CRP_PIG
ID CRP_PIG Reviewed; 222 AA.
AC O19062;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=C-reactive protein;
DE Flags: Precursor;
GN Name=CRP; Synonyms=PTX1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Landrace; TISSUE=Liver;
RA Ozawa A., Matsumoto M., Kajikawa M., Hanazono M., Yasue H.;
RT "Complementary DNA sequence of porcine C-reactive protein (CRP).";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15566474; DOI=10.1111/j.1365-2052.2004.01192.x;
RA Chomdej S., Ponsuksili S., Schellander K., Wimmers K.;
RT "Detection of SNPs and linkage and radiation hybrid mapping of the porcine
RT C-reactive protein (CRP) gene.";
RL Anim. Genet. 35:469-470(2004).
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 {ECO:0000250}.
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. {ECO:0000250}.
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; AB005545; BAA21473.1; -; mRNA.
DR EMBL; AY714055; AAU13779.1; -; mRNA.
DR RefSeq; NP_999009.1; NM_213844.2.
DR AlphaFoldDB; O19062; -.
DR SMR; O19062; -.
DR STRING; 9823.ENSSSCP00000029570; -.
DR PaxDb; O19062; -.
DR PeptideAtlas; O19062; -.
DR Ensembl; ENSSSCT00025007241; ENSSSCP00025002973; ENSSSCG00025005374.
DR GeneID; 396842; -.
DR KEGG; ssc:396842; -.
DR CTD; 1401; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR InParanoid; O19062; -.
DR OrthoDB; 1088298at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001849; F:complement component C1q complex binding; IBA:GO_Central.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0032677; P:regulation of interleukin-8 production; ISS:UniProtKB.
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;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..222
FT /note="C-reactive protein"
FT /id="PRO_0000023530"
FT DOMAIN 24..222
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 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P02741"
FT DISULFID 55..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 222 AA; 24925 MW; 451B7959DD5F8E9B CRC64;
MEKLSLCLLV IISLSNAFAQ TDMIGKAFVF PKESENSYVS LTARLTKPLT AFTVCLRVYT
DLNRDYSLFS YATKTQYNEI LLFRGKTAVY SISVGGADVV FKPHQSSEPM HFCMTWESTS
GITELWVDGK PMVRRSLKRG YSLGTQASII LGQEQDAFAG GFEKNQCLVG DIGDVNMWDY
VLSPEEINTV YAGGTFSPNV LNWRALRYEM SGEVYVKPQL WP
