NPTX1_HUMAN
ID NPTX1_HUMAN Reviewed; 432 AA.
AC Q15818; B3KXH3; Q5FWE6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Neuronal pentraxin-1;
DE Short=NP1;
DE AltName: Full=Neuronal pentraxin I;
DE Short=NP-I;
DE Flags: Precursor;
GN Name=NPTX1;
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 [MRNA].
RX PubMed=8884281; DOI=10.1006/geno.1996.0503;
RA Omeis I.A., Hsu Y.-C., Perin M.S.;
RT "Mouse and human neuronal pentraxin 1 (NPTX1): conservation, genomic
RT structure, and chromosomal localization.";
RL Genomics 36:543-545(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Chondrosarcoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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: Homooligomer or heterooligomer (probably pentamer) with
CC neuronal pentraxin receptor (NPTXR). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000305}.
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DR EMBL; U61849; AAC50727.1; -; mRNA.
DR EMBL; AK127335; BAG54485.1; -; mRNA.
DR EMBL; BC089441; AAH89441.1; -; mRNA.
DR CCDS; CCDS32762.1; -.
DR RefSeq; NP_002513.2; NM_002522.3.
DR PDB; 6YPE; X-ray; 1.45 A; A/B=225-429.
DR PDBsum; 6YPE; -.
DR AlphaFoldDB; Q15818; -.
DR SMR; Q15818; -.
DR BioGRID; 110944; 75.
DR IntAct; Q15818; 37.
DR MINT; Q15818; -.
DR STRING; 9606.ENSP00000307549; -.
DR TCDB; 1.C.92.1.3; the pentraxin (pentraxin) family.
DR GlyGen; Q15818; 2 sites.
DR iPTMnet; Q15818; -.
DR PhosphoSitePlus; Q15818; -.
DR BioMuta; NPTX1; -.
DR DMDM; 77416871; -.
DR EPD; Q15818; -.
DR jPOST; Q15818; -.
DR MassIVE; Q15818; -.
DR MaxQB; Q15818; -.
DR PaxDb; Q15818; -.
DR PeptideAtlas; Q15818; -.
DR PRIDE; Q15818; -.
DR ProteomicsDB; 60774; -.
DR Antibodypedia; 32766; 411 antibodies from 32 providers.
DR DNASU; 4884; -.
DR Ensembl; ENST00000306773.5; ENSP00000307549.4; ENSG00000171246.6.
DR GeneID; 4884; -.
DR KEGG; hsa:4884; -.
DR MANE-Select; ENST00000306773.5; ENSP00000307549.4; NM_002522.4; NP_002513.2.
DR UCSC; uc002jyp.2; human.
DR CTD; 4884; -.
DR DisGeNET; 4884; -.
DR GeneCards; NPTX1; -.
DR HGNC; HGNC:7952; NPTX1.
DR HPA; ENSG00000171246; Tissue enriched (brain).
DR MIM; 602367; gene.
DR neXtProt; NX_Q15818; -.
DR OpenTargets; ENSG00000171246; -.
DR PharmGKB; PA31738; -.
DR VEuPathDB; HostDB:ENSG00000171246; -.
DR eggNOG; ENOG502QTID; Eukaryota.
DR GeneTree; ENSGT01050000244805; -.
DR HOGENOM; CLU_032051_0_0_1; -.
DR InParanoid; Q15818; -.
DR OMA; AQNFGQT; -.
DR OrthoDB; 770812at2759; -.
DR PhylomeDB; Q15818; -.
DR TreeFam; TF330208; -.
DR PathwayCommons; Q15818; -.
DR SignaLink; Q15818; -.
DR SIGNOR; Q15818; -.
DR BioGRID-ORCS; 4884; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; NPTX1; human.
DR GeneWiki; NPTX1; -.
DR GenomeRNAi; 4884; -.
DR Pharos; Q15818; Tbio.
DR PRO; PR:Q15818; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q15818; protein.
DR Bgee; ENSG00000171246; Expressed in cerebellar vermis and 162 other tissues.
DR Genevisible; Q15818; HS.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060385; P:axonogenesis involved in innervation; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0006839; P:mitochondrial transport; IEA:Ensembl.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IEA:Ensembl.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; 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 3D-structure; Calcium; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..432
FT /note="Neuronal pentraxin-1"
FT /id="PRO_0000023547"
FT DOMAIN 226..428
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT REGION 90..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 280
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 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 256..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CONFLICT 7
FT /note="Missing (in Ref. 1; AAC50727)"
FT /evidence="ECO:0000305"
FT CONFLICT 20..22
FT /note="AGA -> P (in Ref. 1; AAC50727)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="S -> SN (in Ref. 1; AAC50727)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="R -> K (in Ref. 1; AAC50727)"
FT /evidence="ECO:0000305"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:6YPE"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:6YPE"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:6YPE"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6YPE"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:6YPE"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:6YPE"
SQ SEQUENCE 432 AA; 47122 MW; B881AC19F7C8F74A CRC64;
MPAGRAARTC ALLALCLLGA GAQDFGPTRF ICTSVPVDAD MCAASVAAGG AEELRSSVLQ
LRETVLQQKE TILSQKETIR ELTAKLGRCE SQSTLDPGAG EARAGGGRKQ PGSGKNTMGD
LSRTPAAETL SQLGQTLQSL KTRLENLEQY SRLNSSSQTN SLKDLLQSKI DELERQVLSR
VNTLEEGKGG PRNDTEERVK IETALTSLHQ RISELEKGQK DNRPGDKFQL TFPLRTNYMY
AKVKKSLPEM YAFTVCMWLK SSATPGVGTP FSYAVPGQAN ELVLIEWGNN PMEILINDKV
AKLPFVINDG KWHHICVTWT TRDGVWEAYQ DGTQGGSGEN LAPYHPIKPQ GVLVLGQEQD
TLGGGFDATQ AFVGELAHFN IWDRKLTPGE VYNLATCSTK ALSGNVIAWA ESHIEIYGGA
TKWTFEACRQ IN
