ID FCER2_HUMAN Reviewed; 321 AA. AC P06734; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 27-MAR-2024, entry version 225. DE RecName: Full=Low affinity immunoglobulin epsilon Fc receptor; DE AltName: Full=BLAST-2; DE AltName: Full=C-type lectin domain family 4 member J; DE AltName: Full=Fc-epsilon-RII; DE AltName: Full=Immunoglobulin E-binding factor; DE AltName: Full=Lymphocyte IgE receptor; DE AltName: CD_antigen=CD23; DE Contains: DE RecName: Full=Low affinity immunoglobulin epsilon Fc receptor membrane-bound form; DE Contains: DE RecName: Full=Low affinity immunoglobulin epsilon Fc receptor soluble form; GN Name=FCER2; Synonyms=CD23A, CLEC4J, FCE2, IGEBF; 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=2949326; DOI=10.1073/pnas.84.3.819; RA Ikuta K., Takami M., Kim C.W., Honjo T., Miyoshi T., Tagaya Y., Kawabe T., RA Yodoi J.; RT "Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA RT with animal lectins."; RL Proc. Natl. Acad. Sci. U.S.A. 84:819-823(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2877743; DOI=10.1016/0092-8674(86)90508-8; RA Kikutani H., Inui S., Sato R., Barsumian E.L., Owaki H., Yamasaki K., RA Kaisho T., Uchibayashi N., Hardy R.R., Hirano T., Tsunasawa S., RA Sakiyama F., Suemura M., Kishimoto T.; RT "Molecular structure of human lymphocyte receptor for immunoglobulin E."; RL Cell 47:657-665(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3034567; DOI=10.1002/j.1460-2075.1987.tb04726.x; RA Luedin C., Hofstetter H., Sarfati M., Levy C.A., Suter U., Alaimo D., RA Kilchherr E., Frost H., Delespesse G.; RT "Cloning and expression of the cDNA coding for a human lymphocyte IgE RT receptor."; RL EMBO J. 6:109-114(1987). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell, and Blood; 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 [6] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2972386; DOI=10.1016/0092-8674(88)90219-x; RA Yokota A., Kikutani H., Tanaka T., Sato R., Barsumian E.L., Suemura M., RA Kishimoto T.; RT "Two species of human Fc epsilon receptor II (Fc epsilon RII/CD23): tissue- RT specific and IL-4-specific regulation of gene expression."; RL Cell 55:611-618(1988). RN [7] RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS. RX PubMed=1417742; DOI=10.1042/bj2860819; RA Rose K., Turcatti G., Graber P., Pochon S., Regamey P.-O., Jansen K.U., RA Magnenat E., Aubonney N., Bonnefoy J.-Y.; RT "Partial characterization of natural and recombinant human soluble CD23."; RL Biochem. J. 286:819-824(1992). RN [8] RP FUNCTION. RX PubMed=2167225; DOI=10.1002/eji.1830200721; RA Pirron U., Schlunck T., Prinz J.C., Rieber E.P.; RT "IgE-dependent antigen focusing by human B lymphocytes is mediated by the RT low-affinity receptor for IgE."; RL Eur. J. Immunol. 20:1547-1551(1990). RN [9] RP FUNCTION. RX PubMed=7544003; DOI=10.1073/pnas.92.17.7804; RA Vouldoukis I., Riveros-Moreno V., Dugas B., Ouaaz F., Becherel P., RA Debre P., Moncada S., Mossalayi M.D.; RT "The killing of Leishmania major by human macrophages is mediated by nitric RT oxide induced after ligation of the Fc epsilon RII/CD23 surface antigen."