CRP_CAVPO
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 03-AUG-2022, entry version 130.
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; ENSCPOP00000011841; ENSCPOG00000013154.
DR GeneID; 100727100; -.
DR KEGG; cpoc:100727100; -.
DR CTD; 1401; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR GeneTree; ENSGT01050000244822; -.
DR HOGENOM; CLU_032051_2_0_1; -.
DR InParanoid; P49254; -.
DR OMA; MEKLLWC; -.
DR OrthoDB; 1088298at2759; -.
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 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 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
