LYAM2_HUMAN
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 03-AUG-2022, entry version 234.
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="http://atlasgeneticsoncology.org/Genes/SELEID42247ch1q22.html";
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";
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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 UniLectin; P16581; -.
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; P16581; -.
DR PeptideAtlas; P16581; -.
DR PRIDE; P16581; -.
DR ProteomicsDB; 53381; -.
DR ABCD; P16581; 13 sequenced antibodies.
DR Antibodypedia; 3682; 1270 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 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; FTYQSVC; -.
DR OrthoDB; 445079at2759; -.
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; 9 hits in 1074 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 144 other tissues.
DR ExpressionAtlas; P16581; baseline and differential.
DR Genevisible; P16581; HS.
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:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
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; TAS:Reactome.
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: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 Gene3D; 3.10.100.10; -; 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 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; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 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.
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 (associated with coronary artery disease; no
FT effect on ligand-specificity; may increase levels of
FT rolling and adhesion of neutrophils and peripheral blood
FT mononuclear cells to the endothelium; may induce
FT constitutive stimulation of the MAPK signaling pathway, in
FT the absence of leukocyte adhesion; 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