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7804-7808(1995). RN [10] RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE BY ADAM10. RX PubMed=17389606; DOI=10.1074/jbc.m608414200; RA Lemieux G.A., Blumenkron F., Yeung N., Zhou P., Williams J., Grammer A.C., RA Petrovich R., Lipsky P.E., Moss M.L., Werb Z.; RT "The low affinity IgE receptor (CD23) is cleaved by the metalloproteinase RT ADAM10."; RL J. Biol. Chem. 282:14836-14844(2007). RN [11] RP PALMITOYLATION AT CYS-17 AND CYS-18, AND SUBCELLULAR LOCATION. RC TISSUE=B-cell; RX PubMed=22615937; DOI=10.1371/journal.pone.0037187; RA Ivaldi C., Martin B.R., Kieffer-Jaquinod S., Chapel A., Levade T., RA Garin J., Journet A.; RT "Proteomic analysis of S-acylated proteins in human B cells reveals RT palmitoylation of the immune regulators CD20 and CD23."; RL PLoS ONE 7:E37187-E37187(2012). RN [12] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-296. RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617; RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.; RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected RT Correlation Between Glycan Sulfation and Attachment Site Characteristics."; RL Mol. Cell. Proteomics 22:100617-100617(2023). RN [13] RP 3D-STRUCTURE MODELING OF LECTIN DOMAIN. RX PubMed=8142907; RA Padlan E.A., Helm B.A.; RT "Modeling of the lectin-homology domains of the human and murine low- RT affinity Fc epsilon receptor (Fc epsilon RII/CD23)."; RL Receptor 3:325-341(1993). RN [14] RP 3D-STRUCTURE MODELING OF 173-285. RX PubMed=8745401; DOI=10.1002/pro.5560050207; RA Bajorath J., Aruffo A.; RT "Structure-based modeling of the ligand binding domain of the human cell RT surface receptor CD23 and comparison of two independently derived molecular RT models."; RL Protein Sci. 5:240-247(1996). RN [15] RP STRUCTURE BY NMR OF 156-298, DISULFIDE BONDS, SUBUNIT, AND INTERACTION WITH RP IGHE AND CR2. RX PubMed=16172256; DOI=10.1084/jem.20050811; RA Hibbert R.G., Teriete P., Grundy G.J., Beavil R.L., Reljic R., Holers V.M., RA Hannan J.P., Sutton B.J., Gould H.J., McDonnell J.M.; RT "The structure of human CD23 and its interactions with IgE and CD21."; RL J. Exp. Med. 202:751-760(2005). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 150-321 ALONE AND IN COMPLEX WITH RP CALCIUM, AND DISULFIDE BONDS. RX PubMed=16765898; DOI=10.1016/j.str.2006.03.017; RA Wurzburg B.A., Tarchevskaya S.S., Jardetzky T.S.; RT "Structural changes in the lectin domain of CD23, the low-affinity IgE RT receptor, upon calcium binding."; RL Structure 14:1049-1058(2006). RN [17] RP VARIANT PHE-316. RX PubMed=23424103; DOI=10.1002/ana.23832; RA Hersheson J., Mencacci N.E., Davis M., Macdonald N., Trabzuni D., Ryten M., RA Pittman A., Paudel R., Kara E., Fawcett K., Plagnol V., Bhatia K.P., RA Medlar A.J., Stanescu H.C., Hardy J., Kleta R., Wood N.W., Houlden H.; RT "Mutations in the autoregulatory domain of beta-tubulin 4a cause hereditary RT dystonia."; RL Ann. Neurol. 73:546-553(2013). CC -!- FUNCTION: Low-affinity receptor for immunoglobulin E (IgE) and CC CR2/CD21. Has essential roles in the regulation of IgE production and CC in the differentiation of B cells. On B cells, initiates IgE-dependent CC antigen uptake and presentation to T cells (PubMed:2167225). On CC macrophages, upon IgE binding and antigen cross-linking induces CC intracellular killing of parasites through activation of L-Arginine- CC nitric oxide pathway (PubMed:7544003). {ECO:0000269|PubMed:2167225, CC ECO:0000269|PubMed:7544003}. CC -!- SUBUNIT: Homotrimer. Interacts (via C-type lectin domain) with IGHE CC (via CH3 region); this interaction regulates IgE homeostasis. Interacts CC (via the C-terminus) with CR2/CD21 (via Sushi domain 1 and 2). CC {ECO:0000269|PubMed:16172256, ECO:0000269|PubMed:16765898}. CC -!