ID LYAM2_HUMAN Reviewed; 610 AA. AC P16581; A2RRD6; P16111; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 27-MAR-2024, entry version 243. DE RecName: Full=E-selectin; DE AltName: Full=CD62 antigen-like family member E; DE AltName: Full=Endothelial leukocyte adhesion molecule 1; DE Short=ELAM-1; DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 2; DE Short=LECAM2; DE AltName: CD_antigen=CD62E; DE Flags: Precursor; GN Name=SELE; Synonyms=ELAM1; 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], FUNCTION, AND INDUCTION. RC TISSUE=Umbilical vein endothelial cell; RX PubMed=1689848; DOI=10.1073/pnas.87.5.1673; RA Hession C., Osborn L., Goff D., Chi-Rosso G., Vassallo C., Pasek M., RA Pittack C., Tizard R., Goelz S., McCarthy K., Hopple S., Lobb R.; RT "Endothelial leukocyte adhesion molecule 1: direct expression cloning and RT functional interactions."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1673-1677(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2466335; DOI=10.1126/science.2466335; RA Bevilacqua M.P., Stengelin S., Gimbrone M.A. Jr., Seed B.; RT "Endothelial leukocyte adhesion molecule 1: an inducible receptor for RT neutrophils related to complement regulatory proteins and lectins."; RL Science 243:1160-1165(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1703529; DOI=10.1016/s0021-9258(18)52267-5; RA Collins T., Williams A., Johnston G.I., Kim J., Eddy R., Shows T., RA Gimbrone M.A. Jr., Bevilacqua M.P.; RT "Structure and chromosomal location of the gene for endothelial-leukocyte RT adhesion molecule 1."; RL J. Biol. Chem. 266:2466-2473(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-21; ILE-31; ARG-149; RP PRO-257; LYS-295; GLN-421; TYR-468; SER-550 AND PHE-575. RG SeattleSNPs variation discovery resource; RL Submitted (AUG-2002) 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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [8] RP LIGAND. RX PubMed=1701274; DOI=10.1126/science.1701274; RA Phillips M.L., Nudelman E., Gaeta F.C., Perez M., Singhal A.K., RA Hakomori S., Paulson J.C.; RT "ELAM-1 mediates cell adhesion by recognition of a carbohydrate ligand, RT sialyl-Lex."; RL Science 250:1130-1132(1990). RN [9] RP INTERACTION WITH PODXL2. RX PubMed=18606703; DOI=10.4049/jimmunol.181.2.1480; RA Kerr S.C., Fieger C.B., Snapp K.R., Rosen S.D.; RT "Endoglycan, a member of the CD34 family of sialomucins, is a ligand for RT the vascular selectins."; RL J. Immunol. 181:1480-1490(2008). RN [10] RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-109, AND FUNCTION. RX PubMed=28011641; DOI=10.1074/jbc.m116.767186; RA Mehta-D'souza P., Klopocki A.G., Oganesyan V., Terzyan S., Mather T., RA Li Z., Panicker S.R., Zhu C., McEver R.P.; RT "Glycan Bound to the Selectin Low Affinity State Engages Glu-88 to RT Stabilize the High Affinity State under Force."; RL J. Biol. Chem. 292:2510-2518(2017). RN [11] RP 3D-STRUCTURE MODELING OF LECTIN DOMAIN. RX PubMed=7681016; DOI=10.1016/0014-5793(93)80026-q; RA Mills A.; RT "Modelling the carbohydrate recognition domain of human E-selectin."; RL FEBS Lett. 319:5-11(1993). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-178. RX PubMed=7509040; DOI=10.1038/367532a0; RA Graves B.J., Crowther R.L., Chandran C., Rumberger J.M., Li S., RA Huang K.-S., Presky D.H., Familletti P.C., Wolitzky B.A., Burns D.K.; RT "Insight into E-selectin/ligand interaction from the crystal structure and RT mutagenesis of the lec/EGF domains."; RL Nature 367:532-538(1994). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 22-178 IN COMPLEX WITH CALCIUM RP IONS AND SELPLG, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=11081633; DOI=10.1016/s0092-8674(00)00138-0; RA Somers W.S., Tang J., Shaw G.D., Camphausen R.T.; RT "Insights into the molecular basis of leukocyte tethering and rolling RT revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1."; RL Cell 103:467-479(2000). RN [14] RP ERRATUM OF PUBMED:11081633. RA Somers W.S., Tang J., Shaw G.D., Camphausen R.T.; RL Cell 105:971-971(2001). RN [15] {ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY} RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 22-301 IN COMPLEX WITH CALCIUM RP AND CARBOHYDRATE, GLYCOSYLATION AT ASN-25; ASN-145; ASN-160; ASN-179; RP ASN-199; ASN-203 AND ASN-265, AND DISULFIDE BONDS. RX PubMed=26117840; DOI=10.1093/jmcb/mjv046; RA Preston R.C., Jakob R.P., Binder F.P., Sager C.P., Ernst B., Maier T.; RT "E-selectin ligand complexes adopt an extended high-affinity RT conformation."; RL J. Mol. Cell Biol. 8:62-72(2016). RN [16] RP VARIANT ARG-149. RX PubMed=7533025; DOI=10.1093/hmg/3.11.1935; RA Wenzel K., Felix S., Kleber F.X., Brachold R., Menke T., Schattke S., RA Schulte K.L., Glaser C., Rohde K., Baumann G., Speer A.; RT "E-selectin polymorphism and atherosclerosis: an association study."; RL Hum. Mol. Genet. 3:1935-1937(1994). RN [17] RP VARIANTS ARG-149 AND PHE-575. RX PubMed=8557254; DOI=10.1007/bf00218826; RA Wenzel K., Ernst M., Rohde K., Baumann G., Speer A.; RT "DNA polymorphisms in adhesion molecule genes -- a new risk factor for RT early atherosclerosis."; RL Hum. Genet. 97:15-20(1996). RN [18] RP VARIANT ARG-149. RX PubMed=9933738; DOI=10.1159/000025366; RA Ye S.Q., Usher D., Virgil D., Zhang L.Q., Yochim S.E., Gupta R.; RT "A PstI polymorphism detects the mutation of serine-128 to arginine in CD RT 62E gene - a risk factor for coronary artery disease."; RL J. Biomed. Sci. 6:18-21(1999). RN [19] RP VARIANTS ARG-149; TYR-468 AND PHE-575. RX PubMed=10391210; DOI=10.1038/10297; RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., RA Cooper R., Lipshutz R., Chakravarti A.; RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood- RT pressure homeostasis."; RL Nat. Genet. 22:239-247(1999). RN [20] RP VARIANT PHE-575. RX PubMed=10982036; DOI=10.1007/s004390000325; RA Sass C., Pallaud C., Zannad F., Visvikis S.; RT "Relationship between E-selectin L/F554 polymorphism and blood pressure in RT the Stanislas cohort."; RL Hum. Genet. 107:58-61(2000). RN [21] RP VARIANT ARG-149, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT RP ARG-149. RX PubMed=12649084; DOI=10.1161/01.atv.0000067427.40133.59; RA Yoshida M., Takano Y., Sasaoka T., Izumi T., Kimura A.; RT "E-selectin polymorphism associated with myocardial infarction causes RT enhanced leukocyte-endothelial interactions under flow conditions."; RL Arterioscler. Thromb. Vasc. Biol. 23:783-788(2003). RN [22] RP CHARACTERIZATION OF VARIANT ARG-149. RX PubMed=24688092; DOI=10.1093/glycob/cwu026; RA Preston R.C., Rabbani S., Binder F.P., Moes S., Magnani J.L., Ernst B.; RT "Implications of the E-selectin S128R mutation for drug discovery."; RL Glycobiology 24:592-601(2014). RN [23] RP VARIANT LEU-545. RX PubMed=25787250; DOI=10.1073/pnas.1503696112; RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W., RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P., RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P., RA Lifton R.P.; RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in RT insulin-producing adenomas."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015). CC -!- FUNCTION: Cell-surface glycoprotein having a role in immunoadhesion. CC Mediates in the adhesion of blood neutrophils in cytokine-activated CC endothelium through interaction with SELPLG/PSGL1. May have a role in CC capillary morphogenesis. {ECO:0000269|PubMed:1689848, CC ECO:0000269|PubMed:28011641}. CC -!