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C-reactive protein

 CRP_RAT                 Reviewed;         230 AA.
P48199; Q5BK94;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
23-MAY-2018, entry version 144.
RecName: Full=C-reactive protein;
Flags: Precursor;
Name=Crp; Synonyms=Ptx1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1737750;
Rassouli M., Sambasivam H., Azadi P., Dell A., Morris H.R.,
Nagpurkar A., Mookerjea S., Murray R.K.;
"Derivation of the amino acid sequence of rat C-reactive protein from
cDNA cloning with additional studies on the nature of its dimeric
component.";
J. Biol. Chem. 267:2947-2954(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 65-74 AND 196-205, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
-!- FUNCTION: Displays several functions associated with host defense:
it promotes agglutination, bacterial capsular swelling,
phagocytosis and complement fixation through its calcium-dependent
binding to phosphorylcholine. Can interact with DNA and histones
and may scavenge nuclear material released from damaged
circulating cells (By similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 2 calcium ions per subunit. {ECO:0000250};
-!- SUBUNIT: Homopentamer; disulfide-linked. Pentraxin (or pentaxin)
have a discoid arrangement of 5 non-covalently bound subunits. Two
of the five chains form a dimer linked by two interchain disulfide
bonds located in the C-terminal heptapeptide and specific to rat
CRP. Interacts with FCN1; may regulate monocyte activation by FCN1
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Found in plasma.
-!- PTM: The last two cysteines are involved either in interchain
disulfide bonds or in an intrachain bond.
-!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=No more Christmas
pudding? - Issue 30 of January 2003;
URL="https://web.expasy.org/spotlight/back_issues/030";
-----------------------------------------------------------------------
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EMBL; M83176; AAA40964.1; -; mRNA.
EMBL; BC091157; AAH91157.1; -; mRNA.
PIR; A42579; A42579.
RefSeq; NP_058792.1; NM_017096.3.
UniGene; Rn.16463; -.
ProteinModelPortal; P48199; -.
SMR; P48199; -.
STRING; 10116.ENSRNOP00000000058; -.
GlyConnect; 114; -.
UniCarbKB; P48199; -.
PaxDb; P48199; -.
PRIDE; P48199; -.
Ensembl; ENSRNOT00000000058; ENSRNOP00000000058; ENSRNOG00000000053.
GeneID; 25419; -.
KEGG; rno:25419; -.
UCSC; RGD:2411; rat.
CTD; 1401; -.
RGD; 2411; Crp.
eggNOG; ENOG410J9V0; Eukaryota.
eggNOG; ENOG410YIJN; LUCA.
GeneTree; ENSGT00910000144007; -.
HOGENOM; HOG000247043; -.
HOVERGEN; HBG005405; -.
InParanoid; P48199; -.
KO; K16143; -.
OMA; NEILIFW; -.
PhylomeDB; P48199; -.
TreeFam; TF330208; -.
PRO; PR:P48199; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000000053; -.
ExpressionAtlas; P48199; baseline and differential.
Genevisible; P48199; RN.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0030175; C:filopodium; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0015485; F:cholesterol binding; IDA:RGD.
GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0006953; P:acute-phase response; IEP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0071277; P:cellular response to calcium ion; IDA:RGD.
GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
GO; GO:0071732; P:cellular response to nitric oxide; IEP:RGD.
GO; GO:0006958; P:complement activation, classical pathway; IMP:RGD.
GO; GO:0032929; P:negative regulation of superoxide anion generation; IDA:RGD.
GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:RGD.
GO; GO:0051258; P:protein polymerization; IDA:RGD.
GO; GO:2000482; P:regulation of interleukin-8 secretion; ISS:UniProtKB.
GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; IDA:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0033574; P:response to testosterone; IEP:RGD.
GO; GO:0042060; P:wound healing; IMP:RGD.
CDD; cd00152; PTX; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR030476; Pentaxin_CS.
InterPro; IPR001759; Pentraxin-related.
Pfam; PF00354; Pentaxin; 1.
PRINTS; PR00895; PENTAXIN.
SMART; SM00159; PTX; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00289; PTX_1; 1.
PROSITE; PS51828; PTX_2; 1.
1: Evidence at protein level;
Acute phase; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Metal-binding; Reference proteome;
Secreted; Signal.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 230 C-reactive protein.
/FTId=PRO_0000023532.
DOMAIN 24 223 Pentraxin (PTX). {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 78 78 Calcium 1. {ECO:0000250}.
METAL 155 155 Calcium 1. {ECO:0000250}.
METAL 155 155 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 156 156 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 157 157 Calcium 1. {ECO:0000250}.
METAL 157 157 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 167 167 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000154.
DISULFID 55 114 {ECO:0000255|PROSITE-ProRule:PRU01172}.
DISULFID 227 228 In monomeric form.
DISULFID 227 227 Interchain; in polymeric form.
DISULFID 228 228 Interchain; in polymeric form.
SEQUENCE 230 AA; 25468 MW; D8CF6BFE72376309 CRC64;
MEKLLWCLLI TISFSQAFGH EDMSKQAFVF PGVSATAYVS LEAESKKPLE AFTVCLYAHA
DVSRSFSIFS YATKTSFNEI LLFWTRGQGF SIAVGGPEIL FSASEIPEVP THICATWESA
TGIVELWLDG KPRVRKSLQK GYIVGTNASI ILGQEQDSYG GGFDANQSLV GDIGDVNMWD
FVLSPEQINA VYVGRVFSPN VLNWRALKYE THGDVFIKPQ LWPLTDCCES


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