CRP_MESAU
ID CRP_MESAU Reviewed; 225 AA.
AC P49262;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=C-reactive protein;
DE Flags: Precursor;
GN Name=CRP; Synonyms=PTX1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1892852; DOI=10.1021/bi00103a021;
RA Dowton S.B., Holden S.N.;
RT "C-reactive protein (CRP) of the Syrian hamster.";
RL Biochemistry 30:9531-9538(1991).
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: By interleukin-1, interleukin-6, and TNF-alpha.
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; S56005; AAB19893.2; -; Genomic_DNA.
DR PIR; A40326; A40326.
DR RefSeq; XP_005078251.1; XM_005078194.2.
DR AlphaFoldDB; P49262; -.
DR SMR; P49262; -.
DR STRING; 10036.XP_005078251.1; -.
DR GeneID; 101826636; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR OrthoDB; 1088298at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0001849; F:complement component C1q complex binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR GO; GO:0032677; P:regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
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:0000250"
FT CHAIN 20..225
FT /note="C-reactive protein"
FT /id="PRO_0000023528"
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 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
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:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 169
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..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 225 AA; 24822 MW; 00B439C45D58E05A CRC64;
MEKLLWCSLV MIGFSQAFAQ KDMSKTAFVF PKESANSYVS LEAQSKKTLK AFTVCLHIFT
ELSTTRSFSI FSYATKNSPN EILIFWSKDR GYAFGVGGPE VLFKASEIPE VPTHICASWE
SATGIAELWV DGKPKVRKIL QKGYTVGTDA SIILGQEQDS YGGGFDANQS LVGDIGDVNM
WDIVLSPEQI NTVCVGGTLD PSVLNWQALK YKVQGDVFIK PQLWP