- SUBUNIT: Interacts with SELPLG/PSGL1 and PODXL2 through the sialyl CC Lewis X epitope. SELPLG sulfation appears not to be required for this CC interaction. {ECO:0000269|PubMed:11081633, CC ECO:0000269|PubMed:18606703}. CC -!- INTERACTION: CC P16581; P54252: ATXN3; NbExp=3; IntAct=EBI-8007671, EBI-946046; CC P16581; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-8007671, EBI-5235340; CC P16581; O76024: WFS1; NbExp=3; IntAct=EBI-8007671, EBI-720609; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12649084, CC ECO:0000269|PubMed:28011641}; Single-pass type I membrane protein. CC -!- POLYMORPHISM: A polymorphism in position 149 is associated with a CC higher risk of coronary artery disease (CAD). A significantly higher CC mutation frequency (Arg-149) is observed in patients with CC angiographically proven severe atherosclerosis compared with an CC unselected population (Ser-149). {ECO:0000269|PubMed:12649084, CC ECO:0000269|PubMed:7533025}. CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42247/SELE"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/sele/"; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=E-selectin; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_233"; 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; M30640; AAA52377.1; -; mRNA. DR EMBL; M61893; AAA52375.1; -; Genomic_DNA. DR EMBL; M61895; AAA52375.1; JOINED; Genomic_DNA. DR EMBL; M61887; AAA52375.1; JOINED; Genomic_DNA. DR EMBL; M61888; AAA52375.1; JOINED; Genomic_DNA. DR EMBL; M61890; AAA52375.1; JOINED; Genomic_DNA. DR EMBL; M61891; AAA52375.1; JOINED; Genomic_DNA. DR EMBL; M61892; AAA52375.1; JOINED; Genomic_DNA. DR EMBL; M24736; AAA52376.1; -; mRNA. DR EMBL; AF540378; AAN01237.1; -; Genomic_DNA. DR EMBL; AL021940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW90860.1; -; Genomic_DNA. DR EMBL; BC131551; AAI31552.1; -; mRNA. DR EMBL; BC142677; AAI42678.1; -; mRNA. DR EMBL; BC142711; AAI42712.1; -; mRNA. DR CCDS; CCDS1283.1; -. DR PIR; A38615; A35046. DR RefSeq; NP_000441.2; NM_000450.2. DR PDB; 1ESL; X-ray; 2.00 A; A=22-183. DR PDB; 1G1T; X-ray; 1.50 A; A=22-178. DR PDB; 4C16; X-ray; 1.93 A; A/B=22-301. DR PDB; 4CSY; X-ray; 2.41 A; A/B=22-301. DR PDB; 6EYI; X-ray; 2.04 A; A=22-301. DR PDB; 6EYJ; X-ray; 2.20 A; A/B=22-301. DR PDB; 6EYK; X-ray; 2.21 A; A=22-301. DR PDBsum; 1ESL; -. DR PDBsum; 1G1T; -. DR PDBsum; 4C16; -. DR PDBsum; 4CSY; -. DR PDBsum; 6EYI; -. DR PDBsum; 6EYJ; -. DR PDBsum; 6EYK; -. DR AlphaFoldDB; P16581; -. DR SMR; P16581; -. DR BioGRID; 112301; 17. DR DIP; DIP-58639N; -. DR IntAct; P16581; 14. DR MINT; P16581; -. DR STRING; 9606.ENSP00000331736; -. DR BindingDB; P16581; -. DR ChEMBL; CHEMBL3890; -. DR DrugBank; DB01136; Carvedilol. DR DrugBank; DB06423; Endostatin. DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid. DR GuidetoPHARMACOLOGY; 3200; -. DR UniLectin; P16581; -. DR GlyCosmos; P16581; 11 sites, No reported glycans. DR GlyGen; P16581; 11 sites. DR iPTMnet; P16581; -. DR PhosphoSitePlus; P16581; -. DR BioMuta; SELE; -. DR DMDM; 126180; -. DR jPOST; P16581; -. DR MassIVE; P16581; -. DR PaxDb; 9606-ENSP00000331736; -. DR PeptideAtlas; P16581; -. DR ProteomicsDB; 53381; -. DR ABCD; P16581; 13 sequenced antibodies. DR Antibodypedia; 3682; 1343 antibodies from 43 providers. DR DNASU; 6401; -. DR Ensembl; ENST00000333360.12; ENSP00000331736.7; ENSG00000007908.16. DR GeneID; 6401; -. DR KEGG; hsa:6401; -. DR MANE-Select; ENST00000333360.12; ENSP00000331736.7; NM_000450.2; NP_000441.2. DR UCSC; uc001ggm.5; human. DR AGR; HGNC:10718; -. DR CTD; 6401; -. DR