CRP_MOUSE
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 03-AUG-2022, entry version 172.
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; P14847; -.
DR PRIDE; P14847; -.
DR ProteomicsDB; 284175; -.
DR Antibodypedia; 3561; 2091 antibodies from 49 providers.
DR DNASU; 12944; -.
DR Ensembl; ENSMUST00000038495; ENSMUSP00000044665; ENSMUSG00000037942.
DR GeneID; 12944; -.
DR KEGG; mmu:12944; -.
DR UCSC; uc011wwq.1; mouse.
DR CTD; 1401; -.
DR MGI; MGI:88512; Crp.
DR VEuPathDB; HostDB:ENSMUSG00000037942; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR GeneTree; ENSGT01050000244822; -.
DR HOGENOM; CLU_032051_2_0_1; -.
DR InParanoid; P14847; -.
DR OMA; MEKLLWC; -.
DR OrthoDB; 1088298at2759; -.
DR PhylomeDB; P14847; -.
DR TreeFam; TF330208; -.
DR Reactome; R-MMU-173623; Classical antibody-mediated complement activation.
DR BioGRID-ORCS; 12944; 4 hits in 73 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 tissues.
DR Genevisible; P14847; MM.
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 GO; GO:0042060; P:wound healing; ISO:MGI.
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; 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
