PTX3_HUMAN
ID PTX3_HUMAN Reviewed; 381 AA.
AC P26022; B2R6T6; Q38M82;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Pentraxin-related protein PTX3 {ECO:0000305};
DE AltName: Full=Pentaxin-related protein PTX3;
DE AltName: Full=Tumor necrosis factor alpha-induced protein 5;
DE Short=TNF alpha-induced protein 5;
DE AltName: Full=Tumor necrosis factor-inducible gene 14 protein;
DE Short=TSG-14;
DE Flags: Precursor;
GN Name=PTX3 {ECO:0000312|HGNC:HGNC:9692}; Synonyms=TNFAIP5, TSG14;
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], AND VARIANT ASP-48.
RC TISSUE=Endothelial cell;
RX PubMed=1429570; DOI=10.1016/s0021-9258(18)41653-5;
RA Breviario F., D'Aniello E.M., Golay J., Peri G., Bottazi B., Bairoch A.,
RA Saccone S., Marzella R., Predazzi V., Rocchi M., Della Valle G., Dejana E.,
RA Mantovani A., Introna M.;
RT "Interleukin-1-inducible genes in endothelial cells. Cloning of a new gene
RT related to C-reactive protein and serum amyloid P component.";
RL J. Biol. Chem. 267:22190-22197(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-48.
RC TISSUE=Endothelial cell;
RX PubMed=8131794;
RA Introna M., Breviario F., D'Aniello E.M., Golay J., Dejana E.,
RA Mantovani A.;
RT "IL-1 inducible genes in human umbilical vein endothelial cells.";
RL Eur. Heart J. 14:78-81(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-48.
RC TISSUE=Foreskin;
RX PubMed=7679696;
RA Lee G.W., Lee T.H., Vilcek J.;
RT "TSG-14, a tumor necrosis factor- and IL-1-inducible protein, is a novel
RT member of the pentaxin family of acute phase proteins.";
RL J. Immunol. 150:1804-1812(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tan J., Davila S., Hibberd M.L., Seielstad M.;
RT "Genetic variation in pentaxin-related protein PTX3.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-48.
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 [9]
RP DISCUSSION OF SEQUENCE.
RX PubMed=7523502;
RA Lee G.W., Goodman A.R., Lee T.H., Vilcek J.;
RT "Relationship of TSG-14 protein to the pentraxin family of major acute
RT phase proteins.";
RL J. Immunol. 153:3700-3707(1994).
RN [10]
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).
RN [11]
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=18223257; DOI=10.1074/jbc.m708535200;
RA Inforzato A., Rivieccio V., Morreale A.P., Bastone A., Salustri A.,
RA Scarchilli L., Verdoliva A., Vincenti S., Gallo G., Chiapparino C.,
RA Pacello L., Nucera E., Serlupi-Crescenzi O., Day A.J., Bottazzi B.,
RA Mantovani A., De Santis R., Salvatori G.;
RT "Structural characterization of PTX3 disulfide bond network and its
RT multimeric status in cumulus matrix organization.";
RL J. Biol. Chem. 283:10147-10161(2008).
RN [12]
RP INTERACTION WITH SARS-COV-2 NUCLEOPROTEIN AND SPIKE GLYCOPROTEIN (MICROBIAL
RP FUNCTION).
RX PubMed=35102342; DOI=10.1038/s41590-021-01114-w;
RA Stravalaci M., Pagani I., Paraboschi E.M., Pedotti M., Doni A.,
RA Scavello F., Mapelli S.N., Sironi M., Perucchini C., Varani L.,
RA Matkovic M., Cavalli A., Cesana D., Gallina P., Pedemonte N., Capurro V.,
RA Clementi N., Mancini N., Invernizzi P., Bayarri-Olmos R., Garred P.,
RA Rappuoli R., Duga S., Bottazzi B., Uguccioni M., Asselta R., Vicenzi E.,
RA Mantovani A., Garlanda C.;
RT "Recognition and inhibition of SARS-CoV-2 by humoral innate immunity
RT pattern recognition molecules.";
RL Nat. Immunol. 23:275-286(2022).
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:0000305|PubMed:12763682}.
CC -!- SUBUNIT: Homooctamer; disulfide-linked (PubMed:18223257). Binds to C1q
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:18223257}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS-
CC CoV-2 Nucleoprotein and Spike protein homotrimer.
CC {ECO:0000269|PubMed:35102342}.
CC -!- INTERACTION:
CC P26022; P08603: CFH; NbExp=15; IntAct=EBI-11574553, EBI-1223708;
CC P26022; P08603-2: CFH; NbExp=2; IntAct=EBI-11574553, EBI-12684810;
CC P26022; O00602: FCN1; NbExp=3; IntAct=EBI-11574553, EBI-5282479;
CC P26022; PRO_0000009136 [O00602]: FCN1; NbExp=7; IntAct=EBI-11574553, EBI-11784425;
CC P26022; Q15485: FCN2; NbExp=7; IntAct=EBI-11574553, EBI-7468784;
CC P26022; P09038: FGF2; NbExp=16; IntAct=EBI-11574553, EBI-977447;
CC P26022; P26022: PTX3; NbExp=17; IntAct=EBI-11574553, EBI-11574553;
CC P26022; P98066: TNFAIP6; NbExp=8; IntAct=EBI-11574553, EBI-11700693;
CC PRO_0000023545; P08603: CFH; NbExp=8; IntAct=EBI-22114950, EBI-1223708;
CC PRO_0000023545; P08603-2: CFH; NbExp=2; IntAct=EBI-22114950, EBI-12684810;
CC PRO_0000023545; Q03591: CFHR1; NbExp=5; IntAct=EBI-22114950, EBI-3935840;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By IL1B/interleukin-1 beta and TNF.
