ID   CRP_RAT                 Reviewed;         230 AA.
AC   P48199; Q5BK94;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 178.
DE   RecName: Full=C-reactive protein;
DE   Flags: Precursor;
GN   Name=Crp; Synonyms=Ptx1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=1737750; DOI=10.1016/s0021-9258(19)50678-0;
RA   Rassouli M., Sambasivam H., Azadi P., Dell A., Morris H.R., Nagpurkar A.,
RA   Mookerjea S., Murray R.K.;
RT   "Derivation of the amino acid sequence of rat C-reactive protein from cDNA
RT   cloning with additional studies on the nature of its dimeric component.";
RL   J. Biol. Chem. 267:2947-2954(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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   PROTEIN SEQUENCE OF 65-74 AND 196-205, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
CC   -!- FUNCTION: Displays several functions associated with host defense: it
CC       promotes agglutination, bacterial capsular swelling, phagocytosis and
CC       complement fixation through its calcium-dependent binding to
CC       phosphorylcholine. Can interact with DNA and histones and may scavenge
CC       nuclear material released from damaged circulating cells (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homopentamer; disulfide-linked. Pentraxin (or pentaxin) have a
CC       discoid arrangement of 5 non-covalently bound subunits. Two of the five
CC       chains form a dimer linked by two interchain disulfide bonds located in
CC       the C-terminal heptapeptide and specific to rat CRP. Interacts with
CC       FCN1; may regulate monocyte activation by FCN1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Found in plasma.
CC   -!- PTM: The last two cysteines are involved either in interchain disulfide
CC       bonds or in an intrachain bond.
CC   -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=No more Christmas pudding?
CC       - Issue 30 of January 2003;
CC       URL="https://www.proteinspotlight.org/back_issues/030";
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DR   EMBL; M83176; AAA40964.1; -; mRNA.
DR   EMBL; BC091157; AAH91157.1; -; mRNA.
DR   PIR; A42579; A42579.
DR   RefSeq; NP_058792.1; NM_017096.4.
DR   AlphaFoldDB; P48199; -.
DR   SMR; P48199; -.
DR   BioGRID; 247454; 1.
DR   FunCoup; P48199; 21.
DR   IntAct; P48199; 1.
DR   MINT; P48199; -.
DR   STRING; 10116.ENSRNOP00000074751; -.
DR   GlyConnect; P48199; 2 N-Linked glycans (1 site).
DR   GlyCosmos; P48199; 1 site, 4 glycans.
DR   GlyGen; P48199; 1 site, 4 N-linked glycans (1 site).
DR   iPTMnet; P48199; -.
DR   PhosphoSitePlus; P48199; -.
DR   PaxDb; 10116-ENSRNOP00000074751; -.
DR   GeneID; 25419; -.
DR   KEGG; rno:25419; -.
DR   UCSC; RGD:2411; rat.
DR   AGR; RGD:2411; -.
DR   CTD; 1401; -.
DR   RGD; 2411; Crp.
DR   VEuPathDB; HostDB:ENSRNOG00000000053; -.
DR   eggNOG; ENOG502S201; Eukaryota.
DR   HOGENOM; CLU_032051_2_0_1; -.
DR   InParanoid; P48199; -.
DR   PhylomeDB; P48199; -.
DR   Reactome; R-RNO-173623; Classical antibody-mediated complement activation.
DR   PRO; PR:P48199; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000000053; Expressed in liver and 17 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IDA:RGD.
DR   GO; GO:0030175; C:filopodium; IDA:RGD.
DR   GO; GO:0030426; C:growth cone; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR   GO; GO:0015485; F:cholesterol binding; IDA:RGD.
DR   GO; GO:0001849; F:complement component C1q complex binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:RGD.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
DR   GO; GO:0006953; P:acute-phase response; IEP:RGD.
DR   GO; GO:0071277; P:cellular response to calcium ion; IDA:RGD.
DR   GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
DR   GO; GO:0071732; P:cellular response to nitric oxide; IEP:RGD.
DR   GO; GO:0006958; P:complement activation, classical pathway; IMP:RGD.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0010888; P:negative regulation of lipid storage; ISO:RGD.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR   GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; ISO:RGD.
DR   GO; GO:0032929; P:negative regulation of superoxide anion generation; IDA:RGD.
DR   GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:RGD.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:RGD.
DR   GO; GO:0051258; P:protein polymerization; IDA:RGD.
DR   GO; GO:0032677; P:regulation of interleukin-8 production; ISS:UniProtKB.
DR   GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; IDA:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR   GO; GO:0042310; P:vasoconstriction; ISO:RGD.
DR   CDD; cd00152; PTX; 1.
DR   FunFam; 2.60.120.200:FF:000070; Serum amyloid P-component; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR030476; Pentaxin_CS.
DR   InterPro; IPR051005; Pentraxin_domain.
DR   InterPro; IPR001759; PTX_dom.
DR   PANTHER; PTHR45869:SF7; C-REACTIVE PROTEIN; 1.
DR   PANTHER; PTHR45869; C-REACTIVE PROTEIN-RELATED; 1.
DR   Pfam; PF00354; Pentaxin; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00289; PTX_1; 1.
DR   PROSITE; PS51828; PTX_2; 1.
PE   1: Evidence at protein level;
KW   Acute phase; Calcium; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..230
FT                   /note="C-reactive protein"
FT                   /id="PRO_0000023532"
FT   DOMAIN          24..223
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         156
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /id="CAR_000154"
FT   DISULFID        55..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   DISULFID        227..228
FT                   /note="In monomeric form"
FT   DISULFID        227
FT                   /note="Interchain; in polymeric form"
FT   DISULFID        228
FT                   /note="Interchain; in polymeric form"
SQ   SEQUENCE   230 AA;  25468 MW;  D8CF6BFE72376309 CRC64;
     MEKLLWCLLI TISFSQAFGH EDMSKQAFVF PGVSATAYVS LEAESKKPLE AFTVCLYAHA
     DVSRSFSIFS YATKTSFNEI LLFWTRGQGF SIAVGGPEIL FSASEIPEVP THICATWESA
     TGIVELWLDG KPRVRKSLQK GYIVGTNASI ILGQEQDSYG GGFDANQSLV GDIGDVNMWD
     FVLSPEQINA VYVGRVFSPN VLNWRALKYE THGDVFIKPQ LWPLTDCCES
//