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NPTX1_MOUSE
ID   NPTX1_MOUSE             Reviewed;         432 AA.
AC   Q62443;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Neuronal pentraxin-1;
DE            Short=NP1;
DE   AltName: Full=Neuronal pentraxin I;
DE            Short=NP-I;
DE   Flags: Precursor;
GN   Name=Nptx1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8884281; DOI=10.1006/geno.1996.0503;
RA   Omeis I.A., Hsu Y.-C., Perin M.S.;
RT   "Mouse and human neuronal pentraxin 1 (NPTX1): conservation, genomic
RT   structure, and chromosomal localization.";
RL   Genomics 36:543-545(1996).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be involved in mediating uptake of synaptic material
CC       during synapse remodeling or in mediating the synaptic clustering of
CC       AMPA glutamate receptors at a subset of excitatory synapses.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homooligomer or heterooligomer (probably pentamer) with
CC       neuronal pentraxin receptor (NPTXR). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000305}.
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DR   EMBL; U62021; AAC52826.1; -; Genomic_DNA.
DR   CCDS; CCDS25719.1; -.
DR   RefSeq; NP_032756.1; NM_008730.2.
DR   AlphaFoldDB; Q62443; -.
DR   SMR; Q62443; -.
DR   BioGRID; 201833; 4.
DR   IntAct; Q62443; 2.
DR   MINT; Q62443; -.
DR   STRING; 10090.ENSMUSP00000026670; -.
DR   GlyConnect; 2552; 11 N-Linked glycans (2 sites).
DR   GlyGen; Q62443; 2 sites, 11 N-linked glycans (2 sites).
DR   PhosphoSitePlus; Q62443; -.
DR   MaxQB; Q62443; -.
DR   PaxDb; Q62443; -.
DR   PRIDE; Q62443; -.
DR   ProteomicsDB; 293882; -.
DR   Antibodypedia; 32766; 411 antibodies from 32 providers.
DR   DNASU; 18164; -.
DR   Ensembl; ENSMUST00000026670; ENSMUSP00000026670; ENSMUSG00000025582.
DR   GeneID; 18164; -.
DR   KEGG; mmu:18164; -.
DR   UCSC; uc007mqv.1; mouse.
DR   CTD; 4884; -.
DR   MGI; MGI:107811; Nptx1.
DR   VEuPathDB; HostDB:ENSMUSG00000025582; -.
DR   eggNOG; ENOG502QTID; Eukaryota.
DR   GeneTree; ENSGT01050000244805; -.
DR   HOGENOM; CLU_032051_0_0_1; -.
DR   InParanoid; Q62443; -.
DR   OMA; AQNFGQT; -.
DR   OrthoDB; 770812at2759; -.
DR   PhylomeDB; Q62443; -.
DR   TreeFam; TF330208; -.
DR   BioGRID-ORCS; 18164; 0 hits in 72 CRISPR screens.
DR   PRO; PR:Q62443; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q62443; protein.
DR   Bgee; ENSMUSG00000025582; Expressed in cerebellum lobe and 142 other tissues.
DR   ExpressionAtlas; Q62443; baseline and differential.
DR   Genevisible; Q62443; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0043083; C:synaptic cleft; ISO:MGI.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0060385; P:axonogenesis involved in innervation; IGI:MGI.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0035865; P:cellular response to potassium ion; ISO:MGI.
DR   GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
DR   GO; GO:0006839; P:mitochondrial transport; ISO:MGI.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR   GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:MGI.
DR   GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; ISO:MGI.
DR   CDD; cd00152; PTX; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR030476; Pentaxin_CS.
DR   InterPro; IPR001759; Pentraxin-related.
DR   Pfam; PF00354; Pentaxin; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00289; PTX_1; 1.
DR   PROSITE; PS51828; PTX_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Metal-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..432
FT                   /note="Neuronal pentraxin-1"
FT                   /id="PRO_0000023548"
FT   DOMAIN          226..428
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   REGION          88..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         359
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         370
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        256..316
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ   SEQUENCE   432 AA;  47117 MW;  0698B8BAE4948923 CRC64;
     MLAGRAARTC ALLALCLLGS GAQDFGPTRF ICTSVPVDAD MCAASVAAGG AEELRSNVLQ
     LRETVLQQKE TILSQKETIR ELTTKLGRCE SQSTLDSGPG EARSGGGRKQ PGSGKNTMGD
     LSRTPAAETL SQLGQTLQSL KTRLENLEQY SRLNSSSQTN SLKDLLQSKI DDLERQVLSR
     VNTLEEGKGG PKNDTEERAK IESALTSLHQ RISELEKGQK DNRPGDKFQL TFPLRTNYMY
     AKVKKSLPEM YAFTVCMWLK SSAAPGVGTP FSYAVPGQAN ELVLIEWGNN PMEILINDKV
     AKLPFVINDG KWHHICVTWT TRDGVWEAYQ DGTQGGNGEN LAPYHPIKPQ GVLVLGQEQD
     TLGGGFDATQ AFVGELAHFN IWDRKLTPGE VYNLATCSSK ALSGNVIAWA ESQIEIFGGA
     TKWTFEACRQ IN
 
 
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