PTX3_MOUSE
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 03-AUG-2022, entry version 154.
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 GlyGen; P48759; 1 site.
DR PhosphoSitePlus; P48759; -.
DR CPTAC; non-CPTAC-3871; -.
DR MaxQB; P48759; -.
DR PaxDb; P48759; -.
DR PRIDE; P48759; -.
DR ProteomicsDB; 291544; -.
DR Antibodypedia; 33649; 482 antibodies from 37 providers.
DR DNASU; 19288; -.
DR Ensembl; ENSMUST00000029421; ENSMUSP00000029421; ENSMUSG00000027832.
DR GeneID; 19288; -.
DR KEGG; mmu:19288; -.
DR UCSC; uc008pla.1; mouse.
DR CTD; 5806; -.
DR MGI; MGI:104641; Ptx3.
DR VEuPathDB; HostDB:ENSMUSG00000027832; -.
DR eggNOG; ENOG502QUBX; Eukaryota.
DR GeneTree; ENSGT01050000244805; -.
DR HOGENOM; CLU_725544_0_0_1; -.
DR InParanoid; P48759; -.
DR OMA; CDCRREH; -.
DR OrthoDB; 770812at2759; -.
DR PhylomeDB; P48759; -.
DR TreeFam; TF330208; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 19288; 1 hit in 71 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 145 other tissues.
DR Genevisible; P48759; MM.
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:1903016; P:negative regulation of exo-alpha-sialidase activity; ISO:MGI.
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 InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR030476; Pentaxin_CS.
DR InterPro; IPR001759; Pentraxin-related.
DR InterPro; IPR042837; PTX3.
DR PANTHER; PTHR46943; PTHR46943; 2.
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 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
