NPTX1_RAT
ID NPTX1_RAT Reviewed; 432 AA.
AC P47971;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Neuronal pentraxin-1;
DE Short=NP1;
DE AltName: Full=47 kDa taipoxin-binding protein;
DE AltName: Full=Neuronal pentraxin I;
DE Short=NP-I;
DE Flags: Precursor;
GN Name=Nptx1;
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], AND PROTEIN SEQUENCE OF 40-80; 119-153 AND
RP 293-337.
RC STRAIN=Sprague-Dawley;
RX PubMed=7695898; DOI=10.1016/0896-6273(95)90308-9;
RA Schlimgen A.K., Helms J.A., Vogel H., Perin M.S.;
RT "Neuronal pentraxin, a secreted protein with homology to acute phase
RT proteins of the immune system.";
RL Neuron 14:519-526(1995).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10748068; DOI=10.1074/jbc.m002254200;
RA Kirkpatrick L.L., Matzuk M.M., Dodds D.C., Perin M.S.;
RT "Biochemical interactions of the neuronal pentraxins. Neuronal pentraxin
RT (NP) receptor binds to taipoxin and taipoxin-associated calcium-binding
RT protein 49 via NP1 and NP2.";
RL J. Biol. Chem. 275:17786-17792(2000).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-154, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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:0000269|PubMed:10748068}.
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:0000269|PubMed:10748068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Cerebellum, hippocampus and cerebral cortex.
CC -!- PTM: Glycosylated.
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DR EMBL; U18772; AAA92685.1; -; mRNA.
DR RefSeq; NP_714957.1; NM_153735.2.
DR AlphaFoldDB; P47971; -.
DR SMR; P47971; -.
DR BioGRID; 251819; 3.
DR CORUM; P47971; -.
DR IntAct; P47971; 1.
DR MINT; P47971; -.
DR STRING; 10116.ENSRNOP00000005067; -.
DR GlyGen; P47971; 2 sites, 9 N-linked glycans (1 site).
DR iPTMnet; P47971; -.
DR PaxDb; P47971; -.
DR PRIDE; P47971; -.
DR Ensembl; ENSRNOT00000005067; ENSRNOP00000005067; ENSRNOG00000003741.
DR GeneID; 266777; -.
DR KEGG; rno:266777; -.
DR CTD; 4884; -.
DR RGD; 628894; Nptx1.
DR eggNOG; ENOG502QTID; Eukaryota.
DR GeneTree; ENSGT01050000244805; -.
DR HOGENOM; CLU_032051_0_0_1; -.
DR InParanoid; P47971; -.
DR OrthoDB; 770812at2759; -.
DR PhylomeDB; P47971; -.
DR TreeFam; TF330208; -.
DR PRO; PR:P47971; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Genevisible; P47971; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
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; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0035865; P:cellular response to potassium ion; IDA:RGD.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:RGD.
DR GO; GO:0006839; P:mitochondrial transport; IMP:RGD.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; ISO:RGD.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..432
FT /note="Neuronal pentraxin-1"
FT /id="PRO_0000023549"
FT DOMAIN 226..428
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT REGION 90..128
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:0007744|PubMed:24090084"
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; 47216 MW; 3071E3E40ACA3820 CRC64;
MLAGRAARTC ALLALCLLGS RAQDFGPTRF ICTSVPVDAD MCAASVAAGG AEELRSNVLQ
LRETVLQQKE TILSQKETIR ELTTKLGRCE SQSTLDAGPG EARSGGGRKQ PGSGKNTMGD
LSRTPASETL 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
