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Protein

C-reactive protein

Gene

Crp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi78Calcium 1By similarity1
Metal bindingi155Calcium 1By similarity1
Metal bindingi155Calcium 2By similarity1
Metal bindingi156Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi157Calcium 1By similarity1
Metal bindingi157Calcium 2By similarity1
Metal bindingi167Calcium 2By similarity1

GO - Molecular functioni

  • cholesterol binding Source: RGD
  • low-density lipoprotein particle binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • acute-phase response Source: RGD
  • aging Source: RGD
  • cellular response to calcium ion Source: RGD
  • cellular response to interleukin-6 Source: RGD
  • cellular response to nitric oxide Source: RGD
  • complement activation, classical pathway Source: RGD
  • negative regulation of superoxide anion generation Source: RGD
  • positive regulation of dendrite development Source: RGD
  • positive regulation of nitric oxide biosynthetic process Source: RGD
  • protein polymerization Source: RGD
  • regulation of interleukin-8 secretion Source: UniProtKB
  • regulation of low-density lipoprotein particle clearance Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to hypoxia Source: RGD
  • response to lead ion Source: RGD
  • response to radiation Source: RGD
  • response to testosterone Source: RGD
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Biological processi

Acute phase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
C-reactive protein
Gene namesi
Name:Crp
Synonyms:Ptx1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi2411. Crp.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
  • filopodium Source: RGD
  • growth cone Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000002353220 – 230C-reactive proteinAdd BLAST211

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi55 ↔ 114
GlycosylationiCAR_000154147N-linked (GlcNAc...)1
Disulfide bondi227 ↔ 228In monomeric form
Disulfide bondi227Interchain; in polymeric form
Disulfide bondi228Interchain; in polymeric form

Post-translational modificationi

The last two cysteines are involved either in interchain disulfide bonds or in an intrachain bond.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP48199.
PRIDEiP48199.

PTM databases

UniCarbKBiP48199.

Expressioni

Tissue specificityi

Found in plasma.

Gene expression databases

BgeeiENSRNOG00000000053.
ExpressionAtlasiP48199. baseline and differential.
GenevisibleiP48199. RN.

Interactioni

Subunit structurei

Homopentamer; disulfide-linked. Pentaxin (or pentraxin) 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).By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000058.

Structurei

3D structure databases

ProteinModelPortaliP48199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 230PentaxinAdd BLAST211

Sequence similaritiesi

Belongs to the pentaxin family.Curated
Contains 1 pentaxin domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J9V0. Eukaryota.
ENOG410YIJN. LUCA.
GeneTreeiENSGT00850000132314.
HOGENOMiHOG000247043.
HOVERGENiHBG005405.
InParanoidiP48199.
KOiK16143.
OMAiTKPLKAF.
PhylomeDBiP48199.
TreeFamiTF330208.

Family and domain databases

CDDicd00152. PTX. 1 hit.
Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001759. Pentaxin-related.
IPR030476. Pentaxin_CS.
[Graphical view]
PfamiPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00895. PENTAXIN.
SMARTiSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00289. PENTAXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48199-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKLLWCLLI TISFSQAFGH EDMSKQAFVF PGVSATAYVS LEAESKKPLE
60 70 80 90 100
AFTVCLYAHA DVSRSFSIFS YATKTSFNEI LLFWTRGQGF SIAVGGPEIL
110 120 130 140 150
FSASEIPEVP THICATWESA TGIVELWLDG KPRVRKSLQK GYIVGTNASI
160 170 180 190 200
ILGQEQDSYG GGFDANQSLV GDIGDVNMWD FVLSPEQINA VYVGRVFSPN
210 220 230
VLNWRALKYE THGDVFIKPQ LWPLTDCCES
Length:230
Mass (Da):25,468
Last modified:February 1, 1996 - v1
Checksum:iD8CF6BFE72376309
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83176 mRNA. Translation: AAA40964.1.
BC091157 mRNA. Translation: AAH91157.1.
PIRiA42579.
RefSeqiNP_058792.1. NM_017096.3.
UniGeneiRn.16463.

Genome annotation databases

EnsembliENSRNOT00000000058; ENSRNOP00000000058; ENSRNOG00000000053.
GeneIDi25419.
KEGGirno:25419.
UCSCiRGD:2411. rat.

Cross-referencesi

Web resourcesi

Protein Spotlight

No more Christmas pudding? - Issue 30 of January 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83176 mRNA. Translation: AAA40964.1.
BC091157 mRNA. Translation: AAH91157.1.
PIRiA42579.
RefSeqiNP_058792.1. NM_017096.3.
UniGeneiRn.16463.

3D structure databases

ProteinModelPortaliP48199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000058.

PTM databases

UniCarbKBiP48199.

Proteomic databases

PaxDbiP48199.
PRIDEiP48199.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000058; ENSRNOP00000000058; ENSRNOG00000000053.
GeneIDi25419.
KEGGirno:25419.
UCSCiRGD:2411. rat.

Organism-specific databases

CTDi1401.
RGDi2411. Crp.

Phylogenomic databases

eggNOGiENOG410J9V0. Eukaryota.
ENOG410YIJN. LUCA.
GeneTreeiENSGT00850000132314.
HOGENOMiHOG000247043.
HOVERGENiHBG005405.
InParanoidiP48199.
KOiK16143.
OMAiTKPLKAF.
PhylomeDBiP48199.
TreeFamiTF330208.

Miscellaneous databases

PROiP48199.

Gene expression databases

BgeeiENSRNOG00000000053.
ExpressionAtlasiP48199. baseline and differential.
GenevisibleiP48199. RN.

Family and domain databases

CDDicd00152. PTX. 1 hit.
Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001759. Pentaxin-related.
IPR030476. Pentaxin_CS.
[Graphical view]
PfamiPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00895. PENTAXIN.
SMARTiSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00289. PENTAXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCRP_RAT
AccessioniPrimary (citable) accession number: P48199
Secondary accession number(s): Q5BK94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.