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Database: UniProt
Entry: P16581
LinkDB: P16581
Original site: P16581 
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   13-FEB-2019, entry version 216.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   and 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;
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-
RT   leukocyte adhesion molecule 1.";
RL   J. Biol. Chem. 266:2466-2473(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-21; ILE-31;
RP   ARG-149; 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   ligand, 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
RT   for 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
RT   and 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
RP   CALCIUM 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-
RT   1.";
RL   Cell 103:467-479(2000).
RN   [14]
RP   ERRATUM.
RA   Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
RL   Cell 105:971-971(2001).
RN   [15] {ECO:0000244|PDB:4C16, ECO:0000244|PDB:4CSY}
RP   X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 22-301 IN COMPLEX WITH
RP   CALCIUM AND CARBOHYDRATE, GLYCOSYLATION AT ASN-25; ASN-145; ASN-160;
RP   ASN-179; 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=10.1007/BF02256419;
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
RT   CD 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
RT   blood-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
RT   pressure in 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.,
RA   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.,
RA   Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T.,
RA   Bjoerklund P., 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
CC       immunoadhesion. Mediates in the adhesion of blood neutrophils in
CC       cytokine-activated endothelium through interaction with
CC       SELPLG/PSGL1. May have a role in capillary morphogenesis.
CC       {ECO:0000269|PubMed:1689848, 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
CC       this interaction. {ECO:0000269|PubMed:11081633,
CC       ECO:0000269|PubMed:18606703}.
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
CC       higher 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
CC       and 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";
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   UniGene; Hs.82848; -.
DR   PDB; 1ESL; X-ray; 2.00 A; A=22-183.
DR   PDB; 1G1T; X-ray; 1.50 A; A=22-178.
DR   PDB; 1KJA; Model; -; A=22-141.
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; 1KJA; -.
DR   PDBsum; 4C16; -.
DR   PDBsum; 4CSY; -.
DR   PDBsum; 6EYI; -.
DR   PDBsum; 6EYJ; -.
DR   PDBsum; 6EYK; -.
DR   ProteinModelPortal; P16581; -.
DR   SMR; P16581; -.
DR   BioGrid; 112301; 16.
DR   DIP; DIP-58639N; -.
DR   IntAct; P16581; 5.
DR   MINT; P16581; -.
DR   STRING; 9606.ENSP00000331736; -.
DR   BindingDB; P16581; -.
DR   ChEMBL; CHEMBL3890; -.
DR   DrugBank; DB01136; Carvedilol.
DR   DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR   UniLectin; P16581; -.
DR   iPTMnet; P16581; -.
DR   PhosphoSitePlus; P16581; -.
DR   BioMuta; SELE; -.
DR   DMDM; 126180; -.
DR   PaxDb; P16581; -.
DR   PeptideAtlas; P16581; -.
DR   PRIDE; P16581; -.
DR   ProteomicsDB; 53381; -.
DR   Ensembl; ENST00000333360; ENSP00000331736; ENSG00000007908.
DR   GeneID; 6401; -.
DR   KEGG; hsa:6401; -.
DR   UCSC; uc001ggm.5; human.
DR   CTD; 6401; -.
DR   DisGeNET; 6401; -.
DR   EuPathDB; HostDB:ENSG00000007908.15; -.
DR   GeneCards; SELE; -.
DR   HGNC; HGNC:10718; SELE.
DR   HPA; CAB002143; -.
DR   MalaCards; SELE; -.
DR   MIM; 131210; gene.
DR   neXtProt; NX_P16581; -.
DR   OpenTargets; ENSG00000007908; -.
DR   PharmGKB; PA35640; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   eggNOG; ENOG410XPJ1; LUCA.
DR   GeneTree; ENSGT00940000160168; -.
DR   HOGENOM; HOG000236254; -.
DR   HOVERGEN; HBG052375; -.
DR   InParanoid; P16581; -.
DR   KO; K06494; -.
DR   OMA; AQGQWTQ; -.
DR   OrthoDB; 445079at2759; -.
DR   PhylomeDB; P16581; -.
DR   TreeFam; TF326910; -.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   SIGNOR; P16581; -.
DR   ChiTaRS; SELE; human.
DR   EvolutionaryTrace; P16581; -.
DR   GeneWiki; E-selectin; -.
DR   GenomeRNAi; 6401; -.
DR   PRO; PR:P16581; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000007908; Expressed in 150 organ(s), highest expression level in vena cava.
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: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:0050900; P:leukocyte migration; TAS:Reactome.
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: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: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   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; IPR013032; EGF-like_CS.
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;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Lectin; Membrane; Metal-binding; Polymorphism; Reference proteome;
KW   Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21
FT   CHAIN        22    610       E-selectin.
FT                                /FTId=PRO_0000017492.
FT   TOPO_DOM     22    556       Extracellular. {ECO:0000255}.
FT   TRANSMEM    557    578       Helical. {ECO:0000255}.
