NPTXR_MOUSE
ID NPTXR_MOUSE Reviewed; 493 AA.
AC Q99J85;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Neuronal pentraxin receptor;
GN Name=Nptxr; Synonyms=Npr;
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 / MRNA].
RC STRAIN=C57BL/6J;
RA Perin M.S.;
RT "Mouse neuronal pentraxin receptor.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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).
RN [3]
RP INTERACTION WITH KLHL2, AND UBIQUITINATION.
RX PubMed=21549840; DOI=10.1016/j.mcn.2011.04.005;
RA Tseng L.A., Bixby J.L.;
RT "Interaction of an intracellular pentraxin with a BTB-Kelch protein is
RT associated with ubiquitylation, aggregation and neuronal apoptosis.";
RL Mol. Cell. Neurosci. 47:254-264(2011).
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: Heteropentamer with NPTX1 and/or NPTX2. Also binds taipoxin-
CC associated calcium-binding protein 49 (TCBP49/RCN2) (By similarity).
CC Interacts with KLHL2. {ECO:0000250, ECO:0000269|PubMed:21549840}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex containing KLHL2.
CC {ECO:0000269|PubMed:21549840}.
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DR EMBL; AF316612; AAK11300.1; -; mRNA.
DR EMBL; AF318076; AAK06717.1; -; Genomic_DNA.
DR CCDS; CCDS27653.1; -.
DR AlphaFoldDB; Q99J85; -.
DR SMR; Q99J85; -.
DR IntAct; Q99J85; 2.
DR MINT; Q99J85; -.
DR STRING; 10090.ENSMUSP00000023057; -.
DR GlyConnect; 2554; 4 N-Linked glycans (2 sites).
DR GlyGen; Q99J85; 3 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q99J85; -.
DR PhosphoSitePlus; Q99J85; -.
DR MaxQB; Q99J85; -.
DR PaxDb; Q99J85; -.
DR PRIDE; Q99J85; -.
DR ProteomicsDB; 253099; -.
DR MGI; MGI:1920590; Nptxr.
DR eggNOG; ENOG502RCVB; Eukaryota.
DR InParanoid; Q99J85; -.
DR PRO; PR:Q99J85; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99J85; protein.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008029; F:pentraxin receptor activity; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
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 GO; GO:0099150; P:regulation of postsynaptic specialization assembly; IDA:SynGO.
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; Membrane; Metal-binding; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..493
FT /note="Neuronal pentraxin receptor"
FT /id="PRO_0000162507"
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..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 285..487
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT REGION 37..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 430
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:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 315..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 493 AA; 52285 MW; EC8114E2AA81F7A1 CRC64;
MKFLAVLLAA GMLAFLGAVI CIIASVPLAA SPARALPGGT DNASAASAAG GSGPQRSLSA
LHSAGGSAGP SVLPGEPAAS VFPPPPVPLL SRFLCTPLAA ACPSGAEQGD AAGERAELLL
LQSTAEQLRQ TALQQEARIR ADRDTIRELT GKLGRCESGL PRGLQDAGPR RDTMADGAWD
SPALLLELED AVRALRDRIE RIEQELPARG NLSSAPAPAM PTALHSKMDE LECQLLAKVL
ALEKERAALS HGSHQQRQEV EKELNALQGR VAELEHGSSA YSPPDAFKVS IPIRNNYMYA
RVRKALPELY AFTACMCVRS RSGGSGQGTP FSYSVPGQAN EIVLLEAGLE PMELLINDKV
AQLPLSLKDS NWHHICISWT TRDGLWSAYQ DGELRGSGEN LAAWHPIKPH GILILGQEQD
TLGGRFDATQ AFVGDIAQFN LWDHALTPAQ VLGMANCTGP LMGNVLPWED KLVEAFGGAK
KAAFDVCKGR AKA