DisGeNET; 6401; -. DR GeneCards; SELE; -. DR HGNC; HGNC:10718; SELE. DR HPA; ENSG00000007908; Tissue enhanced (urinary). DR MIM; 131210; gene. DR neXtProt; NX_P16581; -. DR OpenTargets; ENSG00000007908; -. DR PharmGKB; PA35640; -. DR VEuPathDB; HostDB:ENSG00000007908; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00940000160168; -. DR InParanoid; P16581; -. DR OMA; FVTCDHA; -. DR OrthoDB; 3035244at2759; -. DR PhylomeDB; P16581; -. DR TreeFam; TF326910; -. DR PathwayCommons; P16581; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR SignaLink; P16581; -. DR SIGNOR; P16581; -. DR BioGRID-ORCS; 6401; 11 hits in 1152 CRISPR screens. DR ChiTaRS; SELE; human. DR EvolutionaryTrace; P16581; -. DR GeneWiki; E-selectin; -. DR GenomeRNAi; 6401; -. DR Pharos; P16581; Tchem. DR PRO; PR:P16581; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P16581; Protein. DR Bgee; ENSG00000007908; Expressed in vena cava and 146 other cell types or tissues. DR ExpressionAtlas; P16581; baseline and differential. DR GO; GO:0005901; C:caveola; IDA:BHF-UCL. DR GO; GO:0005905; C:clathrin-coated pit; IDA:BHF-UCL. DR GO; GO:0030863; C:cortical cytoskeleton; IDA:BHF-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070492; F:oligosaccharide binding; IDA:BHF-UCL. DR GO; GO:0043274; F:phospholipase binding; IDA:BHF-UCL. DR GO; GO:0033691; F:sialic acid binding; IDA:BHF-UCL. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:BHF-UCL. DR GO; GO:0030029; P:actin filament-based process; IDA:BHF-UCL. DR GO; GO:0007202; P:activation of phospholipase C activity; IMP:BHF-UCL. DR GO; GO:0019722; P:calcium-mediated signaling; TAS:BHF-UCL. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:BHF-UCL. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL. DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; TAS:BHF-UCL. DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:BHF-UCL. DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl. DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB. DR GO; GO:0002092; P:positive regulation of receptor internalization; IDA:BHF-UCL. DR GO; GO:0050727; P:regulation of inflammatory response; TAS:BHF-UCL. DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central. DR GO; GO:0070555; P:response to interleukin-1; IDA:BHF-UCL. DR GO; GO:0032496; P:response to lipopolysaccharide; TAS:BHF-UCL. DR GO; GO:0034612; P:response to tumor necrosis factor; TAS:BHF-UCL. DR CDD; cd00033; CCP; 6. DR CDD; cd03592; CLECT_selectins_like; 1. DR CDD; cd00054; EGF_CA; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 6. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1. DR IDEAL; IID00351; -. 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; IPR016187; CTDL_fold. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR033991; Selectin_CTLD. DR InterPro; IPR002396; Selectin_superfamily. DR InterPro; IPR035976; Sushi/SCR/CCP_sf. DR InterPro; IPR000436; Sushi_SCR_CCP_dom. DR PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1. DR PANTHER; PTHR19325:SF493; E-SELECTIN; 1. DR Pfam; PF00008; EGF; 1. DR Pfam; PF00059; Lectin_C; 1. DR Pfam; PF00084; Sushi; 6. DR PRINTS; PR00343; SELECTIN. DR SMART; SM00032; CCP; 6. DR SMART; SM00034; CLECT; 1. DR SMART; SM00181; EGF; 2. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR SUPFAM; SSF57535; Complement control module/SCR domain; 6. