CRP_RABIT
ID CRP_RABIT Reviewed; 225 AA.
AC P02742;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=C-reactive protein;
DE Flags: Precursor;
GN Name=CRP; Synonyms=PTX1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=3026463; DOI=10.1021/bi00372a008;
RA Hu S.-I., Miller S.M., Samols D.;
RT "Cloning and characterization of the gene for rabbit C-reactive protein.";
RL Biochemistry 25:7834-7839(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3007506; DOI=10.1016/s0021-9258(19)57240-4;
RA Syin C., Gotschlich E.C., Liu T.-Y.;
RT "Rabbit C-reactive protein. Biosynthesis and characterization of cDNA
RT clones.";
RL J. Biol. Chem. 261:5473-5479(1986).
RN [3]
RP PROTEIN SEQUENCE OF 21-225.
RX PubMed=6754715; DOI=10.1016/s0021-9258(18)33491-4;
RA Wang C.-M., Nguyen N.Y., Yonaha K., Robey F., Liu T.-Y.;
RT "Primary structure of rabbit C-reactive protein.";
RL J. Biol. Chem. 257:13610-13615(1982).
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 -!- INDUCTION: The concentration of CRP in plasma increases greatly during
CC acute phase response to tissue injury, infection or other inflammatory
CC stimuli.
CC -!- MISCELLANEOUS: Asp-61, Arg-76, Arg-77, and Glu-81 may be involved in
CC the calcium-dependent binding of phosphorylcholine, a property that may
CC be important for the biological function of this protein.
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; M14538; AAA75403.1; -; Genomic_DNA.
DR EMBL; L47237; AAA75404.1; -; mRNA.
DR EMBL; M13497; AAA31206.1; -; mRNA.
DR PIR; A25605; CJRB.
DR RefSeq; NP_001075734.1; NM_001082265.1.
DR AlphaFoldDB; P02742; -.
DR SMR; P02742; -.
DR BioGRID; 1172114; 1.
DR STRING; 9986.ENSOCUP00000004059; -.
DR GeneID; 100009091; -.
DR KEGG; ocu:100009091; -.
DR CTD; 1401; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR InParanoid; P02742; -.
DR OrthoDB; 1088298at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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 1: Evidence at protein level;
KW Acute phase; Calcium; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:6754715"
FT CHAIN 21..225
FT /note="C-reactive protein"
FT /evidence="ECO:0000269|PubMed:6754715"
FT /id="PRO_0000023531"
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,
FT ECO:0000269|PubMed:6754715"
FT VARIANT 62
FT /note="L -> K"
FT VARIANT 89
FT /note="D -> V"
FT CONFLICT 10
FT /note="T -> I (in Ref. 2; AAA31206)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="K -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="K -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="R -> K (in Ref. 1; AAA75404)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..88
FT /note="LFWSK -> FFVKE (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="G -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..101
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="I -> V (in Ref. 2; AAA31206)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="K -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="I -> V (in Ref. 2; AAA31206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 25493 MW; C6D634FDE844438F CRC64;
MEKLLWCFLT LVSFSNMSDQ AGMHKKAFVF PKESDNSYVS LNAQLKKPLK AFTVCLYFYT
DLSMTRGYSI FSYATRRQFN EILLFWSKDI GYSFSVGGDE IIFKVSDIPV DPTHLCASWE
SSTGIAELWV DGKPMVRKSL KKGYILGPEA SIILGQDQDS FGGSFEKQQS LVGDIGNVNM
WDYALSPEEI NTIYAGGTFS PNVLDWRELT YQVRGEVHVK PQLWP
