NPTX2_RAT
ID NPTX2_RAT Reviewed; 432 AA.
AC P97738;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Neuronal pentraxin-2;
DE Short=NP2;
DE AltName: Full=Neuronal activity-regulated pentraxin;
DE AltName: Full=Neuronal pentraxin II;
DE Short=NP-II;
DE Flags: Precursor;
GN Name=Nptx2; Synonyms=Narp;
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 CHARACTERIZATION.
RC TISSUE=Hippocampus;
RX PubMed=8786423; DOI=10.1523/jneurosci.16-08-02463.1996;
RA Tsui C.C., Copeland N.G., Gilbert D.J., Jenkins N.A., Barnes C.,
RA Worley P.F.;
RT "Narp, a novel member of the pentraxin family, promotes neurite outgrowth
RT and is dynamically regulated by neuronal activity.";
RL J. Neurosci. 16:2463-2478(1996).
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.
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.
CC -!- INDUCTION: Rapidly induced in neurons of the hippocampus and cortex by
CC physiological synaptic activity.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S82649; AAB46783.1; -; mRNA.
DR AlphaFoldDB; P97738; -.
DR SMR; P97738; -.
DR STRING; 10116.ENSRNOP00000001331; -.
DR GlyGen; P97738; 3 sites.
DR iPTMnet; P97738; -.
DR PhosphoSitePlus; P97738; -.
DR PaxDb; P97738; -.
DR PRIDE; P97738; -.
DR RGD; 1309447; Nptx2.
DR eggNOG; ENOG502QV29; Eukaryota.
DR InParanoid; P97738; -.
DR PhylomeDB; P97738; -.
DR PRO; PR:P97738; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098892; C:extrinsic component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
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; ISO:RGD.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; 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; Disulfide bond; Glycoprotein; Lectin; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..432
FT /note="Neuronal pentraxin-2"
FT /id="PRO_0000023553"
FT DOMAIN 224..425
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 357
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 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 254..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 432 AA; 47429 MW; DD642A6AA323D24A CRC64;
MLALLTAGVA LAVAAGQAQD NPIPGSRFVC TALPPEAARA GCPLPAMPMQ GGALSPEEEL
RAAVLHWRET VVQQKETLGA QREAIRELTS KLARCEGLAG GKARGTGATG KDTMGDLPRD
PGHVVEQLSR SLQTLKDRLE SLELQLHTNA SNAGLPSDFR EVLQRRLGEL ERQLLRKVAE
LEDEKSLLHN ETSAHRQKTE NTLNALLQRV TELERGNSAF KSPDAFKVSL PLRTNYLYGK
IKKTLPELYA FTICLWLRSS ASPGIGTPFS YAVPGQANEI VLIEWGNNPI ELLINDKVAQ
LPLFVSDGKW HHICITWTTR DGMWEAFQDG EKLGTGENLA PWHPIKPGGV LILGQEQDTV
GGRFDATQAF VGELSQFNIW DRVLRAQEII NIANCSTNMP GNIIPWVDNN VDVFGGASKW
PVETCEERLL DL