CC -!- PTM: Glycosylated. {ECO:0000305}.
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DR EMBL; X63613; CAA45158.1; -; mRNA.
DR EMBL; X63053; CAA44778.1; -; mRNA.
DR EMBL; M31166; AAA61234.1; -; mRNA.
DR EMBL; DQ207368; ABA64467.1; -; Genomic_DNA.
DR EMBL; AK312705; BAG35583.1; -; mRNA.
DR EMBL; AC020630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78708.1; -; Genomic_DNA.
DR EMBL; BC039733; AAH39733.1; -; mRNA.
DR CCDS; CCDS3180.1; -.
DR PIR; A44323; A44323.
DR RefSeq; NP_002843.2; NM_002852.3.
DR AlphaFoldDB; P26022; -.
DR SMR; P26022; -.
DR BioGRID; 111770; 72.
DR IntAct; P26022; 21.
DR STRING; 9606.ENSP00000295927; -.
DR GlyConnect; 704; 1 N-Linked glycan (1 site).
DR GlyGen; P26022; 3 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; P26022; -.
DR PhosphoSitePlus; P26022; -.
DR BioMuta; PTX3; -.
DR DMDM; 296452984; -.
DR EPD; P26022; -.
DR jPOST; P26022; -.
DR MassIVE; P26022; -.
DR MaxQB; P26022; -.
DR PaxDb; P26022; -.
DR PeptideAtlas; P26022; -.
DR PRIDE; P26022; -.
DR ProteomicsDB; 54310; -.
DR Antibodypedia; 33649; 482 antibodies from 37 providers.
DR DNASU; 5806; -.
DR Ensembl; ENST00000295927.4; ENSP00000295927.3; ENSG00000163661.4.
DR GeneID; 5806; -.
DR KEGG; hsa:5806; -.
DR MANE-Select; ENST00000295927.4; ENSP00000295927.3; NM_002852.4; NP_002843.2.
DR UCSC; uc003fbl.5; human.
DR CTD; 5806; -.
DR DisGeNET; 5806; -.
DR GeneCards; PTX3; -.
DR HGNC; HGNC:9692; PTX3.
DR HPA; ENSG00000163661; Tissue enhanced (adipose tissue, urinary bladder).
DR MIM; 602492; gene.
DR neXtProt; NX_P26022; -.
DR OpenTargets; ENSG00000163661; -.
DR PharmGKB; PA34036; -.
DR VEuPathDB; HostDB:ENSG00000163661; -.
DR eggNOG; ENOG502QUBX; Eukaryota.
DR GeneTree; ENSGT01050000244805; -.
DR HOGENOM; CLU_725544_0_0_1; -.
DR InParanoid; P26022; -.
DR OMA; CDCRREH; -.
DR OrthoDB; 770812at2759; -.
DR PhylomeDB; P26022; -.
DR TreeFam; TF330208; -.
DR PathwayCommons; P26022; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P26022; -.
DR SIGNOR; P26022; -.
DR BioGRID-ORCS; 5806; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; PTX3; human.
DR GeneWiki; PTX3; -.
DR GenomeRNAi; 5806; -.
DR Pharos; P26022; Tbio.
DR PRO; PR:P26022; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P26022; protein.
DR Bgee; ENSG00000163661; Expressed in cartilage tissue and 145 other tissues.
DR Genevisible; P26022; HS.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IEA:Ensembl.
DR GO; GO:0001849; F:complement component C1q complex binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046790; F:virion binding; IDA:BHF-UCL.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; IDA:BHF-UCL.
DR GO; GO:0044869; P:negative regulation by host of viral exo-alpha-sialidase activity; IDA:BHF-UCL.
DR GO; GO:0044871; P:negative regulation by host of viral glycoprotein metabolic process; IDA:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:1903019; P:negative regulation of glycoprotein metabolic process; IDA:BHF-UCL.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:BHF-UCL.
DR GO; GO:0008228; P:opsonization; IEA:Ensembl.
DR GO; GO:0001550; P:ovarian cumulus expansion; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0001878; P:response to yeast; IEA:Ensembl.
DR CDD; cd00152; PTX; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006558; LamG-like.
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; SM00560; LamGL; 1.
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 Coiled coil; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..381
FT /note="Pentraxin-related protein PTX3"
FT /id="PRO_0000023545"
FT DOMAIN 179..381
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT COILED 74..101
FT /evidence="ECO:0000255"
FT COILED 143..167
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18223257"
FT DISULFID 49
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18223257"
FT DISULFID 103
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18223257"
FT DISULFID 179..357
FT /evidence="ECO:0000269|PubMed:18223257"
FT DISULFID 210..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172,
FT ECO:0000269|PubMed:18223257"
FT DISULFID 317
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18223257"
FT DISULFID 318
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18223257"
FT VARIANT 39
FT /note="H -> Q (in dbSNP:rs34655398)"
FT /id="VAR_043140"
FT VARIANT 48
FT /note="A -> D (in dbSNP:rs3816527)"
FT /evidence="ECO:0000269|PubMed:1429570,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7679696,
FT ECO:0000269|PubMed:8131794"
FT /id="VAR_043141"
FT VARIANT 290
FT /note="A -> V (in dbSNP:rs35415718)"
FT /id="VAR_043142"
FT VARIANT 313
FT /note="E -> K (in dbSNP:rs4478039)"
FT /id="VAR_043143"
FT CONFLICT 202
FT /note="M -> L (in Ref. 3; AAA61234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 41976 MW; 09BCE02E2A62D62A CRC64;
MHLLAILFCA LWSAVLAENS DDYDLMYVNL DNEIDNGLHP TEDPTPCACG QEHSEWDKLF
IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL
LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE
TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL
SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH
IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR
GNIVGWGVTE IQPHGGAQYV S
