ID   CRP_MOUSE               Reviewed;         225 AA.
AC   P14847; E9PZ20;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=C-reactive protein;
DE   Flags: Precursor;
GN   Name=Crp; Synonyms=Ptx1;
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 [GENOMIC DNA].
RX   PubMed=3190681; DOI=10.1016/s0006-291x(88)80917-3;
RA   Ohnishi S., Maeda S., Nishiguchi S., Arao T., Shimada K.;
RT   "Structure of the mouse C-reactive protein gene.";
RL   Biochem. Biophys. Res. Commun. 156:814-822(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CBA/J; TISSUE=Liver;
RX   PubMed=2310378; DOI=10.1042/bj2660283;
RA   Whitehead A.S., Zahedi K., Rits M., Mortensen R.F., Lelias J.M.;
RT   "Mouse C-reactive protein. Generation of cDNA clones, structural analysis,
RT   and induction of mRNA during inflammation.";
RL   Biochem. J. 266:283-290(1990).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Liver, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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.
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. Pentraxin (or pentaxin) have a discoid
CC       arrangement of 5 non-covalently bound subunits. Interacts with FCN1;
CC       may regulate monocyte activation by FCN1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Found in plasma.
CC   -!- INDUCTION: The concentration of CRP in plasma increases greatly during
CC       acute phase response to tissue injury, infection or other inflammatory
CC       stimuli.
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; X13588; CAA31928.1; -; Genomic_DNA.
DR   EMBL; AC131177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X17496; CAA35531.1; -; mRNA.
DR   CCDS; CCDS35787.1; -.
DR   PIR; A31583; A31583.
DR   RefSeq; NP_031794.3; NM_007768.4.
DR   AlphaFoldDB; P14847; -.
DR   SMR; P14847; -.
DR   BioGRID; 198899; 3.
DR   STRING; 10090.ENSMUSP00000044665; -.
DR   PhosphoSitePlus; P14847; -.
DR   CPTAC; non-CPTAC-3331; -.
DR   MaxQB; P14847; -.
DR   PaxDb; 10090-ENSMUSP00000044665; -.
DR   ProteomicsDB; 284175; -.
DR   Antibodypedia; 3561; 2251 antibodies from 49 providers.
DR   DNASU; 12944; -.
DR   Ensembl; ENSMUST00000038495.5; ENSMUSP00000044665.4; ENSMUSG00000037942.6.
DR   GeneID; 12944; -.
DR   KEGG; mmu:12944; -.
DR   UCSC; uc011wwq.1; mouse.
DR   AGR; MGI:88512; -.
DR   CTD; 1401; -.
DR   MGI; MGI:88512; Crp.
DR   VEuPathDB; HostDB:ENSMUSG00000037942; -.
DR   eggNOG; ENOG502S201; Eukaryota.
DR   GeneTree; ENSGT01100000263515; -.
DR   HOGENOM; CLU_032051_2_0_1; -.
DR   InParanoid; P14847; -.
DR   OMA; MEKLLWC; -.
DR   OrthoDB; 4219275at2759; -.
DR   PhylomeDB; P14847; -.
DR   TreeFam; TF330208; -.
DR   Reactome; R-MMU-173623; Classical antibody-mediated complement activation.
DR   BioGRID-ORCS; 12944; 4 hits in 78 CRISPR screens.
DR   ChiTaRS; Crp; mouse.
DR   PRO; PR:P14847; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P14847; Protein.
DR   Bgee; ENSMUSG00000037942; Expressed in left lobe of liver and 33 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0030175; C:filopodium; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR   GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR   GO; GO:0001849; F:complement component C1q complex binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR   GO; GO:0006958; P:complement activation, classical pathway; ISO:MGI.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0010888; P:negative regulation of lipid storage; ISO:MGI.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR   GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; ISO:MGI.
DR   GO; GO:0032929; P:negative regulation of superoxide anion generation; ISO:MGI.
DR   GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR   GO; GO:0051258; P:protein polymerization; ISO:MGI.
DR   GO; GO:0032677; P:regulation of interleukin-8 production; ISS:UniProtKB.
DR   GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; ISO:MGI.
DR   GO; GO:0042310; P:vasoconstriction; ISO:MGI.
DR   CDD; cd00152; PTX; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR030476; Pentaxin_CS.
DR   InterPro; IPR001759; Pentraxin-related.
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.
DR   Genevisible; P14847; MM.
PE   1: Evidence at protein level;
KW   Acute phase; Calcium; Disulfide bond; Metal-binding; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..225
FT                   /note="C-reactive protein"
FT                   /id="PRO_0000023529"
FT   DOMAIN          24..225
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         80
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         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   DISULFID        55..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   CONFLICT        134
FT                   /note="P -> A (in Ref. 1; CAA31928)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="S -> N (in Ref. 1; CAA31928 and 3; CAA35531)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   225 AA;  25360 MW;  0E5FC77BEB8052D8 CRC64;
     MEKLLWCLLI MISFSRTFGH EDMFKKAFVF PKESDTSYVS LEAESKKPLN TFTVCLHFYT
     ALSTVRSFSV FSYATKKNSN DILIFWNKDK QYTFGVGGAE VRFMVSEIPE APTHICASWE
     SATGIVEFWI DGKPKVRKSL HKGYTVGPDA SIILGQEQDS YGGDFDAKQS LVGDIGDVNM
     WDFVLSPEQI STVYVGGTLS PNVLNWRALN YKAQGDVFIK PQLWS
//