CRP_HUMAN
ID CRP_HUMAN Reviewed; 224 AA.
AC P02741; A8K078; D3DVD9; D3DVE0; Q08AK3; Q8WW75;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 239.
DE RecName: Full=C-reactive protein;
DE Contains:
DE RecName: Full=C-reactive protein(1-205);
DE Flags: Precursor;
GN Name=CRP; Synonyms=PTX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2997165; DOI=10.1016/s0021-9258(17)38880-4;
RA Lei K.-J., Liu T., Zon G., Soravia E., Liu T.-Y., Goldman N.D.;
RT "Genomic DNA sequence for human C-reactive protein.";
RL J. Biol. Chem. 260:13377-13383(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3840479; DOI=10.1016/s0021-9258(17)38881-6;
RA Woo P., Korenberg J.R., Whitehead A.S.;
RT "Characterization of genomic and complementary DNA sequence of human C-
RT reactive protein, and comparison with the complementary DNA sequence of
RT serum amyloid P component.";
RL J. Biol. Chem. 260:13384-13388(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Murphy T.M., Baum L., Beaman K.;
RT "Extrahepetic transcription of human C-reactive protein.";
RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Tenchini M.L., Marchetti L., Bossi E., Malcovati M., Lorenzetti R.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Harraghy N.;
RT "Controlled gene expression using acute phase response elements.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-26.
RX PubMed=6685157;
RA Tucci A., Goldberger G., Whitehead A.S., Kay R.M., Woods D.E., Colten H.R.;
RT "Biosynthesis and postsynthetic processing of human C-reactive protein.";
RL J. Immunol. 131:2416-2419(1983).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 144-175.
RX PubMed=6857266; DOI=10.1126/science.6857266;
RA Whitehead A.S., Bruns G.A.P., Markham A.F., Colten H.R., Woods D.E.;
RT "Isolation of human C-reactive protein complementary DNA and localization
RT of the gene to chromosome 1.";
RL Science 221:69-71(1983).
RN [13]
RP PROTEIN SEQUENCE OF 19-224, AND PYROGLUTAMATE FORMATION AT GLN-19.
RX PubMed=762075; DOI=10.1016/s0021-9258(17)37943-7;
RA Oliveira E.B., Gotschlich E.C., Liu T.-Y.;
RT "Primary structure of human C-reactive protein.";
RL J. Biol. Chem. 254:489-502(1979).
RN [14]
RP PROTEIN SEQUENCE OF 22-55.
RX PubMed=403526; DOI=10.1073/pnas.74.3.1214;
RA Osmand A.P., Gewurz H., Friedenson B.;
RT "Partial amino-acid sequences of human and rabbit C-reactive proteins:
RT homology with immunoglobulins and histocompatibility antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:1214-1218(1977).
RN [15]
RP MASS SPECTROMETRY.
RA Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.;
RT "Selected expression profiling of full-length proteins and their variants
RT in human plasma.";
RL Clin. Proteomics 1:7-16(2004).
RN [16]
RP INTERACTION WITH FCN1.
RX PubMed=21037097; DOI=10.4049/jimmunol.1001225;
RA Zhang J., Yang L., Ang Z., Yoong S.L., Tran T.T., Anand G.S., Tan N.S.,
RA Ho B., Ding J.L.;
RT "Secreted M-ficolin anchors onto monocyte transmembrane G protein-coupled
RT receptor 43 and cross talks with plasma C-reactive protein to mediate
RT immune signaling and regulate host defense.";
RL J. Immunol. 185:6899-6910(2010).
RN [17]
RP 3D-STRUCTURE MODELING.
