SAMP_HUMAN
ID SAMP_HUMAN Reviewed; 223 AA.
AC P02743;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Serum amyloid P-component;
DE Short=SAP;
DE AltName: Full=9.5S alpha-1-glycoprotein;
DE Contains:
DE RecName: Full=Serum amyloid P-component(1-203);
DE Flags: Precursor;
GN Name=APCS; Synonyms=PTX2;
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 [MRNA].
RX PubMed=2987268; DOI=10.1016/s0021-9258(17)39671-0;
RA Mantzouranis E.C., Dowton S.B., Whitehead A.S., Edge M.D., Bruns G.A.P.,
RA Colten H.R.;
RT "Human serum amyloid P component. cDNA isolation, complete sequence of pre-
RT serum amyloid P component, and localization of the gene to chromosome 1.";
RL J. Biol. Chem. 260:7752-7756(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3029048; DOI=10.1093/oxfordjournals.jbchem.a121797;
RA Ohnishi S., Maeda S., Shimada K., Arao T.;
RT "Isolation and characterization of the complete complementary and genomic
RT DNA sequences of human serum amyloid P component.";
RL J. Biochem. 100:849-858(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [7]
RP PROTEIN SEQUENCE OF 20-223.
RX PubMed=4055725; DOI=10.1016/s0021-9258(17)38809-9;
RA Prelli F., Pras M., Frangione B.;
RT "The primary structure of human tissue amyloid P component from a patient
RT with primary idiopathic amyloidosis.";
RL J. Biol. Chem. 260:12895-12898(1985).
RN [8]
RP PROTEIN SEQUENCE OF 20-49.
RX PubMed=81686; DOI=10.1021/bi00613a030;
RA Thompson A.R., Enfield D.L.;
RT "Human plasma P component: isolation and characterization.";
RL Biochemistry 17:4304-4311(1978).
RN [9]
RP STRUCTURE OF CARBOHYDRATE, AND MASS SPECTROMETRY.
RX PubMed=8202534; DOI=10.1073/pnas.91.12.5602;
RA Pepys M.B., Rademacher T.W., Amatayakul-Chantler S., Williams P.,
RA Noble G.E., Hutchinson W.L., Hawkins P.N., Nelson S.R., Gallimore J.R.,
RA Herbert J., Hutton T., Dwek R.A.;
RT "Human serum amyloid P component is an invariant constituent of amyloid
RT deposits and has a uniquely homogeneous glycostructure.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5602-5606(1994).
RN [10]
RP TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RX PubMed=15174148; DOI=10.1002/pmic.200300690;
RA Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.;
RT "Proteomic characterization of novel serum amyloid P component variants
RT from human plasma and urine.";
RL Proteomics 4:1825-1829(2004).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8114934; DOI=10.1038/367338a0;
RA Emsley J., White H.E., O'Hara B., Oliva G., Srinivasan N., Tickle I.J.,
RA Blundell T.L., Pepys M.B., Wood S.P.;
RT "Structure of pentameric human serum amyloid P component.";
RL Nature 367:338-345(1994).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=9217261; DOI=10.1006/jmbi.1997.1075;
RA Hohenester E., Hutchinson W.L., Pepys M.B., Wood S.P.;
RT "Crystal structure of a decameric complex of human serum amyloid P
RT component with bound dAMP.";
RL J. Mol. Biol. 269:570-578(1997).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] SER-141.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Can interact with DNA and histones and may scavenge nuclear
CC material released from damaged circulating cells. May also function as
CC a calcium-dependent lectin.
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.
CC -!- INTERACTION:
CC P02743; Q15699: ALX1; NbExp=3; IntAct=EBI-2115799, EBI-750671;
CC P02743; P02743: APCS; NbExp=8; IntAct=EBI-2115799, EBI-2115799;
CC P02743; P05067: APP; NbExp=3; IntAct=EBI-2115799, EBI-77613;
CC P02743; Q9Y5P4-1: CERT1; NbExp=6; IntAct=EBI-2115799, EBI-21199571;
CC P02743; Q9Y5P4-2: CERT1; NbExp=4; IntAct=EBI-2115799, EBI-11156432;
CC P02743; P11226: MBL2; NbExp=2; IntAct=EBI-2115799, EBI-5325353;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Found in serum and urine.
CC {ECO:0000269|PubMed:15174148}.
CC -!- PTM: N-glycosylated with a complex biantennary oligosaccharide chain
CC with a sialic acid at the end (disialo-SAP). Monosialo-SAP as well as
CC asioalo-SAP are also detected (PubMed:15174148).
CC {ECO:0000269|PubMed:15174148, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19159218}.
