ID   CRP_CAVPO               Reviewed;         225 AA.
AC   P49254;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 135.
DE   RecName: Full=C-reactive protein;
DE   Flags: Precursor;
GN   Name=CRP; Synonyms=PTX1;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hartley;
RX   PubMed=8486600; DOI=10.1093/oxfordjournals.jbchem.a124039;
RA   Rubio N., Sharp P.M., Rits M., Zahedi K., Whitehead A.S.;
RT   "Structure, expression, and evolution of guinea pig serum amyloid P
RT   component and C-reactive protein.";
RL   J. Biochem. 113:277-284(1993).
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. 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   -!- 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; S60422; AAC60662.1; -; Genomic_DNA.
DR   PIR; JX0259; JX0259.
DR   RefSeq; XP_003466601.1; XM_003466553.2.
DR   AlphaFoldDB; P49254; -.
DR   SMR; P49254; -.
DR   STRING; 10141.ENSCPOP00000011841; -.
DR   Ensembl; ENSCPOT00000013281.3; ENSCPOP00000011841.2; ENSCPOG00000013154.4.
DR   GeneID; 100727100; -.
DR   KEGG; cpoc:100727100; -.
DR   CTD; 1401; -.
DR   VEuPathDB; HostDB:ENSCPOG00000013154; -.
DR   eggNOG; ENOG502S201; Eukaryota.
DR   GeneTree; ENSGT01100000263515; -.
DR   HOGENOM; CLU_032051_2_0_1; -.
DR   InParanoid; P49254; -.
DR   OMA; MEKLLWC; -.
DR   OrthoDB; 4219275at2759; -.
DR   TreeFam; TF330208; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000013154; Expressed in liver.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0001849; F:complement component C1q complex binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR   GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0032677; P:regulation of interleukin-8 production; ISS:UniProtKB.
DR   GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
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.
PE   2: Evidence at transcript level;
KW   Acute phase; Calcium; Disulfide bond; Metal-binding; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..225
FT                   /note="C-reactive protein"
FT                   /id="PRO_0000023525"
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         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:0000250"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ   SEQUENCE   225 AA;  25225 MW;  47AF3E2D9A660F2E CRC64;
     MAKLLLYFLL LTSLSDVFGG TDMSKKTFVF PKETDNSYVS LKAQLKKPLS AFTVCLHIYT
     ELFMTRGYSI FSYATEKEAN EILIFWSKDR GYILGVGGIE MPFKAPEIPS APVHICTSWE
     SVSGIIELWV DGKAQVRKSL QKGYFVGTEA MIILGQDQDS FGGSFDANQS FVGDIGDVNM
     WDFVLSPKEI DMVYSGGTFS PNVLSWRSLT YETHGEVFIK PQLWP
//