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PROSITE documentation PDOC00261 [for PROSITE entry PS00289]

Pentraxin (PTX) domain signature and profile





Description

Pentraxins (earlier also termed pentaxins), named for their homopentameric quaternary structure, are a superfamily of multifunctional conserved proteins that are characterized by a cyclic multimeric structure and by the presence in their carboxyl-terminal of an ~200 aa-long conserved domain, called pentraxin (PTX) domain. In addition, all the members of this family share an 8 aa-long conserved sequence (HxCxS/TWxS, in which x is any amino acid) in the pentraxin domain, called pentraxin signature. Some pentraxins, together with collectins and ficolins, constitute the humoral arm of innate immunity and behave as functional ancestors of Abs by mediating agglutination, complement activation, and opsonisation [1,2,3]. They are divided into short:

  • C-reactive protein (CRP), a protein which, in mammals, is expressed during acute phase response to tissue injury or inflammation. CRP displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. CRPs have also been sequenced in an invertebrate, the Atlantic horseshoe crab, where they are a normal constituent of the hemolymph.
  • Serum Amyloid P-component (SAP), a precursor of amyloid component P which is found in basement membrane and is associated with amyloid deposits.
  • Hamster female protein (FP), a plasma protein whose concentration is altered by sex steroids and stimuli that elicit an acute phase response.

and long pentraxins:

  • Human PTX3 (or TSG-14). PTX3 is a cytokine-induced protein.
  • Vertebrate PTX4 [3].
  • Guinea pig apexin [4], a sperm acrosomal protein. Apexin seems to be the ortholog of human neuronal pentraxin II (gene NPTX2) [5].
  • Rat neuronal pentraxin I [6].

The pentraxin domain has also been found in multidomain proteins, such as:

  • Mammalian polydom, an extracellular protein which includes an N-terminal von Willebrand factor A domain (see <PDOC50234>), hyalin repeats (HYRs) (see <PDOC50825>), epidermal growth factor repeats (EGFs) (see <PDOC00021>), sushi domains (see <PDOC50923>), and a single pentraxin domain.
  • Vertebrate adhesion G-protein–coupled receptors (GPRs), in particular GPR144, GPR112, and GPR126.

The function of these proteins has not been defined yet, nor has the role of the pentraxin domain in multidomain proteins.

The pentraxin domain consists of two anti-parallel β-sheets in the form of a flattened β-barrel with a jellyroll topology (see <PDB:3KQR>) [7,8].

The pentraxin domain is related to the laminin G (LamG) (see <PDOC50025>) and thrombospondin N-terminal (TspN) domains [10].

The sequences of the different members of this family are quite conserved. As a signature, we selected a six residue pattern which includes a cysteine known to be involved in a disulfide bridge in CRPs and SAP. We have also developed a profile that covers the entire pentraxin domain.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

January 2017 / Text revised; profile added.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

PTX_1, PS00289; Pentraxin domain signature  (PATTERN)

PTX_2, PS51828; Pentraxin (PTX) domain profile  (MATRIX)


References

1AuthorsPepys M.B. Baltz M.L.
TitleAcute phase proteins with special reference to C-reactive protein and related proteins (pentaxins) and serum amyloid A protein.
SourceAdv. Immunol. 34:141-212(1983).
PubMed ID6356809

2AuthorsGewurz H. Zhang X.H. Lint T.F.
TitleStructure and function of the pentraxins.
SourceCurr. Opin. Immunol. 7:54-64(1995).
PubMed ID7772283

3AuthorsMartinez de la Torre Y. Fabbri M. Jaillon S. Bastone A. Nebuloni M. Vecchi A. Mantovani A. Garlanda C.
TitleEvolution of the pentraxin family: the new entry PTX4.
SourceJ. Immunol. 184:5055-5064(2010).
PubMed ID20357257
DOI10.4049/jimmunol.0901672

4AuthorsReid M.S. Blobel C.P.
TitleApexin, an acrosomal pentaxin.
SourceJ. Biol. Chem. 269:32615-32620(1994).
PubMed ID7798266

5AuthorsHsu Y.-C. Perin M.S.
TitleHuman neuronal pentraxin II (NPTX2): conservation, genomic structure, and chromosomal localization.
SourceGenomics 28:220-227(1995).
PubMed ID8530029

6AuthorsSchlimgen A.K. Helms J.A. Vogel H. Perin M.S.
TitleNeuronal pentraxin, a secreted protein with homology to acute phase proteins of the immune system.
SourceNeuron 14:519-526(1995).
PubMed ID7695898

7AuthorsMikolajek H. Kolstoe S.E. Pye V.E. Mangione P. Pepys M.B. Wood S.P.
TitleStructural basis of ligand specificity in the human pentraxins, C-reactive protein and serum amyloid P component.
SourceJ. Mol. Recognit. 24:371-377(2011).
PubMed ID21360619
DOI10.1002/jmr.1090

8AuthorsShrive A.K. Cheetham G.M.T. Holden D. Myles D.A.A. Turnell W.G. Volanakis J.E. Pepys M.B. Bloomer A.C. Greenhough T.J.
TitleThree dimensional structure of human C-reactive protein.
SourceNat. Struct. Biol. 3:346-354(1996).
PubMed ID8599761

9AuthorsNordstroem K.J. Lagerstroem M.C. Waller L.M. Fredriksson R. Schioeth H.B.
TitleThe Secretin GPCRs descended from the family of Adhesion GPCRs.
SourceMol. Biol. Evol. 26:71-84(2009).
PubMed ID18845549
DOI10.1093/molbev/msn228

10AuthorsBeckmann G. Hanke J. Bork P. Reich J.G.
TitleMerging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins.
SourceJ. Mol. Biol. 275:725-730(1998).
PubMed ID9480764
DOI10.1006/jmbi.1997.1510



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