PTX4_MOUSE
ID PTX4_MOUSE Reviewed; 478 AA.
AC Q6RUU0; Q08EL0; Q148B7; Q14BG6; Q9D1A3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Pentraxin-4;
DE Flags: Precursor;
GN Name=Ptx4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/Sv;
RA Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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 [LARGE SCALE MRNA] OF 148-478 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20357257; DOI=10.4049/jimmunol.0901672;
RA Martinez de la Torre Y., Fabbri M., Jaillon S., Bastone A., Nebuloni M.,
RA Vecchi A., Mantovani A., Garlanda C.;
RT "Evolution of the pentraxin family: the new entry PTX4.";
RL J. Immunol. 184:5055-5064(2010).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6RUU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6RUU0-2; Sequence=VSP_031705;
CC Name=3;
CC IsoId=Q6RUU0-3; Sequence=VSP_031704;
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level). Widely
CC expressed at low levels with highest levels in liver.
CC {ECO:0000269|PubMed:20357257}.
CC -!- INDUCTION: Induced by lipopolysaccharide (LPS) in thymus. Down-
CC regulated by LPS in liver, lung, heart, spleen, dendritic cells and
CC peritoneal macrophages. Induced by TNF-alpha in dendritic cells and
CC peritoneal macrophages. {ECO:0000269|PubMed:20357257}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB22989.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY491413; AAS21645.1; -; Genomic_DNA.
DR EMBL; BC107380; AAI07381.1; -; mRNA.
DR EMBL; BC107381; AAI07382.1; -; mRNA.
DR EMBL; BC115902; AAI15903.1; -; mRNA.
DR EMBL; BC118508; AAI18509.1; -; mRNA.
DR EMBL; AK003777; BAB22989.1; ALT_FRAME; mRNA.
DR RefSeq; XP_006524909.1; XM_006524846.3.
DR AlphaFoldDB; Q6RUU0; -.
DR SMR; Q6RUU0; -.
DR STRING; 10090.ENSMUSP00000055984; -.
DR GlyGen; Q6RUU0; 1 site.
DR MaxQB; Q6RUU0; -.
DR PaxDb; Q6RUU0; -.
DR PRIDE; Q6RUU0; -.
DR ProteomicsDB; 302027; -. [Q6RUU0-1]
DR ProteomicsDB; 302028; -. [Q6RUU0-2]
DR MGI; MGI:1915759; Ptx4.
DR eggNOG; ENOG502QTID; Eukaryota.
DR InParanoid; Q6RUU0; -.
DR PhylomeDB; Q6RUU0; -.
DR BioGRID-ORCS; 68509; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q6RUU0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6RUU0; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001759; Pentraxin-related.
DR Pfam; PF00354; Pentaxin; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..478
FT /note="Pentraxin-4"
FT /id="PRO_0000320646"
FT DOMAIN 269..473
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 300..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT VAR_SEQ 1..291
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031704"
FT VAR_SEQ 48..77
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031705"
FT CONFLICT 34
FT /note="R -> S (in Ref. 2; AAI07381/AAI18509)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="R -> G (in Ref. 1; AAS21645 and 2; AAI07381/
FT AAI15903/AAI18509)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="L -> F (in Ref. 1; AAS21645 and 2; AAI07381/
FT AAI15903/AAI18509)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="P -> PYATP (in Ref. 3; BAB22989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 53150 MW; 825AFD007D350608 CRC64;
MRCLKKKTLL FLLIFVSLNV HRTPSQEAHP ARQRKPFFER LRRLEEQFQR FQQVTLTHLQ
NIANNYNVYH NMDVRFQSLV EQSQAVALAM NQSQAAIQGD VAHLKTWYRK SQRRSRKVDA
RLQALDLSLS TKSRQWVEKE GEQKAQREAI ASLALSVQAL QDALASLTQQ VHSQGARLAA
LEGQTQSASS GTVALGLTTA PTPTQLAQRG PGSLQLWRDR QVAKSSPQHR SSPHDVTVHV
QEMQKFQTPS SHQAAPPRTY QGPGNICNTD PVLIFPNTST ENVIFLSPGF LMPLRALSFC
SWVRMATSHL GTLLSYATKD NDNKLVLHGR NSLVPGSIHF VIGDPDFREL SLKPLLDGQW
HHICIIWTSV EGKYWLHIDR RLVATGSRFR EGYEIPPGGS LVLGQEQDTV GGEFDSSEAF
VGSISGLAIW DRALLPREVA NLASGKELPT GAILTLTNVT SVGGFVQRAK CTCLEQCP
