NPTXR_HUMAN
ID NPTXR_HUMAN Reviewed; 500 AA.
AC O95502;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Neuronal pentraxin receptor;
GN Name=NPTXR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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). Interacts with
CC KLHL2 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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DR EMBL; AL008583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS33647.1; -.
DR RefSeq; NP_055108.2; NM_014293.3.
DR AlphaFoldDB; O95502; -.
DR SMR; O95502; -.
DR BioGRID; 117029; 29.
DR STRING; 9606.ENSP00000327545; -.
DR GlyConnect; 1556; 1 N-Linked glycan (1 site).
DR GlyGen; O95502; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; O95502; -.
DR PhosphoSitePlus; O95502; -.
DR BioMuta; NPTXR; -.
DR MassIVE; O95502; -.
DR MaxQB; O95502; -.
DR PaxDb; O95502; -.
DR PeptideAtlas; O95502; -.
DR PRIDE; O95502; -.
DR ProteomicsDB; 50931; -.
DR Antibodypedia; 21566; 86 antibodies from 21 providers.
DR DNASU; 23467; -.
DR Ensembl; ENST00000333039.4; ENSP00000327545.3; ENSG00000221890.6.
DR GeneID; 23467; -.
DR KEGG; hsa:23467; -.
DR MANE-Select; ENST00000333039.4; ENSP00000327545.3; NM_014293.4; NP_055108.2.
DR UCSC; uc062eix.1; human.
DR CTD; 23467; -.
DR DisGeNET; 23467; -.
DR GeneCards; NPTXR; -.
DR HGNC; HGNC:7954; NPTXR.
DR HPA; ENSG00000221890; Tissue enriched (brain).
DR MIM; 609474; gene.
DR neXtProt; NX_O95502; -.
DR OpenTargets; ENSG00000221890; -.
DR PharmGKB; PA31740; -.
DR VEuPathDB; HostDB:ENSG00000221890; -.
DR eggNOG; ENOG502RCVB; Eukaryota.
DR GeneTree; ENSGT00940000154405; -.
DR HOGENOM; CLU_032051_0_0_1; -.
DR InParanoid; O95502; -.
DR OMA; CPSGAQQ; -.
DR OrthoDB; 770812at2759; -.
DR PhylomeDB; O95502; -.
DR TreeFam; TF330208; -.
DR PathwayCommons; O95502; -.
DR SignaLink; O95502; -.
DR BioGRID-ORCS; 23467; 9 hits in 1002 CRISPR screens.
DR ChiTaRS; NPTXR; human.
DR GeneWiki; NPTXR; -.
DR GenomeRNAi; 23467; -.
DR Pharos; O95502; Tbio.
DR PRO; PR:O95502; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O95502; protein.
DR Bgee; ENSG00000221890; Expressed in Brodmann (1909) area 10 and 154 other tissues.
DR ExpressionAtlas; O95502; baseline and differential.
DR Genevisible; O95502; HS.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IMP:SynGO.
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 3: Inferred from homology;
KW Calcium; Disulfide bond; Glycoprotein; Membrane; Metal-binding; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..500
FT /note="Neuronal pentraxin receptor"
FT /id="PRO_0000162506"
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..500
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 292..494
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT REGION 42..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 437
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 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 322..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 500 AA; 52846 MW; 831D12AB76ACCA00 CRC64;
MKFLAVLLAA GMLAFLGAVI CIIASVPLAA SPARALPGGA DNASVASGAA ASPGPQRSLS
ALHGAGGSAG PPALPGAPAA SAHPLPPGPL FSRFLCTPLA AACPSGAQQG DAAGAAPGER
EELLLLQSTA EQLRQTALQQ EARIRADQDT IRELTGKLGR CESGLPRGLQ GAGPRRDTMA
DGPWDSPALI LELEDAVRAL RDRIDRLEQE LPARVNLSAA PAPVSAVPTG LHSKMDQLEG
QLLAQVLALE KERVALSHSS RRQRQEVEKE LDVLQGRVAE LEHGSSAYSP PDAFKISIPI
RNNYMYARVR KALPELYAFT ACMWLRSRSS GTGQGTPFSY SVPGQANEIV LLEAGHEPME
LLINDKVAQL PLSLKDNGWH HICIAWTTRD GLWSAYQDGE LQGSGENLAA WHPIKPHGIL
ILGQEQDTLG GRFDATQAFV GDIAQFNLWD HALTPAQVLG IANCTAPLLG NVLPWEDKLV
EAFGGATKAA FDVCKGRAKA
