NPTX2_MOUSE
ID NPTX2_MOUSE Reviewed; 429 AA.
AC O70340;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Neuronal pentraxin-2;
DE Short=NP2;
DE AltName: Full=Neuronal pentraxin II;
DE Short=NP-II;
DE Flags: Precursor;
GN Name=Nptx2;
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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Perin M.S.;
RT "Mouse neuronal pentraxin 2 gene.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Likely to play role in the modification of cellular
CC properties that underlie long-term plasticity. Binds to agar matrix in
CC a calcium-dependent manner (By similarity). {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: Secreted {ECO:0000250}.
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DR EMBL; AF049124; AAC05131.1; -; mRNA.
DR EMBL; AF318618; AAK06745.1; -; Genomic_DNA.
DR EMBL; BC026054; AAH26054.1; -; mRNA.
DR CCDS; CCDS19849.1; -.
DR RefSeq; NP_058069.1; NM_016789.3.
DR AlphaFoldDB; O70340; -.
DR SMR; O70340; -.
DR BioGRID; 207287; 1.
DR IntAct; O70340; 2.
DR MINT; O70340; -.
DR STRING; 10090.ENSMUSP00000071687; -.
DR GlyConnect; 2553; 2 N-Linked glycans (2 sites).
DR GlyGen; O70340; 3 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; O70340; -.
DR PhosphoSitePlus; O70340; -.
DR MaxQB; O70340; -.
DR PaxDb; O70340; -.
DR PRIDE; O70340; -.
DR ProteomicsDB; 293962; -.
DR Antibodypedia; 30245; 232 antibodies from 33 providers.
DR DNASU; 53324; -.
DR Ensembl; ENSMUST00000071782; ENSMUSP00000071687; ENSMUSG00000059991.
DR GeneID; 53324; -.
DR KEGG; mmu:53324; -.
DR UCSC; uc012egq.1; mouse.
DR CTD; 4885; -.
DR MGI; MGI:1858209; Nptx2.
DR VEuPathDB; HostDB:ENSMUSG00000059991; -.
DR eggNOG; ENOG502QV29; Eukaryota.
DR GeneTree; ENSGT01050000244805; -.
DR HOGENOM; CLU_032051_0_0_1; -.
DR InParanoid; O70340; -.
DR OMA; PGNRFVC; -.
DR OrthoDB; 770812at2759; -.
DR PhylomeDB; O70340; -.
DR TreeFam; TF330208; -.
DR BioGRID-ORCS; 53324; 3 hits in 73 CRISPR screens.
DR PRO; PR:O70340; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O70340; protein.
DR Bgee; ENSMUSG00000059991; Expressed in lumbar dorsal root ganglion and 81 other tissues.
DR Genevisible; O70340; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098892; C:extrinsic component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; 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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Lectin; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..429
FT /note="Neuronal pentraxin-2"
FT /id="PRO_0000023552"
FT DOMAIN 221..422
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 251..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 429 AA; 47137 MW; 638EED14C4CECA28 CRC64;
MLALLTVGVA LAVAAGRAQD SPIPGSRFVC TALPPEAARA GCPLPAMPMQ GGALSPEEEL
RAAVLQLRET VVQQKETLGA QREAIRELTG KLARCEGLAG GKARGTGKDT MGDLPRDPGH
VVEQLSRSLQ TLKDRLESLE LQLRTNVSNA GLPSDFREVL QRRLGELERQ LLRKVAELED
EKSLLHNETS AHRQKTESTL NALLQRVTEL ERGNSAFKSP DAFKVSLPLR TNYLYGKIKK
TLPELYAFTI CLWLRSSASP GIGTPFSYAV PGQANEIVLI EWGNNPIELL INDKVAQLPL
FVSDGKWHHI CITWTTRDGM WEAFQDGEKL GTGENLAPWH PIKPGGVLIL GQEQDTVGGR
FDATQAFVGE LSQFNIWDRV LRAQEIINIA NCSTNMPGNI IPWVDNNVDV FGGASKWPVE
TCEERLLDL
