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 02-OCT-2024, entry version 241. 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; 29. DR DIP; DIP-46911N; -. DR IntAct; P02743; 20. 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 GlyCosmos; P02743; 2 sites, 15 glycans. 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 OGP; P02743; -. DR REPRODUCTION-2DPAGE; IPI00022391; -. DR REPRODUCTION-2DPAGE; P02743; -. DR jPOST; P02743; -. DR MassIVE; P02743; -. DR PaxDb; 9606-ENSP00000255040; -. DR PeptideAtlas; P02743; -. DR ProteomicsDB; 51560; -. DR ABCD; P02743; 1 sequenced antibody. DR Antibodypedia; 3590; 661 antibodies from 39 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 AGR; HGNC:584; -. 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; ENSGT01100000263515; -. DR HOGENOM; CLU_032051_2_0_1; -. DR InParanoid; P02743; -. DR OMA; NPNILDW; -. DR OrthoDB; 4219275at2759; -. 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 1143 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 cell types or tissues. DR ExpressionAtlas; P02743; baseline and differential. 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 Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR030476; Pentaxin_CS. DR InterPro; IPR001759; Pentraxin-related. DR InterPro; IPR051005; Pentraxin_domain. DR PANTHER; PTHR45869; C-REACTIVE PROTEIN-RELATED; 1. DR PANTHER; PTHR45869:SF5; SERUM AMYLOID P-COMPONENT; 1. DR Pfam; PF00354; Pentaxin; 1. DR PRINTS; PR00895; PENTAXIN. DR SMART; SM00159; PTX; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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; Proteomics identification; KW 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 //