CC -!- MASS SPECTROMETRY: [Serum amyloid P-component]: Mass=25462.5;
CC Mass_error=1.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15174148, ECO:0000269|PubMed:8202534};
CC -!- MASS SPECTROMETRY: [Serum amyloid P-component]: Mass=25463;
CC Mass_error=3; Method=MALDI; Evidence={ECO:0000269|PubMed:15174148,
CC ECO:0000269|PubMed:8202534};
CC -!- DISEASE: Note=SAP is a precursor of amyloid component P which is found
CC in basement membrane and associated with amyloid deposits.
CC -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Serum amyloid P component entry;
CC URL="https://en.wikipedia.org/wiki/Serum_Amyloid_P_Component";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D00097; BAA00060.1; -; Genomic_DNA.
DR EMBL; M10944; AAA60302.1; -; mRNA.
DR EMBL; X04608; CAA28275.1; -; mRNA.
DR EMBL; CR450313; CAG29309.1; -; mRNA.
DR EMBL; AL445528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT006750; AAP35396.1; -; mRNA.
DR EMBL; BC007039; AAH07039.1; -; mRNA.
DR EMBL; BC007058; AAH07058.1; -; mRNA.
DR CCDS; CCDS1186.1; -.
DR PIR; A25503; YLHUP.
DR RefSeq; NP_001630.1; NM_001639.3.
DR PDB; 1GYK; X-ray; 2.20 A; A/B/C/D/E=20-223.
DR PDB; 1LGN; X-ray; 2.80 A; A/B/C/D/E=20-223.
DR PDB; 1SAC; X-ray; 2.00 A; A/B/C/D/E=20-223.
DR PDB; 2A3W; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=20-223.
DR PDB; 2A3X; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=20-223.
DR PDB; 2A3Y; X-ray; 2.00 A; A/B/C/D/E=20-223.
DR PDB; 2W08; X-ray; 1.70 A; A/B/C/D/E=20-223.
DR PDB; 3D5O; X-ray; 2.80 A; A/B/C/D/E=20-223.
DR PDB; 3KQR; X-ray; 1.50 A; A/B/C/D/E=20-223.
DR PDB; 4AVS; X-ray; 1.40 A; A/B/C/D/E=20-223.
DR PDB; 4AVT; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J=20-223.
DR PDB; 4AVV; X-ray; 1.60 A; A/B/C/D/E=20-223.
DR PDB; 4AYU; X-ray; 1.50 A; A/B/C/D/E=20-223.
DR PDBsum; 1GYK; -.
DR PDBsum; 1LGN; -.
DR PDBsum; 1SAC; -.
DR PDBsum; 2A3W; -.
DR PDBsum; 2A3X; -.
DR PDBsum; 2A3Y; -.
DR PDBsum; 2W08; -.
DR PDBsum; 3D5O; -.
DR PDBsum; 3KQR; -.
DR PDBsum; 4AVS; -.
DR PDBsum; 4AVT; -.
DR PDBsum; 4AVV; -.
DR PDBsum; 4AYU; -.
DR AlphaFoldDB; P02743; -.
DR SMR; P02743; -.
DR BioGRID; 106822; 28.
DR DIP; DIP-46911N; -.
DR IntAct; P02743; 11.
DR MINT; P02743; -.
DR STRING; 9606.ENSP00000255040; -.
DR ChEMBL; CHEMBL4929; -.
DR DrugBank; DB07579; Bis-1,2-{[(Z)-2-carboxy-2-methyl-1,3-dioxane]-5-yloxycarbamoyl}-ethane.
DR DrugBank; DB07580; BIS-1,2-{[(Z)-2CARBOXY-2-METHYL-1,3-DIOXANE]-5-YLOXYCARBONYL}-PIPERAZINE.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01651; Methyl 4,6-O-[(1R)-1-carboxyethylidene]-beta-D-galactopyranoside.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR GuidetoPHARMACOLOGY; 2839; -.
DR TCDB; 1.C.92.1.2; the pentraxin (pentraxin) family.
DR UniLectin; P02743; -.
DR CarbonylDB; P02743; -.
DR GlyConnect; 560; 12 N-Linked glycans (1 site).
DR GlyGen; P02743; 2 sites, 14 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P02743; -.
DR PhosphoSitePlus; P02743; -.
DR BioMuta; APCS; -.
DR DMDM; 730704; -.
DR DOSAC-COBS-2DPAGE; P02743; -.
DR OGP; P02743; -.
DR REPRODUCTION-2DPAGE; IPI00022391; -.
DR REPRODUCTION-2DPAGE; P02743; -.
DR SWISS-2DPAGE; P02743; -.
DR jPOST; P02743; -.
