NPTXR_RAT
ID NPTXR_RAT Reviewed; 494 AA.
AC O35764;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Neuronal pentraxin receptor;
GN Name=Nptxr; Synonyms=Npr;
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], PARTIAL PROTEIN SEQUENCE, AND SUBUNIT.
RC TISSUE=Brain;
RX PubMed=9261167; DOI=10.1074/jbc.272.34.21488;
RA Dodds D.C., Omeis I.A., Cushman S.J., Helms J.A., Perin M.S.;
RT "Neuronal pentraxin receptor, a novel putative integral membrane pentraxin
RT that interacts with neuronal pentraxin 1 and 2 and taipoxin-associated
RT calcium-binding protein 49.";
RL J. Biol. Chem. 272:21488-21494(1997).
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-211, 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: Interacts with KLHL2 (By similarity). Heteropentamer with
CC NPTX1 and/or NPTX2. Also binds taipoxin-associated calcium-binding
CC protein 49 (TCBP49/RCN2). {ECO:0000250, ECO:0000269|PubMed:10748068,
CC ECO:0000269|PubMed:9261167}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain specific.
CC -!- PTM: N-glycosylated.
CC -!- PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex containing KLHL2. {ECO:0000250}.
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DR EMBL; AF005099; AAB62885.1; -; mRNA.
DR AlphaFoldDB; O35764; -.
DR SMR; O35764; -.
DR CORUM; O35764; -.
DR STRING; 10116.ENSRNOP00000004703; -.
DR GlyGen; O35764; 3 sites, 15 N-linked glycans (1 site).
DR iPTMnet; O35764; -.
DR jPOST; O35764; -.
DR PaxDb; O35764; -.
DR PRIDE; O35764; -.
DR UCSC; RGD:628898; rat.
DR RGD; 628898; Nptxr.
DR eggNOG; ENOG502RCVB; Eukaryota.
DR InParanoid; O35764; -.
DR PhylomeDB; O35764; -.
DR PRO; PR:O35764; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008029; F:pentraxin receptor activity; IDA:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031175; P:neuron projection development; 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 GO; GO:0099150; P:regulation of postsynaptic specialization assembly; ISO:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR CDD; cd00152; PTX; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; PS51828; PTX_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..494
FT /note="Neuronal pentraxin receptor"
FT /id="PRO_0000162508"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 286..488
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT REGION 37..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 316..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 494 AA; 52371 MW; FEC996CA311E40E2 CRC64;
MKFLAVLLAA GMLAFLGAVI CIIASVPLAA SPARALPGGT DNASAASAAG APGPQRSLSA
LQGAGGSAGP SVLPGEPAAS VFPPPPGPLL SRFLCTPLAA ACPSGAEQGD AAGERAELLL
LQSTAEQLRQ TALQQEARIR ADRDTIRELT GKLGRCESGL PRGLQDAGPR RDTMADGAWD
SPALLVELEN AVRALRDRIE RIEQELPARG NLSSSAPAPA VPTALHSKMD ELEGQLLAKV
LALEKERAAL SHGSHQQRQE VEKELDALQG RVAELEHGSS AYSPPDAFKV SIPIRNNYMY
ARVRKAVPEL YAFTACMWLR SRSGGSGQGT PFSYSVPGQA NEIVLLEAGL EPMELLINDK
VAQLPLSLKD SNWHHICIAW TTRDGLWSAY QDGELRGSGE NLAAWHPIKP HGILILGQEQ
DTLGGRFDAT QAFVGDIAQF NLWDHALTPA QVLGIANCTG PLMGNVLPWE DKLVEAFGGA
KKAAFDVCKR RAKA
