1_PONAB
ID NEUR1_PONAB Reviewed; 415 AA.
AC Q5RAF4; Q5RA14; Q5RF22;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, Heart, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RAF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RAF4-2; Sequence=VSP_028119;
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: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; CR857339; CAH89635.1; -; mRNA.
DR EMBL; CR859063; CAH91256.1; -; mRNA.
DR EMBL; CR859212; CAH91396.1; -; mRNA.
DR RefSeq; NP_001125743.1; NM_001132271.1. [Q5RAF4-1]
DR RefSeq; NP_001128939.1; NM_001135467.1.
DR AlphaFoldDB; Q5RAF4; -.
DR SMR; Q5RAF4; -.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR GeneID; 100172668; -.
DR KEGG; pon:100172668; -.
DR CTD; 4758; -.
DR InParanoid; Q5RAF4; -.
DR OrthoDB; 652179at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
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: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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 Alternative splicing; Carbohydrate metabolism; Cell membrane;
KW Cytoplasmic vesicle; Glycoprotein; Glycosidase; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..47
FT /evidence="ECO:0000250"
FT CHAIN 48..415
FT /note="Sialidase-1"
FT /id="PRO_0000304728"
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 VAR_SEQ 267..414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028119"
FT CONFLICT 5
FT /note="R -> Q (in Ref. 1; CAH89635/CAH91396)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="D -> G (in Ref. 1; CAH89635/CAH91396)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="W -> R (in Ref. 1; CAH89635/CAH91396)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="L -> P (in Ref. 1; CAH91396)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="Q -> H (in Ref. 1; CAH89635/CAH91396)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="L -> P (in Ref. 1; CAH89635)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="V -> M (in Ref. 1; CAH89635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45467 MW; 360E60A256DEA07F CRC64;
MTGERPSTAL PDRRWGPRIL GFWGGCRVWV FAAIFLLLSL AASWSKAEND FGLVQPLVTM
EQLLWVSGRQ IGSVDTFRIP LITATPRGTL LAFAEARKMS SSDEGAKFIA LRRSMDQGST
WSPTAFIVND GDVPDGLNLG AVVSDVETGV VFLFYSLCAH KAGCQVASTM LVWSKDDGVS
WSTPRNLSLD IGTEVFAPGP GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGASW
RYGSGVSGIP YGQPKQENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IVLRSYDACD
TLRPRDVTFD PELVDPVVAA GAVVTSSGIV FFSNPAHPEF RVNLTLRWSF SNGTSWRKET
VQLWPGPSGY SSLATLEGSM DGEEQAPQLY VLYEKGRNHY TESISVAKIS VYGTL