RX PubMed=7881902; DOI=10.1016/s0969-2126(94)00105-7;
RA Srinivasan N., White H.E., Emsley J., Wood S.P., Pepys M.B., Blundell T.L.;
RT "Comparative analyses of pentraxins: implications for protomer assembly and
RT ligand binding.";
RL Structure 2:1017-1027(1994).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=8599761; DOI=10.1038/nsb0496-346;
RA Shrive A.K., Cheetham G.M.T., Holden D., Myles D.A.A., Turnell W.G.,
RA Volanakis J.E., Pepys M.B., Bloomer A.C., Greenhough T.J.;
RT "Three dimensional structure of human C-reactive protein.";
RL Nat. Struct. Biol. 3:346-353(1996).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10368284; DOI=10.1016/s0969-2126(99)80023-9;
RA Thompson D., Pepys M.B., Wood S.P.;
RT "The physiological structure of human C-reactive protein and its complex
RT with phosphocholine.";
RL Structure 7:169-177(1999).
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.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
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.
CC {ECO:0000269|PubMed:21037097}.
CC -!- INTERACTION:
CC P02741; P08603: CFH; NbExp=39; IntAct=EBI-1395983, EBI-1223708;
CC P02741; P08603-1: CFH; NbExp=3; IntAct=EBI-1395983, EBI-22027829;
CC P02741; P08603-2: CFH; NbExp=8; IntAct=EBI-1395983, EBI-12684810;
CC P02741; PRO_0000005894 [P08603]: CFH; NbExp=5; IntAct=EBI-1395983, EBI-22114230;
CC P02741; Q03591: CFHR1; NbExp=10; IntAct=EBI-1395983, EBI-3935840;
CC P02741; Q02985: CFHR3; NbExp=2; IntAct=EBI-1395983, EBI-3941903;
CC P02741; Q92496-1: CFHR4; NbExp=23; IntAct=EBI-1395983, EBI-22033617;
CC P02741; Q92496-3: CFHR4; NbExp=5; IntAct=EBI-1395983, EBI-22033638;
CC P02741; PRO_0000005900 [Q9BXR6]: CFHR5; NbExp=5; IntAct=EBI-1395983, EBI-22114654;
CC P02741; P02741: CRP; NbExp=9; IntAct=EBI-1395983, EBI-1395983;
CC P02741; P31995: FCGR2C; NbExp=2; IntAct=EBI-1395983, EBI-1396036;
CC P02741; O00602: FCN1; NbExp=4; IntAct=EBI-1395983, EBI-5282479;
CC P02741; Q96IJ6: GMPPA; NbExp=3; IntAct=EBI-1395983, EBI-750953;
CC P02741; P02769: ALB; Xeno; NbExp=2; IntAct=EBI-1395983, EBI-2296927;
CC PRO_0000023526; P04003: C4BPA; NbExp=4; IntAct=EBI-22033103, EBI-978348;
CC PRO_0000023526; P08603: CFH; NbExp=3; IntAct=EBI-22033103, EBI-1223708;
CC PRO_0000023526; P27918: CFP; NbExp=2; IntAct=EBI-22033103, EBI-9038570;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P02741-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P02741-2; Sequence=VSP_004656;
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. It is induced by IL1/interleukin-1 and IL6/interleukin-6.
CC -!- MASS SPECTROMETRY: [C-reactive protein]: Mass=23028; Method=MALDI;
CC Evidence={ECO:0000269|Ref.15};
CC -!- MASS SPECTROMETRY: [C-reactive protein(1-205)]: Mass=22930;
CC Method=MALDI; Evidence={ECO:0000269|Ref.15};
CC -!- MISCELLANEOUS: This protein owes its name to its ability precipitate
CC pneumococcal C-polysaccharide in the presence of calcium.
CC -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=C-reactive protein entry;
CC URL="https://en.wikipedia.org/wiki/C-reactive_protein";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/crp/";
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; M11880; AAB59526.1; -; Genomic_DNA.
DR EMBL; M11725; AAA52075.1; -; Genomic_DNA.
DR EMBL; X56692; CAA40020.1; -; mRNA.
DR EMBL; X56214; CAA39671.1; -; mRNA.
DR EMBL; AF442818; AAL48218.2; -; Genomic_DNA.
DR EMBL; AK289443; BAF82132.1; -; mRNA.
DR EMBL; AF449713; AAL40835.1; -; Genomic_DNA.
