CRP_RAT
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 03-AUG-2022, entry version 162.
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://web.expasy.org/spotlight/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_017096.3.
DR AlphaFoldDB; P48199; -.
DR SMR; P48199; -.
DR BioGRID; 247454; 1.
DR IntAct; P48199; 1.
DR MINT; P48199; -.
DR STRING; 10116.ENSRNOP00000000058; -.
DR GlyConnect; 114; 2 N-Linked glycans (1 site).
DR GlyGen; P48199; 1 site, 4 N-linked glycans (1 site).
DR PaxDb; P48199; -.
DR PRIDE; P48199; -.
DR GeneID; 25419; -.
DR KEGG; rno:25419; -.
DR UCSC; RGD:2411; rat.
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 OMA; MEKLLWC; -.
DR OrthoDB; 1088298at2759; -.
DR PhylomeDB; P48199; -.
DR TreeFam; TF330208; -.
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 tissues.
DR ExpressionAtlas; P48199; baseline and differential.
DR Genevisible; P48199; RN.
DR GO; GO:0005615; C:extracellular space; 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:0007568; P:aging; 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:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0042310; P:vasoconstriction; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IMP:RGD.
DR CDD; cd00152; PTX; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR030476; Pentaxin_CS.
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; 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