DR MassIVE; P02743; -.
DR PaxDb; P02743; -.
DR PeptideAtlas; P02743; -.
DR PRIDE; P02743; -.
DR ProteomicsDB; 51560; -.
DR ABCD; P02743; 1 sequenced antibody.
DR Antibodypedia; 3590; 617 antibodies from 38 providers.
DR DNASU; 325; -.
DR Ensembl; ENST00000255040.3; ENSP00000255040.2; ENSG00000132703.4.
DR GeneID; 325; -.
DR KEGG; hsa:325; -.
DR MANE-Select; ENST00000255040.3; ENSP00000255040.2; NM_001639.4; NP_001630.1.
DR CTD; 325; -.
DR DisGeNET; 325; -.
DR GeneCards; APCS; -.
DR HGNC; HGNC:584; APCS.
DR HPA; ENSG00000132703; Tissue enriched (liver).
DR MIM; 104770; gene.
DR neXtProt; NX_P02743; -.
DR OpenTargets; ENSG00000132703; -.
DR PharmGKB; PA24877; -.
DR VEuPathDB; HostDB:ENSG00000132703; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR GeneTree; ENSGT01050000244822; -.
DR HOGENOM; CLU_032051_2_0_1; -.
DR InParanoid; P02743; -.
DR OMA; GFDKSQS; -.
DR OrthoDB; 1088298at2759; -.
DR PhylomeDB; P02743; -.
DR TreeFam; TF330208; -.
DR PathwayCommons; P02743; -.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P02743; -.
DR BioGRID-ORCS; 325; 16 hits in 1065 CRISPR screens.
DR ChiTaRS; APCS; human.
DR EvolutionaryTrace; P02743; -.
DR GeneWiki; Serum_amyloid_P_component; -.
DR GenomeRNAi; 325; -.
DR Pharos; P02743; Tchem.
DR PRO; PR:P02743; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P02743; protein.
DR Bgee; ENSG00000132703; Expressed in right lobe of liver and 94 other tissues.
DR ExpressionAtlas; P02743; baseline and differential.
DR Genevisible; P02743; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0046790; F:virion binding; IDA:BHF-UCL.
DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; IDA:BHF-UCL.
DR GO; GO:0044869; P:negative regulation by host of viral exo-alpha-sialidase activity; IDA:BHF-UCL.
DR GO; GO:0044871; P:negative regulation by host of viral glycoprotein metabolic process; IDA:BHF-UCL.
DR GO; GO:0002674; P:negative regulation of acute inflammatory response; IC:BHF-UCL.
DR GO; GO:1903016; P:negative regulation of exo-alpha-sialidase activity; IDA:BHF-UCL.
DR GO; GO:1903019; P:negative regulation of glycoprotein metabolic process; IDA:BHF-UCL.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; IDA:BHF-UCL.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:BHF-UCL.
DR GO; GO:0048525; P:negative regulation of viral process; IDA:BHF-UCL.
DR GO; GO:0061045; P:negative regulation of wound healing; IC:BHF-UCL.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
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; Amyloid; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lectin; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:4055725,
FT ECO:0000269|PubMed:81686"
FT CHAIN 20..223
FT /note="Serum amyloid P-component"
FT /id="PRO_0000023540"
FT CHAIN 20..222
FT /note="Serum amyloid P-component(1-203)"
FT /id="PRO_0000023541"
FT DOMAIN 24..223
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
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 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT /id="CAR_000169"
FT DISULFID 55..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172,
FT ECO:0000269|PubMed:4055725"
FT VARIANT 141
FT /note="G -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035814"
FT VARIANT 155
FT /note="E -> G"
FT /id="VAR_006054"
FT VARIANT 158
FT /note="S -> G"
FT /id="VAR_006055"
FT CONFLICT 101
FT /note="S -> P (in Ref. 1; AAA60302)"
FT /evidence="ECO:0000305"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:4AVS"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4AVS"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:4AVS"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4AVS"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4AYU"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:4AVS"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:4AVS"
SQ SEQUENCE 223 AA; 25387 MW; 6C88A515FE88B393 CRC64;
MNKPLLWISV LTSLLEAFAH TDLSGKVFVF PRESVTDHVN LITPLEKPLQ NFTLCFRAYS
DLSRAYSLFS YNTQGRDNEL LVYKERVGEY SLYIGRHKVT SKVIEKFPAP VHICVSWESS
SGIAEFWING TPLVKKGLRQ GYFVEAQPKI VLGQEQDSYG GKFDRSQSFV GEIGDLYMWD
SVLPPENILS AYQGTPLPAN ILDWQALNYE IRGYVIIKPL VWV
