Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

C-reactive protein

Gene

CRP

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi80Calcium 1By similarity1
Metal bindingi158Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi159Calcium 1By similarity1
Metal bindingi159Calcium 2By similarity1
Metal bindingi169Calcium 2By similarity1

GO - Molecular functioni

GO - Biological processi

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000002353121 – 225C-reactive protein1 PublicationAdd BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi55 ↔ 1161 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Found in plasma.

Inductioni

The concentration of CRP in plasma increases greatly during acute phase response to tissue injury, infection or other inflammatory stimuli.

Interactioni

Subunit structurei

Homopentamer. Pentaxin (or pentraxin) have a discoid arrangement of 5 non-covalently bound subunits. Interacts with FCN1; may regulate monocyte activation by FCN1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000004059.

Structurei

3D structure databases

ProteinModelPortaliP02742.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 225PentaxinAdd BLAST205

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J9V0. Eukaryota.
ENOG410YIJN. LUCA.
HOGENOMiHOG000247043.
HOVERGENiHBG005405.
InParanoidiP02742.
KOiK16143.

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.

P02742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKLLWCFLT LVSFSNMSDQ AGMHKKAFVF PKESDNSYVS LNAQLKKPLK
60 70 80 90 100
AFTVCLYFYT DLSMTRGYSI FSYATRRQFN EILLFWSKDI GYSFSVGGDE
110 120 130 140 150
IIFKVSDIPV DPTHLCASWE SSTGIAELWV DGKPMVRKSL KKGYILGPEA
160 170 180 190 200
SIILGQDQDS FGGSFEKQQS LVGDIGNVNM WDYALSPEEI NTIYAGGTFS
210 220
PNVLDWRELT YQVRGEVHVK PQLWP
Length:225
Mass (Da):25,493
Last modified:January 1, 1988 - v1
Checksum:iC6D634FDE844438F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10T → I in AAA31206 (PubMed:3007506).Curated1
Sequence conflicti46K → T AA sequence (PubMed:6754715).Curated1
Sequence conflicti50K → L AA sequence (PubMed:6754715).Curated1
Sequence conflicti76R → K in AAA75404 (PubMed:3026463).Curated1
Sequence conflicti84 – 88LFWSK → FFVKE AA sequence (PubMed:6754715).Curated5
Sequence conflicti91G → V AA sequence (PubMed:6754715).Curated1
Sequence conflicti93 – 101Missing AA sequence (PubMed:6754715).Curated9
Sequence conflicti108I → V in AAA31206 (PubMed:3007506).Curated1
Sequence conflicti167K → W AA sequence (PubMed:6754715).Curated1
Sequence conflicti177N → D AA sequence (PubMed:6754715).Curated1
Sequence conflicti193I → V in AAA31206 (PubMed:3007506).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti62L → K.1
Natural varianti89D → V.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14538 Genomic DNA. Translation: AAA75403.1.
L47237 mRNA. Translation: AAA75404.1.
M13497 mRNA. Translation: AAA31206.1.
PIRiA25605. CJRB.
RefSeqiNP_001075734.1. NM_001082265.1.
UniGeneiOcu.1848.

Genome annotation databases

GeneIDi100009091.
KEGGiocu:100009091.

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
M14538 Genomic DNA. Translation: AAA75403.1.
L47237 mRNA. Translation: AAA75404.1.
M13497 mRNA. Translation: AAA31206.1.
PIRiA25605. CJRB.
RefSeqiNP_001075734.1. NM_001082265.1.
UniGeneiOcu.1848.

3D structure databases

ProteinModelPortaliP02742.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000004059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009091.
KEGGiocu:100009091.

Organism-specific databases

CTDi1401.

Phylogenomic databases

eggNOGiENOG410J9V0. Eukaryota.
ENOG410YIJN. LUCA.
HOGENOMiHOG000247043.
HOVERGENiHBG005405.
InParanoidiP02742.
KOiK16143.

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_RABIT
AccessioniPrimary (citable) accession number: P02742
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: November 30, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Asp-61, Arg-76, Arg-77, and Glu-81 may be involved in the calcium-dependent binding of phosphorylcholine, a property that may be important for the biological function of this protein.

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.