- INTERACTION: CC P06734; P17544: ATF7; NbExp=3; IntAct=EBI-10199985, EBI-765623; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane CC protein. Cell membrane; Lipid-anchor. Secreted CC {ECO:0000269|PubMed:37453717}. Note=Also exists as a soluble excreted CC form, sCD23. CC -!- TISSUE SPECIFICITY: Detected in urine (at protein level). CC {ECO:0000269|PubMed:37453717}. CC -!- PTM: N- and O-glycosylated. CC -!- PTM: The secreted form sCD23 is produced by ADAM10-mediated ectodomain CC shedding. CC -!- MISCELLANEOUS: There are two kinds of Fc receptors for IgE, which CC differ in both structure and function: high affinity receptors on CC basophils and mast cells and low affinity receptors on lymphocytes and CC monocytes. CC -!- SEQUENCE CAUTION: CC Sequence=AAA52433.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=CD23; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_221"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44222/FCER2"; 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; M15059; AAA52434.1; -; mRNA. DR EMBL; M14766; AAA52435.1; -; mRNA. DR EMBL; X04772; CAA28465.1; -; mRNA. DR EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014108; AAH14108.1; -; mRNA. DR EMBL; BC062591; AAH62591.1; -; mRNA. DR EMBL; M23562; AAA52433.1; ALT_SEQ; Genomic_DNA. DR CCDS; CCDS12184.1; -. DR PIR; A26067; LNHUER. DR RefSeq; NP_001193948.2; NM_001207019.2. DR RefSeq; NP_001207429.1; NM_001220500.1. DR RefSeq; NP_001993.2; NM_002002.4. DR RefSeq; XP_005272519.1; XM_005272462.4. DR PDB; 1T8C; NMR; -; A=156-298. DR PDB; 1T8D; NMR; -; A=156-298. DR PDB; 2H2R; X-ray; 1.50 A; A/B=150-321. DR PDB; 2H2T; X-ray; 1.30 A; B=150-321. DR PDB; 4EZM; X-ray; 3.10 A; G/H/I/J/K/L=156-298. DR PDB; 4G96; X-ray; 2.25 A; A/B/C/D=156-298. DR PDB; 4G9A; X-ray; 2.00 A; A/B/C/D=156-298. DR PDB; 4GI0; X-ray; 2.27 A; A/B/C=156-298. DR PDB; 4GJ0; X-ray; 1.95 A; A/B/C/D=156-298. DR PDB; 4GJX; X-ray; 2.80 A; A/B/C/D/E/F/G/H=156-298. DR PDB; 4GK1; X-ray; 2.24 A; A/B/C/D/E/F/G=156-298. DR PDB; 4GKO; X-ray; 3.30 A; G/H/I/J/K/L=156-298. DR PDB; 4J6J; X-ray; 1.90 A; A/B/C/D=156-298. DR PDB; 4J6K; X-ray; 2.30 A; A/B/C/D/E/F/G/H=156-298. DR PDB; 4J6L; X-ray; 3.15 A; A/B/C/D/E/F/G/H=156-298. DR PDB; 4J6M; X-ray; 2.48 A; A/B/C/D/E/F/G/H=156-298. DR PDB; 4J6N; X-ray; 2.85 A; A/B=156-298. DR PDB; 4J6P; X-ray; 1.90 A; A/B/C/D=156-298. DR PDB; 4J6Q; X-ray; 2.54 A; A=156-298. DR PDB; 4KI1; X-ray; 3.20 A; E/F/G/H=156-298. DR PDB; 5LGK; X-ray; 3.50 A; E/F=165-284. DR PDB; 6Y0L; X-ray; 1.65 A; A=156-298. DR PDB; 6Y0M; X-ray; 1.50 A; A=156-298. DR PDBsum; 1T8C; -. DR PDBsum; 1T8D; -. DR PDBsum; 2H2R; -. DR PDBsum; 2H2T; -. DR PDBsum; 4EZM; -. DR PDBsum; 4G96; -. DR PDBsum; 4G9A; -. DR PDBsum; 4GI0; -. DR PDBsum; 4GJ0; -. DR PDBsum; 4GJX; -. DR PDBsum; 4GK1; -. DR PDBsum; 4GKO; -. DR PDBsum; 4J6J; -. DR PDBsum; 4J6K; -. DR PDBsum; 4J6L; -. DR PDBsum; 4J6M; -. DR PDBsum; 4J6N; -. DR PDBsum; 4J6P; -. DR PDBsum; 4J6Q; -. DR PDBsum; 4KI1; -. DR PDBsum; 5LGK; -. DR PDBsum; 6Y0L; -. DR PDBsum; 6Y0M; -. DR AlphaFoldDB; P06734; -. DR BMRB; P06734; -. DR SMR; P06734; -. DR BioGRID; 108502; 7. DR CORUM; P06734; -. DR IntAct; P06734; 1. DR STRING; 9606.ENSP00000264072; -. DR BindingDB; P06734; -. DR ChEMBL; CHEMBL2940; -. DR DrugBank; DB06162; Lumiliximab. DR