DR EMBL; AL445528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52778.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52779.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52780.1; -; Genomic_DNA.
DR EMBL; BC020766; AAH20766.1; -; mRNA.
DR EMBL; BC125135; AAI25136.1; -; mRNA.
DR EMBL; M35163; AAA52076.1; -; mRNA.
DR EMBL; K00518; AAA52074.1; -; mRNA.
DR CCDS; CCDS30911.1; -. [P02741-1]
DR CCDS; CCDS86024.1; -. [P02741-2]
DR PIR; A24515; CJHU.
DR RefSeq; NP_000558.2; NM_000567.2. [P02741-1]
DR RefSeq; NP_001315986.1; NM_001329057.1. [P02741-1]
DR RefSeq; NP_001315987.1; NM_001329058.1. [P02741-2]
DR PDB; 1B09; X-ray; 2.50 A; A/B/C/D/E=19-224.
DR PDB; 1GNH; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=19-224.
DR PDB; 1LJ7; X-ray; 3.15 A; A/B/C/D/E/F/G/H/I/J=19-224.
DR PDB; 3L2Y; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=19-224.
DR PDB; 3PVN; X-ray; 1.98 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=19-224.
DR PDB; 3PVO; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=19-224.
DR PDB; 7PK9; EM; 2.80 A; A/B/C/D/E/F/G/H/I/J=19-224.
DR PDB; 7PKB; EM; 3.20 A; A/B/C/D/E=19-224.
DR PDB; 7PKD; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J=19-224.
DR PDB; 7PKE; EM; 3.30 A; A/B/C/D/E=19-224.
DR PDB; 7PKF; EM; 2.80 A; A/B/C/D/E/F/G/H/I/J=19-224.
DR PDB; 7PKG; EM; 3.30 A; A/B/C/D/E=19-224.
DR PDB; 7PKH; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J=19-224.
DR PDBsum; 1B09; -.
DR PDBsum; 1GNH; -.
DR PDBsum; 1LJ7; -.
DR PDBsum; 3L2Y; -.
DR PDBsum; 3PVN; -.
DR PDBsum; 3PVO; -.
DR PDBsum; 7PK9; -.
DR PDBsum; 7PKB; -.
DR PDBsum; 7PKD; -.
DR PDBsum; 7PKE; -.
DR PDBsum; 7PKF; -.
DR PDBsum; 7PKG; -.
DR PDBsum; 7PKH; -.
DR AlphaFoldDB; P02741; -.
DR SMR; P02741; -.
DR BioGRID; 107791; 71.
DR DIP; DIP-39125N; -.
DR IntAct; P02741; 61.
DR MINT; P02741; -.
DR STRING; 9606.ENSP00000255030; -.
DR DrugBank; DB05744; CRx-139.
DR DrugBank; DB03945; N,N,N-Trimethyl-2-(phosphonooxy)ethanaminium.
DR UniLectin; P02741; -.
DR iPTMnet; P02741; -.
DR PhosphoSitePlus; P02741; -.
DR BioMuta; CRP; -.
DR DMDM; 117486; -.
DR DOSAC-COBS-2DPAGE; P02741; -.
DR SWISS-2DPAGE; P02741; -.
DR CPTAC; CPTAC-1478; -.
DR jPOST; P02741; -.
DR MassIVE; P02741; -.
DR PaxDb; P02741; -.
DR PeptideAtlas; P02741; -.
DR PRIDE; P02741; -.
DR ProteomicsDB; 51558; -. [P02741-1]
DR ProteomicsDB; 51559; -. [P02741-2]
DR ABCD; P02741; 8 sequenced antibodies.
DR Antibodypedia; 3561; 2091 antibodies from 49 providers.
DR CPTC; P02741; 1 antibody.
DR DNASU; 1401; -.
DR Ensembl; ENST00000255030.9; ENSP00000255030.5; ENSG00000132693.12. [P02741-1]
DR Ensembl; ENST00000368112.5; ENSP00000357093.1; ENSG00000132693.12. [P02741-2]
DR GeneID; 1401; -.