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50923; SUSHI; 6. DR Genevisible; P16581; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Disulfide bond; KW EGF-like domain; Glycoprotein; Lectin; Membrane; Metal-binding; KW Reference proteome; Repeat; Signal; Sushi; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..21 FT CHAIN 22..610 FT /note="E-selectin" FT /id="PRO_0000017492" FT TOPO_DOM 22..556 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 557..578 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 579..610 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 22..139 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 140..175 FT /note="EGF-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 178..239 FT /note="Sushi 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 240..301 FT /note="Sushi 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 303..364 FT /note="Sushi 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 366..427 FT /note="Sushi 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 429..490 FT /note="Sushi 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 491..549 FT /note="Sushi 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT BINDING 101..109 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT BINDING 101 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:1ESL, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT BINDING 103 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, FT ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT BINDING 109 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT BINDING 113..118 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT BINDING 126..128 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT BINDING 126 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, FT ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT BINDING 127 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, FT ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT CARBOHYD 145 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT CARBOHYD 160 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT CARBOHYD 179 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT CARBOHYD 199 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT CARBOHYD 203 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT CARBOHYD 265 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT CARBOHYD 312 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 332 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 503 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 527 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 40..138 FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, FT ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT DISULFID 111..130 FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, FT ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT DISULFID 143..154 FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, FT ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT DISULFID 148..163 FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, FT ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT DISULFID 165..174 FT /evidence="ECO:0000269|PubMed:11081633, FT ECO:0000269|PubMed:26117840, ECO:0007744|PDB:1ESL, FT ECO:0007744|PDB:1G1T, ECO:0007744|PDB:4C16, FT ECO:0007744|PDB:4CSY" FT DISULFID 180..224 FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT DISULFID 193..206 FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT DISULFID 210..237 FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT DISULFID 242..286 FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT DISULFID 255..268 FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT DISULFID 272..299 FT /evidence="ECO:0000269|PubMed:26117840, FT ECO:0007744|PDB:4C16, ECO:0007744|PDB:4CSY" FT DISULFID 304..349 FT /evidence="ECO:0000250" FT DISULFID 335..362 FT /evidence="ECO:0000250" FT DISULFID 367..412 FT /evidence="ECO:0000250" FT DISULFID 