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   24-JAN-2024, entry version 173.
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   GlyCosmos; O95502; 4 sites, 2 glycans.
DR   GlyGen; O95502; 5 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (2 sites).
DR   iPTMnet; O95502; -.
DR   PhosphoSitePlus; O95502; -.
DR   BioMuta; NPTXR; -.
DR   MassIVE; O95502; -.
DR   MaxQB; O95502; -.
DR   PaxDb; 9606-ENSP00000327545; -.
DR   PeptideAtlas; O95502; -.
DR   ProteomicsDB; 50931; -.
DR   Antibodypedia; 21566; 95 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   AGR; HGNC:7954; -.
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; IAPWTDQ; -.
DR   OrthoDB; 4219275at2759; -.
DR   PhylomeDB; O95502; -.
DR   TreeFam; TF330208; -.
DR   PathwayCommons; O95502; -.
DR   SignaLink; O95502; -.
DR   BioGRID-ORCS; 23467; 9 hits in 1063 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 156 other cell types or tissues.
DR   ExpressionAtlas; O95502; baseline and differential.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00152; PTX; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001759; Pentraxin-related.
DR   PANTHER; PTHR19277:SF94; NEURONAL PENTRAXIN RECEPTOR; 1.
DR   PANTHER; PTHR19277; PENTRAXIN; 1.
DR   Pfam; PF00354; Pentaxin; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51828; PTX_2; 1.
DR   Genevisible; O95502; HS.
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
//