ID   PTX3_MOUSE              Reviewed;         381 AA.
AC   P48759; Q8VDF1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Pentraxin-related protein PTX3;
DE   AltName: Full=Pentaxin-related protein PTX3;
DE   AltName: Full=Tumor necrosis factor-inducible gene 14 protein;
DE            Short=TSG-14;
DE   Flags: Precursor;
GN   Name=Ptx3; Synonyms=Tsg14;
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 [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Fibroblast;
RX   PubMed=8634434;
RA   Introna M., Vidal Alles V., Castellano M., Picardi G., de Gioia L.,
RA   Bottazzai B., Peri G., Breviario F., Salmona M., de Gregorio I.,
RA   Dragani T.A., Srinivasan N., Blundell T.L., Hamilton T.A., Mantovani A.;
RT   "Cloning of mouse ptx3, a new member of the pentraxin gene family expressed
RT   at extrahepatic sites.";
RL   Blood 87:1862-1872(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
RC   STRAIN=129/Sv;
RX   PubMed=7592730; DOI=10.1074/jbc.270.43.25584;
RA   Altmeyer A., Klampfer L., Goodman A.R., Vilcek J.;
RT   "Promoter structure and transcriptional activation of the murine TSG-14
RT   gene encoding a tumor necrosis factor/interleukin-1-inducible pentraxin
RT   protein.";
RL   J. Biol. Chem. 270:25584-25590(1995).
RN   [4]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=9407058; DOI=10.1074/jbc.272.52.32817;
RA   Bottazzi B., Vouret-Craviari V., Bastone A., De Gioia L., Matteucci C.,
RA   Peri G., Spreafico F., Pausa M., D'Ettorre C., Gianazza E., Tagliabue A.,
RA   Salmona M., Tedesco F., Introna M., Mantovani A.;
RT   "Multimer formation and ligand recognition by the long pentraxin PTX3.
RT   Similarities and differences with the short pentraxins C-reactive protein
RT   and serum amyloid P component.";
RL   J. Biol. Chem. 272:32817-32823(1997).
RN   [5]
RP   REVIEW.
RX   PubMed=12763682; DOI=10.1016/s0264-410x(03)00199-3;
RA   Mantovani A., Garlanda C., Bottazzi B.;
RT   "Pentraxin 3, a non-redundant soluble pattern recognition receptor involved
RT   in innate immunity.";
RL   Vaccine 21:S43-S47(2003).
CC   -!- FUNCTION: Plays a role in the regulation of innate resistance to
CC       pathogens, inflammatory reactions, possibly clearance of self-
CC       components and female fertility. {ECO:0000269|PubMed:9407058}.
CC   -!- SUBUNIT: Homooctamer; disulfide-linked (By similarity). Binds to C1q.
CC       {ECO:0000250, ECO:0000269|PubMed:9407058}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; X83601; CAA58580.1; -; mRNA.
DR   EMBL; BC022176; AAH22176.1; -; mRNA.
DR   EMBL; U33842; AAC52273.1; -; Genomic_DNA.
DR   CCDS; CCDS17392.1; -.
DR   RefSeq; NP_033013.3; NM_008987.3.
DR   AlphaFoldDB; P48759; -.
DR   SMR; P48759; -.
DR   IntAct; P48759; 1.
DR   MINT; P48759; -.
DR   STRING; 10090.ENSMUSP00000029421; -.
DR   GlyCosmos; P48759; 1 site, No reported glycans.
DR   GlyGen; P48759; 1 site.
DR   PhosphoSitePlus; P48759; -.
DR   CPTAC; non-CPTAC-3871; -.
DR   MaxQB; P48759; -.
DR   PaxDb; 10090-ENSMUSP00000029421; -.
DR   ProteomicsDB; 291544; -.
DR   Pumba; P48759; -.
DR   Antibodypedia; 33649; 528 antibodies from 37 providers.
DR   DNASU; 19288; -.
DR   Ensembl; ENSMUST00000029421.6; ENSMUSP00000029421.5; ENSMUSG00000027832.6.
DR   GeneID; 19288; -.
