NPTX2_HUMAN
ID NPTX2_HUMAN Reviewed; 431 AA.
AC P47972; A4D267; Q86XV7; Q96G70;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Neuronal pentraxin-2;
DE Short=NP2;
DE AltName: Full=Neuronal pentraxin II;
DE Short=NP-II;
DE Flags: Precursor;
GN Name=NPTX2;
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].
RC TISSUE=Brain;
RX PubMed=8530029; DOI=10.1006/geno.1995.1134;
RA Hsu Y.-C., Perin M.S.;
RT "Human neuronal pentraxin II (NPTX2): conservation, genomic structure, and
RT chromosomal localization.";
RL Genomics 28:220-227(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [6]
RP 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).
CC -!- FUNCTION: Likely to play role in the modification of cellular
CC properties that underlie long-term plasticity. Binds to agar matrix in
CC a calcium-dependent manner (By similarity). {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:0000269|PubMed:10748068}.
CC -!- INTERACTION:
CC P47972; O60353: FZD6; NbExp=9; IntAct=EBI-3957229, EBI-8754490;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain, pancreas, liver, heart and skeletal muscle.
CC Highest levels are seen in the testis.
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DR EMBL; U29195; AAA68980.2; -; Genomic_DNA.
DR EMBL; U29191; AAA68980.2; JOINED; Genomic_DNA.
DR EMBL; U29192; AAA68980.2; JOINED; Genomic_DNA.
DR EMBL; U29193; AAA68980.2; JOINED; Genomic_DNA.
DR EMBL; U29194; AAA68980.2; JOINED; Genomic_DNA.
DR EMBL; U26662; AAA92296.1; -; mRNA.
DR EMBL; AC074121; AAQ93363.1; -; Genomic_DNA.
DR EMBL; CH236956; EAL23889.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76705.1; -; Genomic_DNA.
DR EMBL; BC009924; AAH09924.1; -; mRNA.
DR EMBL; BC034781; AAH34781.1; -; mRNA.
DR EMBL; BC035339; AAH35339.1; -; mRNA.
DR EMBL; BC048275; AAH48275.2; -; mRNA.
DR CCDS; CCDS5657.1; -.
DR RefSeq; NP_002514.1; NM_002523.2.
DR AlphaFoldDB; P47972; -.
DR SMR; P47972; -.
DR BioGRID; 110945; 22.
DR CORUM; P47972; -.
DR IntAct; P47972; 5.
DR STRING; 9606.ENSP00000265634; -.
DR GlyGen; P47972; 3 sites.
DR iPTMnet; P47972; -.
DR PhosphoSitePlus; P47972; -.
DR BioMuta; NPTX2; -.
DR DMDM; 20981708; -.
DR EPD; P47972; -.
DR jPOST; P47972; -.
DR MassIVE; P47972; -.
DR PaxDb; P47972; -.
DR PeptideAtlas; P47972; -.
DR PRIDE; P47972; -.
DR ProteomicsDB; 55826; -.
DR Antibodypedia; 30245; 232 antibodies from 33 providers.
DR DNASU; 4885; -.
DR Ensembl; ENST00000265634.4; ENSP00000265634.3; ENSG00000106236.4.
DR GeneID; 4885; -.
DR KEGG; hsa:4885; -.
DR MANE-Select; ENST00000265634.4; ENSP00000265634.3; NM_002523.3; NP_002514.1.
DR UCSC; uc003upl.3; human.
DR CTD; 4885; -.
DR DisGeNET; 4885; -.
DR GeneCards; NPTX2; -.
DR HGNC; HGNC:7953; NPTX2.
DR HPA; ENSG00000106236; Group enriched (brain, pituitary gland).
DR MIM; 600750; gene.
DR neXtProt; NX_P47972; -.
DR OpenTargets; ENSG00000106236; -.
DR PharmGKB; PA31739; -.
DR VEuPathDB; HostDB:ENSG00000106236; -.
DR eggNOG; ENOG502QV29; Eukaryota.
DR GeneTree; ENSGT01050000244805; -.
DR HOGENOM; CLU_032051_0_0_1; -.
DR InParanoid; P47972; -.
DR OMA; PGNRFVC; -.
DR OrthoDB; 770812at2759; -.
DR PhylomeDB; P47972; -.
DR TreeFam; TF330208; -.
DR PathwayCommons; P47972; -.
DR SignaLink; P47972; -.
DR BioGRID-ORCS; 4885; 9 hits in 1070 CRISPR screens.
DR GeneWiki; NPTX2; -.
DR GenomeRNAi; 4885; -.
DR Pharos; P47972; Tbio.
DR PRO; PR:P47972; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P47972; protein.
DR Bgee; ENSG00000106236; Expressed in type B pancreatic cell and 139 other tissues.
DR Genevisible; P47972; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; NAS:UniProtKB.
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 Calcium; Disulfide bond; Glycoprotein; Lectin; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..431
FT /note="Neuronal pentraxin-2"
FT /id="PRO_0000023551"
FT DOMAIN 223..424
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 367
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 253..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CONFLICT 78..82
FT /note="GAQRE -> ASAR (in Ref. 1; AAA68980/AAA92296)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="V -> L (in Ref. 1; AAA68980/AAA92296)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="R -> A (in Ref. 1; AAA68980/AAA92296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 47042 MW; 87B7BF9BA1049AC5 CRC64;
MLALLAASVA LAVAAGAQDS PAPGSRFVCT ALPPEAVHAG CPLPAMPMQG GAQSPEEELR
AAVLQLRETV VQQKETLGAQ REAIRELTGK LARCEGLAGG KARGAGATGK DTMGDLPRDP
GHVVEQLSRS LQTLKDRLES LEHQLRANVS NAGLPGDFRE VLQQRLGELE RQLLRKVAEL
EDEKSLLHNE TSAHRQKTES TLNALLQRVT ELERGNSAFK SPDAFKVSLP LRTNYLYGKI
KKTLPELYAF TICLWLRSSA SPGIGTPFSY AVPGQANEIV LIEWGNNPIE LLINDKVAQL
PLFVSDGKWH HICVTWTTRD GMWEAFQDGE KLGTGENLAP WHPIKPGGVL ILGQEQDTVG
GRFDATQAFV GELSQFNIWD RVLRAQEIVN IANCSTNMPG NIIPWVDNNV DVFGGASKWP
VETCEERLLD L
