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NEUR1_PIG
ID   NEUR1_PIG               Reviewed;         416 AA.
AC   A5PF10;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, 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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (JUN-2007) 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; AL773527; CAN87707.1; -; Genomic_DNA.
DR   RefSeq; NP_001095292.1; NM_001101822.1.
DR   AlphaFoldDB; A5PF10; -.
DR   SMR; A5PF10; -.
DR   STRING; 9823.ENSSSCP00000001513; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   PaxDb; A5PF10; -.
DR   PeptideAtlas; A5PF10; -.
DR   PRIDE; A5PF10; -.
DR   Ensembl; ENSSSCT00070046815; ENSSSCP00070039491; ENSSSCG00070023485.
DR   GeneID; 100124381; -.
DR   KEGG; ssc:100124381; -.
DR   CTD; 4758; -.
DR   eggNOG; ENOG502QSIT; Eukaryota.
DR   InParanoid; A5PF10; -.
DR   OrthoDB; 652179at2759; -.
DR   Reactome; R-SSC-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-SSC-4085001; Sialic acid metabolism.
DR   Reactome; R-SSC-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 7.
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   3: Inferred from homology;
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..48
FT                   /evidence="ECO:0000250"
FT   CHAIN           49..416
FT                   /note="Sialidase-1"
FT                   /id="PRO_0000304727"
FT   REPEAT          113..124
FT                   /note="BNR 1"
FT   REPEAT          173..184
FT                   /note="BNR 2"
FT   REPEAT          232..243
FT                   /note="BNR 3"
FT   REPEAT          348..359
FT                   /note="BNR 4"
FT   MOTIF           78..81
FT                   /note="FRIP motif"
FT   MOTIF           413..416
FT                   /note="Internalization signal"
FT   ACT_SITE        104
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        371
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        395
FT                   /evidence="ECO:0000255"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   416 AA;  45159 MW;  65E99172C69F3EB8 CRC64;
     MTAERPGAVP LGRPGRPPML GLGEAYRAQV FASIFLLLLS PAGVGARAKN DFNLVHPLVT
     MEQLLWVSGK QIGSVDTFRI PLITTTPRGT LLAFAEARKM SASDKGAKFI ALRRSMDQGS
     TWSPTAFIVD DGETPDGLNL GAVVSDTTTG VVFLFYSLCA HKAGCRVAST MLVWSKDDGI
     SWSSPRNLSL DIGTEMFAPG PGSGIQKQWA PQKGRLIVCG HGTLERDGVF CLLSDDHGAS
     WRYGSGISGI PYGQPKREND FNPDECQPYE LPDGSVVINA RNQNNYHCRC RIVLRSYDAC
     DTLRPRDVTF DPELVDPVVA AGAVATSSGI IFFSNPAHPE FRVNLTLRWS FSNGTSWRKE
     TVQIWPGPSG YSSLATLEGS VGGEDQAPQL YVLYEKGRNR YTESISLAKV SVYGTL
 
 
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