GuidetoPHARMACOLOGY; 2935; -. DR UniLectin; P06734; -. DR GlyCosmos; P06734; 2 sites, 1 glycan. DR GlyGen; P06734; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P06734; -. DR PhosphoSitePlus; P06734; -. DR SwissPalm; P06734; -. DR BioMuta; FCER2; -. DR DMDM; 119862; -. DR jPOST; P06734; -. DR MassIVE; P06734; -. DR MaxQB; P06734; -. DR PaxDb; 9606-ENSP00000264072; -. DR PeptideAtlas; P06734; -. DR ProteomicsDB; 51921; -. DR ABCD; P06734; 1 sequenced antibody. DR Antibodypedia; 2294; 1978 antibodies from 51 providers. DR DNASU; 2208; -. DR Ensembl; ENST00000346664.9; ENSP00000264072.6; ENSG00000104921.15. DR Ensembl; ENST00000597921.6; ENSP00000471974.1; ENSG00000104921.15. DR GeneID; 2208; -. DR KEGG; hsa:2208; -. DR MANE-Select; ENST00000597921.6; ENSP00000471974.1; NM_001220500.2; NP_001207429.1. DR UCSC; uc002mhm.3; human. DR AGR; HGNC:3612; -. DR CTD; 2208; -. DR DisGeNET; 2208; -. DR GeneCards; FCER2; -. DR HGNC; HGNC:3612; FCER2. DR HPA; ENSG00000104921; Tissue enriched (lymphoid). DR MIM; 151445; gene. DR neXtProt; NX_P06734; -. DR OpenTargets; ENSG00000104921; -. DR PharmGKB; PA28058; -. DR VEuPathDB; HostDB:ENSG00000104921; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00940000162574; -. DR HOGENOM; CLU_049894_7_2_1; -. DR InParanoid; P06734; -. DR OMA; PRKRCCG; -. DR OrthoDB; 4735139at2759; -. DR PhylomeDB; P06734; -. DR TreeFam; TF333341; -. DR PathwayCommons; P06734; -. DR Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription. DR Reactome; R-HSA-6783783; Interleukin-10 signaling. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR SignaLink; P06734; -. DR SIGNOR; P06734; -. DR BioGRID-ORCS; 2208; 8 hits in 1144 CRISPR screens. DR EvolutionaryTrace; P06734; -. DR GeneWiki; CD23; -. DR GenomeRNAi; 2208; -. DR Pharos; P06734; Tchem. DR PRO; PR:P06734; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P06734; Protein. DR Bgee; ENSG00000104921; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 111 other cell types or tissues. DR ExpressionAtlas; P06734; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central. DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB. DR GO; GO:0005178; F:integrin binding; TAS:ProtInc. DR GO; GO:0019769; F:low-affinity IgE receptor activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0002450; P:B cell antigen processing and presentation; IDA:UniProtKB. DR GO; GO:0160006; P:Fc receptor-mediated immune complex endocytosis; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0042116; P:macrophage activation; IDA:UniProtKB. DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl. DR GO; GO:0051712; P:positive regulation of killing of cells of another organism; IDA:BHF-UCL. DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL. DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL. DR CDD; cd03590; CLECT_DC-SIGN_like; 1. DR DisProt; DP02975; -. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1. DR InterPro; IPR001304; C-type_lectin-like. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR018378; C-type_lectin_CS. DR InterPro; IPR033989; CD209-like_CTLD. DR InterPro; IPR016187; CTDL_fold. DR PANTHER; PTHR22803:SF155; C-TYPE LECTIN DOMAIN CONTAINING 10A; 1. DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR Genevisible; P06734; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell membrane; Direct protein sequencing; KW Disulfide bond; Glycoprotein; IgE-binding protein; Lectin; Lipoprotein; KW Membrane; Metal-binding; Palmitate; Proteoglycan; Receptor; KW Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1..321 FT /note="Low affinity immunoglobulin epsilon Fc receptor FT membrane-bound form" FT /id="PRO_0000017391" FT CHAIN 150..321 FT /note="Low affinity immunoglobulin epsilon Fc receptor FT soluble form" FT /id="PRO_0000017392" FT TOPO_DOM 1..21 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 22..47 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 48..321 FT /note="Extracellular" FT /evidence="ECO:0000255" FT REPEAT 69..89 FT REPEAT 90..110 FT REPEAT 111..131 FT DOMAIN 162..284 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT REGION 66..85 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 290..321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 249 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:16765898" FT BINDING 251 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:16765898" FT BINDING 269 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:16765898" FT BINDING 270 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:16765898" FT SITE 149..150 FT /note="Cleavage" FT LIPID 17 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:22615937" FT LIPID 18 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:22615937" FT CARBOHYD 63 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 296 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:37453717" FT DISULFID 160..288 FT DISULFID 163..174 FT DISULFID 191..282 FT DISULFID 259..273 FT VARIANT 62 FT /note="R -> W (in dbSNP:rs2228137)" FT /id="VAR_035387" FT VARIANT 284 FT /note="R -> Q (in dbSNP:rs8102872)" FT /id="VAR_035388" FT VARIANT 316 FT /note="S -> F" FT /evidence="ECO:0000269|PubMed:23424103" FT /id="VAR_069800" FT CONFLICT 269 FT /note="N -> T (in Ref. 3; CAA28465)" FT /evidence="ECO:0000305" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:2H2R" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:1T8C" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:2H2T" FT STRAND 173..182 FT /evidence="ECO:0007829|PDB:2H2T" FT HELIX 184..193 FT /evidence="ECO:0007829|PDB:2H2T" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:4J6N" FT HELIX 204..211 FT /evidence="ECO:0007829|PDB:2H2T" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:1T8C" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:2H2T" FT TURN 227..230 FT /evidence="ECO:0007829|PDB:2H2T" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:2H2T" FT TURN 247..252 FT /evidence="ECO:0007829|PDB:4GK1" FT TURN 253..256 FT /evidence="ECO:0007829|PDB:6Y0M" FT STRAND 259..262 FT /evidence="ECO:0007829|PDB:2H2T" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:5LGK" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:2H2T" FT STRAND 277..285 FT /evidence="ECO:0007829|PDB:2H2T" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:2H2R" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:1T8C" SQ SEQUENCE 321 AA; 36469 MW; F86708C0E6515B87 CRC64; MEEGQYSEIE ELPRRRCCRR GTQIVLLGLV TAALWAGLLT LLLLWHWDTT QSLKQLEERA ARNVSQVSKN LESHHGDQMA QKSQSTQISQ ELEELRAEQQ RLKSQDLELS WNLNGLQADL SSFKSQELNE RNEASDLLER LREEVTKLRM ELQVSSGFVC NTCPEKWINF QRKCYYFGKG TKQWVHARYA CDDMEGQLVS IHSPEEQDFL TKHASHTGSW IGLRNLDLKG EFIWVDGSHV DYSNWAPGEP TSRSQGEDCV MMRGSGRWND AFCDRKLGAW VCDRLATCTP PASEGSAESM GPDSRPDPDG RLPTPSAPLH S //