DR KEGG; hsa:1401; -.
DR MANE-Select; ENST00000255030.9; ENSP00000255030.5; NM_000567.3; NP_000558.2.
DR UCSC; uc001ftw.3; human. [P02741-1]
DR CTD; 1401; -.
DR DisGeNET; 1401; -.
DR GeneCards; CRP; -.
DR HGNC; HGNC:2367; CRP.
DR HPA; ENSG00000132693; Tissue enriched (liver).
DR MIM; 123260; gene.
DR neXtProt; NX_P02741; -.
DR OpenTargets; ENSG00000132693; -.
DR PharmGKB; PA120; -.
DR VEuPathDB; HostDB:ENSG00000132693; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR GeneTree; ENSGT01050000244822; -.
DR HOGENOM; CLU_032051_2_0_1; -.
DR InParanoid; P02741; -.
DR OMA; MEKLLWC; -.
DR OrthoDB; 1088298at2759; -.
DR PhylomeDB; P02741; -.
DR TreeFam; TF330208; -.
DR PathwayCommons; P02741; -.
DR Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
DR SignaLink; P02741; -.
DR SIGNOR; P02741; -.
DR BioGRID-ORCS; 1401; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; CRP; human.
DR EvolutionaryTrace; P02741; -.
DR GeneWiki; C-reactive_protein; -.
DR GenomeRNAi; 1401; -.
DR Pharos; P02741; Tbio.
DR PRO; PR:P02741; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P02741; protein.
DR Bgee; ENSG00000132693; Expressed in right lobe of liver and 86 other tissues.
DR ExpressionAtlas; P02741; baseline and differential.
DR Genevisible; P02741; HS.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0033265; F:choline binding; TAS:BHF-UCL.
DR GO; GO:0001849; F:complement component C1q complex binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:AgBase.
DR GO; GO:0006953; P:acute-phase response; TAS:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; TAS:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010888; P:negative regulation of lipid storage; IDA:BHF-UCL.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
DR GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; IDA:CACAO.
DR GO; GO:0008228; P:opsonization; TAS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:AgBase.
DR GO; GO:0032677; P:regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0042310; P:vasoconstriction; IDA:GO_Central.
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 3D-structure; Acute phase; Alternative splicing; Calcium;
KW Direct protein sequencing; Disulfide bond; Metal-binding;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:762075"
FT CHAIN 19..224
FT /note="C-reactive protein"
FT /id="PRO_0000023526"
FT CHAIN 19..223
FT /note="C-reactive protein(1-205)"
FT /id="PRO_0000023527"
FT DOMAIN 23..224
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:762075"
FT DISULFID 54..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172,
FT ECO:0000269|PubMed:762075"
FT VAR_SEQ 67..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_004656"
FT CONFLICT 49
FT /note="K -> G (in Ref. 14; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="T -> G (in Ref. 14; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..82
FT /note="YSIFSYATKRQDNEIL -> TVFSRMPPRDKTMRFF (in Ref. 4;
FT CAA39671)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..98
FT /note="Missing (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> V (in Ref. 12; AAA52074)"
FT /evidence="ECO:0000305"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 48..60
FT /evidence="ECO:0007829|PDB:3PVN"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:3PVN"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:3PVN"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:1LJ7"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:7PKH"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:7PKG"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:3PVN"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3PVN"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1B09"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3PVN"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3PVN"
SQ SEQUENCE 224 AA; 25039 MW; 669228636A8544F6 CRC64;
MEKLLCFLVL TSLSHAFGQT DMSRKAFVFP KESDTSYVSL KAPLTKPLKA FTVCLHFYTE
LSSTRGYSIF SYATKRQDNE ILIFWSKDIG YSFTVGGSEI LFEVPEVTVA PVHICTSWES
ASGIVEFWVD GKPRVRKSLK KGYTVGAEAS IILGQEQDSF GGNFEGSQSL VGDIGNVNMW
DFVLSPDEIN TIYLGGPFSP NVLNWRALKY EVQGEVFTKP QLWP
