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Protein

Pentraxin-related protein PTX3

Gene

PTX3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility.By similarity

GO - Molecular functioni

  • (1->3)-beta-D-glucan binding Source: Ensembl
  • complement component C1q binding Source: BHF-UCL
  • virion binding Source: BHF-UCL

GO - Biological processi

  • inflammatory response Source: ProtInc
  • innate immune response Source: BHF-UCL
  • negative regulation by host of viral exo-alpha-sialidase activity Source: BHF-UCL
  • negative regulation by host of viral glycoprotein metabolic process Source: BHF-UCL
  • negative regulation of exo-alpha-sialidase activity Source: BHF-UCL
  • negative regulation of glycoprotein metabolic process Source: BHF-UCL
  • negative regulation of viral entry into host cell Source: BHF-UCL
  • opsonization Source: Ensembl
  • positive regulation of nitric oxide biosynthetic process Source: Ensembl
  • positive regulation of phagocytosis Source: Ensembl
  • response to yeast Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Pentraxin-related protein PTX3
Alternative name(s):
Pentaxin-related protein PTX3
Tumor necrosis factor alpha-induced protein 5
Short name:
TNF alpha-induced protein 5
Tumor necrosis factor-inducible gene 14 protein
Short name:
TSG-14
Gene namesi
Name:PTX3
Synonyms:TNFAIP5, TSG14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9692. PTX3.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: ProtInc
  • extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34036.

Polymorphism and mutation databases

BioMutaiPTX3.
DMDMi296452984.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 381364Pentraxin-related protein PTX3PRO_0000023545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 – 47Interchain1 Publication
Disulfide bondi49 – 49Interchain1 Publication
Disulfide bondi103 – 103Interchain1 Publication
Disulfide bondi179 ↔ 3571 Publication
Disulfide bondi210 ↔ 2711 Publication
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi317 – 317Interchain1 Publication
Disulfide bondi318 – 318Interchain1 Publication

Post-translational modificationi

Glycosylated.Curated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP26022.
PaxDbiP26022.
PRIDEiP26022.

PTM databases

PhosphoSiteiP26022.

Miscellaneous databases

PMAP-CutDBB2R6T6.

Expressioni

Inductioni

By IL1B/interleukin-1 beta and TNF.

Gene expression databases

BgeeiP26022.
CleanExiHS_PTX3.
GenevisibleiP26022. HS.

Interactioni

Subunit structurei

Homooctamer; disulfide-linked. Binds to C1q (By similarity).By similarity

Protein-protein interaction databases

BioGridi111770. 2 interactions.
STRINGi9606.ENSP00000295927.

Structurei

3D structure databases

ProteinModelPortaliP26022.
SMRiP26022. Positions 182-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 381199PentaxinAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili74 – 10128Sequence AnalysisAdd
BLAST
Coiled coili143 – 16725Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 pentaxin domain.Curated

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG40461.
GeneTreeiENSGT00760000119128.
HOGENOMiHOG000247046.
HOVERGENiHBG008331.
InParanoidiP26022.
OMAiCHIRGNI.
OrthoDBiEOG74XS6F.
PhylomeDBiP26022.
TreeFamiTF330208.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001759. Pentaxin.
IPR030476. Pentaxin_CS.
[Graphical view]
PfamiPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00895. PENTAXIN.
SMARTiSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00289. PENTAXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26022-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLLAILFCA LWSAVLAENS DDYDLMYVNL DNEIDNGLHP TEDPTPCACG
60 70 80 90 100
QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA
110 120 130 140 150
RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA
160 170 180 190 200
AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR
210 220 230 240 250
PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG
260 270 280 290 300
GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH
310 320 330 340 350
IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE
360 370 380
TGGAESCHIR GNIVGWGVTE IQPHGGAQYV S
Length:381
Mass (Da):41,976
Last modified:May 18, 2010 - v3
Checksum:i09BCE02E2A62D62A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021M → L in AAA61234 (PubMed:7679696).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391H → Q.
Corresponds to variant rs34655398 [ dbSNP | Ensembl ].
VAR_043140
Natural varianti48 – 481A → D.4 Publications
Corresponds to variant rs3816527 [ dbSNP | Ensembl ].
VAR_043141
Natural varianti290 – 2901A → V.
Corresponds to variant rs35415718 [ dbSNP | Ensembl ].
VAR_043142
Natural varianti313 – 3131E → K.
Corresponds to variant rs4478039 [ dbSNP | Ensembl ].
VAR_043143

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63613 mRNA. Translation: CAA45158.1.
X63053 mRNA. Translation: CAA44778.1.
M31166 mRNA. Translation: AAA61234.1.
DQ207368 Genomic DNA. Translation: ABA64467.1.
AK312705 mRNA. Translation: BAG35583.1.
AC020630 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78708.1.
BC039733 mRNA. Translation: AAH39733.1.
CCDSiCCDS3180.1.
PIRiA44323.
RefSeqiNP_002843.2. NM_002852.3.
UniGeneiHs.591286.