398..425 FT /evidence="ECO:0000250" FT DISULFID 430..475 FT /evidence="ECO:0000250" FT DISULFID 461..488 FT /evidence="ECO:0000250" FT DISULFID 493..534 FT /evidence="ECO:0000250" FT DISULFID 520..547 FT /evidence="ECO:0000250" FT VARIANT 21 FT /note="A -> S (in dbSNP:rs3917407)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_014300" FT VARIANT 31 FT /note="M -> I (in dbSNP:rs3917408)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_014301" FT VARIANT 130 FT /note="C -> W (in dbSNP:rs5360)" FT /id="VAR_011790" FT VARIANT 149 FT /note="S -> R (probable risk factor for coronary artery FT disease; no effect on ligand-specificity; may increase FT levels of rolling and adhesion of neutrophils and FT peripheral blood mononuclear cells to the endothelium; may FT induce constitutive stimulation of the MAPK signaling FT pathway, in the absence of leukocyte adhesion; FT dbSNP:rs5361)" FT /evidence="ECO:0000269|PubMed:10391210, FT ECO:0000269|PubMed:12649084, ECO:0000269|PubMed:24688092, FT ECO:0000269|PubMed:7533025, ECO:0000269|PubMed:8557254, FT ECO:0000269|PubMed:9933738, ECO:0000269|Ref.4" FT /id="VAR_004191" FT VARIANT 257 FT /note="Q -> P (in dbSNP:rs3917422)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_014302" FT VARIANT 295 FT /note="E -> K (in dbSNP:rs5364)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_011791" FT VARIANT 421 FT /note="E -> Q (in dbSNP:rs5366)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_011792" FT VARIANT 468 FT /note="H -> Y (in dbSNP:rs5368)" FT /evidence="ECO:0000269|PubMed:10391210, ECO:0000269|Ref.4" FT /id="VAR_011793" FT VARIANT 545 FT /note="P -> L" FT /evidence="ECO:0000269|PubMed:25787250" FT /id="VAR_074189" FT VARIANT 550 FT /note="P -> S (in dbSNP:rs3917429)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_014303" FT VARIANT 575 FT /note="L -> F (in dbSNP:rs5355)" FT /evidence="ECO:0000269|PubMed:10391210, FT ECO:0000269|PubMed:10982036, ECO:0000269|PubMed:8557254, FT ECO:0000269|Ref.4" FT /id="VAR_011794" FT MUTAGEN 109 FT /note="E->D: Decreased adhesion to cells expressing FT SELPLG." FT /evidence="ECO:0000269|PubMed:28011641" FT STRAND 23..26 FT /evidence="ECO:0007829|PDB:1G1T" FT HELIX 33..43 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:1G1T" FT HELIX 53..62 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 70..77 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:1G1T" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:1G1T" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:1G1T" FT HELIX 147..150 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 151..157 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:1G1T" FT STRAND 189..194 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:6EYJ" FT STRAND 267..272 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 277..280 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:4C16" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:4C16" SQ SEQUENCE 610 AA; 66655 MW; 7D43E3C0D1229229 CRC64; MIASQFLSAL TLVLLIKESG AWSYNTSTEA MTYDEASAYC QQRYTHLVAI QNKEEIEYLN SILSYSPSYY WIGIRKVNNV WVWVGTQKPL TEEAKNWAPG EPNNRQKDED CVEIYIKREK DVGMWNDERC SKKKLALCYT AACTNTSCSG HGECVETINN YTCKCDPGFS GLKCEQIVNC TALESPEHGS LVCSHPLGNF SYNSSCSISC DRGYLPSSME TMQCMSSGEW SAPIPACNVV ECDAVTNPAN GFVECFQNPG SFPWNTTCTF DCEEGFELMG AQSLQCTSSG NWDNEKPTCK AVTCRAVRQP QNGSVRCSHS PAGEFTFKSS CNFTCEEGFM LQGPAQVECT TQGQWTQQIP VCEAFQCTAL SNPERGYMNC LPSASGSFRY GSSCEFSCEQ GFVLKGSKRL QCGPTGEWDN EKPTCEAVRC DAVHQPPKGL VRCAHSPIGE FTYKSSCAFS CEEGFELHGS TQLECTSQGQ WTEEVPSCQV VKCSSLAVPG KINMSCSGEP VFGTVCKFAC PEGWTLNGSA ARTCGATGHW SGLLPTCEAP TESNIPLVAG LSAAGLSLLT LAPFLLWLRK CLRKAKKFVP ASSCQSLESD GSYQKPSYIL //