DR   KEGG; mmu:19288; -.
DR   UCSC; uc008pla.1; mouse.
DR   AGR; MGI:104641; -.
DR   CTD; 5806; -.
DR   MGI; MGI:104641; Ptx3.
DR   VEuPathDB; HostDB:ENSMUSG00000027832; -.
DR   eggNOG; ENOG502QUBX; Eukaryota.
DR   GeneTree; ENSGT01100000263515; -.
DR   HOGENOM; CLU_725544_0_0_1; -.
DR   InParanoid; P48759; -.
DR   OMA; CDCRREH; -.
DR   OrthoDB; 4219275at2759; -.
DR   PhylomeDB; P48759; -.
DR   TreeFam; TF330208; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 19288; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Ptx3; mouse.
DR   PRO; PR:P48759; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P48759; Protein.
DR   Bgee; ENSMUSG00000027832; Expressed in stroma of bone marrow and 147 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IMP:MGI.
DR   GO; GO:0001849; F:complement component C1q complex binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046790; F:virion binding; ISO:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   GO; GO:0045087; P:innate immune response; ISO:MGI.
DR   GO; GO:0044869; P:negative regulation by host of viral exo-alpha-sialidase activity; ISO:MGI.
DR   GO; GO:0044871; P:negative regulation by host of viral glycoprotein metabolic process; ISO:MGI.
DR   GO; GO:0044793; P:negative regulation by host of viral process; IBA:GO_Central.
DR   GO; GO:1903019; P:negative regulation of glycoprotein metabolic process; ISO:MGI.
DR   GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR   GO; GO:0008228; P:opsonization; IMP:MGI.
DR   GO; GO:0001550; P:ovarian cumulus expansion; IDA:MGI.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR   GO; GO:0001878; P:response to yeast; IMP:MGI.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR030476; Pentaxin_CS.
DR   InterPro; IPR001759; Pentraxin-related.
DR   InterPro; IPR042837; PTX3.
DR   PANTHER; PTHR46943; PENTRAXIN-RELATED PROTEIN PTX3; 1.
DR   PANTHER; PTHR46943:SF1; PENTRAXIN-RELATED PROTEIN PTX3; 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; PS00289; PTX_1; 1.
DR   PROSITE; PS51828; PTX_2; 1.
DR   Genevisible; P48759; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..381
FT                   /note="Pentraxin-related protein PTX3"
FT                   /id="PRO_0000023546"
FT   DOMAIN          179..381
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        49
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        103
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        179..357
FT                   /evidence="ECO:0000250"
FT   DISULFID        210..271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   DISULFID        317
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        318
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        50
FT                   /note="R -> A (in Ref. 3; AAC52273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="A -> S (in Ref. 3; AAC52273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="L -> R (in Ref. 2; AAH22176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="P -> S (in Ref. 2; AAH22176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147
FT                   /note="P -> S (in Ref. 2; AAH22176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="A -> S (in Ref. 3; AAC52273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="R -> H (in Ref. 3; AAC52273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="F -> L (in Ref. 2; AAH22176)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  41812 MW;  E3CA3B1D93CFE4EB CRC64;
     MHLPAILLCA LWSAVVAETS DDYELMYVNL DNEIDNGLHP TEDPTPCDCR QEHSEWDKLF
     IMLENSQMRE GMLLQATDDV LRGELQRLRA ELGRLAGGMA RPCAAGGPAD ARLVRALEPL
     LQESRDASLR LARLEDAEAR RPEATVPGLG AVLEELRRTR ADLSAVQSWV ARHWLPAGCE
     TAIFFPMRSK KIFGSVHPVR PMKLESFSTC IWVKATDVLN KTILFSYGTK WNPYEIQLYL
     SSQSLVLVVG GKENKLAADT VVSLGRWSHL CGTWSSEQGS MSLWANGELV ATTVEMAKSH
     SVPEGGLLQI GQEKNGCCVG GGFDESLAFS GRITGFNIWD RVLSEEEIRA SGGVESCHIR
     GNVVGWGVTE IQAHGGAQYV S
//