Genome annotation databases

EnsembliENST00000295927; ENSP00000295927; ENSG00000163661.
GeneIDi5806.
KEGGihsa:5806.
UCSCiuc003fbl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63613 mRNA. Translation: CAA45158.1.
X63053 mRNA. Translation: CAA44778.1.
M31166 mRNA. Translation: AAA61234.1.
DQ207368 Genomic DNA. Translation: ABA64467.1.
AK312705 mRNA. Translation: BAG35583.1.
AC020630 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78708.1.
BC039733 mRNA. Translation: AAH39733.1.
CCDSiCCDS3180.1.
PIRiA44323.
RefSeqiNP_002843.2. NM_002852.3.
UniGeneiHs.591286.

3D structure databases

ProteinModelPortaliP26022.
SMRiP26022. Positions 182-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111770. 2 interactions.
STRINGi9606.ENSP00000295927.

PTM databases

PhosphoSiteiP26022.

Polymorphism and mutation databases

BioMutaiPTX3.
DMDMi296452984.

Proteomic databases

MaxQBiP26022.
PaxDbiP26022.
PRIDEiP26022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295927; ENSP00000295927; ENSG00000163661.
GeneIDi5806.
KEGGihsa:5806.
UCSCiuc003fbl.4. human.

Organism-specific databases

CTDi5806.
GeneCardsiGC03P157154.
H-InvDBHIX0024325.
HGNCiHGNC:9692. PTX3.
MIMi602492. gene.
neXtProtiNX_P26022.
PharmGKBiPA34036.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40461.
GeneTreeiENSGT00760000119128.
HOGENOMiHOG000247046.
HOVERGENiHBG008331.
InParanoidiP26022.
OMAiCHIRGNI.
OrthoDBiEOG74XS6F.
PhylomeDBiP26022.
TreeFamiTF330208.

Miscellaneous databases

GeneWikiiPTX3.
GenomeRNAii5806.
NextBioi22632.
PMAP-CutDBB2R6T6.
PROiP26022.
SOURCEiSearch...

Gene expression databases

BgeeiP26022.
CleanExiHS_PTX3.
GenevisibleiP26022. HS.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001759. Pentaxin.
IPR030476. Pentaxin_CS.
[Graphical view]
PfamiPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00895. PENTAXIN.
SMARTiSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00289. PENTAXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Interleukin-1-inducible genes in endothelial cells. Cloning of a new gene related to C-reactive protein and serum amyloid P component."
    Breviario F., D'Aniello E.M., Golay J., Peri G., Bottazi B., Bairoch A., Saccone S., Marzella R., Predazzi V., Rocchi M., Della Valle G., Dejana E., Mantovani A., Introna M.
    J. Biol. Chem. 267:22190-22197(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-48.
    Tissue: Endothelial cell.
  2. "IL-1 inducible genes in human umbilical vein endothelial cells."
    Introna M., Breviario F., D'Aniello E.M., Golay J., Dejana E., Mantovani A.
    Eur. Heart J. 14:78-81(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-48.
    Tissue: Endothelial cell.
  3. "TSG-14, a tumor necrosis factor- and IL-1-inducible protein, is a novel member of the pentaxin family of acute phase proteins."
    Lee G.W., Lee T.H., Vilcek J.
    J. Immunol. 150:1804-1812(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-48.
    Tissue: Foreskin.
  4. "Genetic variation in pentaxin-related protein PTX3."
    Tan J., Davila S., Hibberd M.L., Seielstad M.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-48.
    Tissue: Brain.
  9. "Relationship of TSG-14 protein to the pentraxin family of major acute phase proteins."
    Lee G.W., Goodman A.R., Lee T.H., Vilcek J.
    J. Immunol. 153:3700-3707(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.
  10. "Pentraxin 3, a non-redundant soluble pattern recognition receptor involved in innate immunity."
    Mantovani A., Garlanda C., Bottazzi B.
    Vaccine 21:S43-S47(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. Cited for: SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiPTX3_HUMAN
AccessioniPrimary (citable) accession number: P26022
Secondary accession number(s): B2R6T6, Q38M82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 18, 2010
Last modified: June 24, 2015
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.