FT   TOPO_DOM    579    610       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       22    139       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      140    175       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      178    239       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      240    301       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      303    364       Sushi 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      366    427       Sushi 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      429    490       Sushi 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      491    549       Sushi 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION      101    109       Carbohydrate binding.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   REGION      113    118       Carbohydrate binding.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   REGION      126    128       Carbohydrate binding.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   METAL       101    101       Calcium. {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   METAL       103    103       Calcium. {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:1G1T,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   METAL       109    109       Calcium. {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   METAL       126    126       Calcium. {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:1G1T,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   METAL       127    127       Calcium. {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:1G1T,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   CARBOHYD    145    145       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   CARBOHYD    160    160       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   CARBOHYD    179    179       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   CARBOHYD    199    199       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   CARBOHYD    203    203       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   CARBOHYD    265    265       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   CARBOHYD    312    312       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    332    332       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    503    503       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    527    527       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     40    138       {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:1G1T,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    111    130       {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:1G1T,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    143    154       {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:1G1T,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    148    163       {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:1G1T,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    165    174       {ECO:0000244|PDB:1ESL,
FT                                ECO:0000244|PDB:1G1T,
FT                                ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:11081633,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    180    224       {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    193    206       {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    210    237       {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    242    286       {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    255    268       {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    272    299       {ECO:0000244|PDB:4C16,
FT                                ECO:0000244|PDB:4CSY,
FT                                ECO:0000269|PubMed:26117840}.
FT   DISULFID    304    349       {ECO:0000250}.
FT   DISULFID    335    362       {ECO:0000250}.
FT   DISULFID    367    412       {ECO:0000250}.
FT   DISULFID    398    425       {ECO:0000250}.
FT   DISULFID    430    475       {ECO:0000250}.
FT   DISULFID    461    488       {ECO:0000250}.
FT   DISULFID    493    534       {ECO:0000250}.
FT   DISULFID    520    547       {ECO:0000250}.
FT   VARIANT      21     21       A -> S (in dbSNP:rs3917407).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_014300.
FT   VARIANT      31     31       M -> I (in dbSNP:rs3917408).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_014301.
FT   VARIANT     130    130       C -> W (in dbSNP:rs5360).
FT                                /FTId=VAR_011790.
FT   VARIANT     149    149       S -> R (polymorphism associated with
FT                                coronary artery disease; no effect on
FT                                ligand-specificity; may increase levels
FT                                of rolling and adhesion of neutrophils
FT                                and peripheral blood mononuclear cells to
FT                                the endothelium; may induce constitutive
FT                                stimulation of the MAPK signaling
FT                                pathway, in the absence of leukocyte
FT                                adhesion; dbSNP:rs5361).
FT                                {ECO:0000269|PubMed:10391210,
FT                                ECO:0000269|PubMed:12649084,
FT                                ECO:0000269|PubMed:24688092,
FT                                ECO:0000269|PubMed:7533025,
FT                                ECO:0000269|PubMed:8557254,
FT                                ECO:0000269|PubMed:9933738,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_004191.
FT   VARIANT     257    257       Q -> P (in dbSNP:rs3917422).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_014302.
FT   VARIANT     295    295       E -> K (in dbSNP:rs5364).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_011791.
FT   VARIANT     421    421       E -> Q (in dbSNP:rs5366).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_011792.
FT   VARIANT     468    468       H -> Y (in dbSNP:rs5368).
FT                                {ECO:0000269|PubMed:10391210,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_011793.
FT   VARIANT     545    545       P -> L. {ECO:0000269|PubMed:25787250}.
FT                                /FTId=VAR_074189.
FT   VARIANT     550    550       P -> S (in dbSNP:rs3917429).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_014303.
FT   VARIANT     575    575       L -> F (in dbSNP:rs5355).
FT                                {ECO:0000269|PubMed:10391210,
FT                                ECO:0000269|PubMed:10982036,
FT                                ECO:0000269|PubMed:8557254,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_011794.
FT   MUTAGEN     109    109       E->D: Decreased adhesion to cells
FT                                expressing SELPLG.
FT                                {ECO:0000269|PubMed:28011641}.
FT   STRAND       23     26       {ECO:0000244|PDB:1G1T}.
FT   HELIX        33     43       {ECO:0000244|PDB:1G1T}.
FT   STRAND       44     47       {ECO:0000244|PDB:1G1T}.
FT   HELIX        53     62       {ECO:0000244|PDB:1G1T}.
FT   STRAND       70     77       {ECO:0000244|PDB:1G1T}.
FT   STRAND       80     83       {ECO:0000244|PDB:1G1T}.
FT   TURN         84     86       {ECO:0000244|PDB:1G1T}.
FT   TURN         92     94       {ECO:0000244|PDB:1G1T}.
FT   STRAND      111    114       {ECO:0000244|PDB:1G1T}.
FT   STRAND      119    121       {ECO:0000244|PDB:1G1T}.
FT   STRAND      125    128       {ECO:0000244|PDB:1G1T}.
FT   STRAND      134    140       {ECO:0000244|PDB:1G1T}.
FT   HELIX       147    150       {ECO:0000244|PDB:1G1T}.
FT   STRAND      151    157       {ECO:0000244|PDB:1G1T}.
FT   STRAND      160    165       {ECO:0000244|PDB:1G1T}.
FT   STRAND      169    171       {ECO:0000244|PDB:1G1T}.
FT   STRAND      189    194       {ECO:0000244|PDB:4C16}.
FT   STRAND      196    198       {ECO:0000244|PDB:4C16}.
FT   STRAND      205    210       {ECO:0000244|PDB:4C16}.
FT   STRAND      214    217       {ECO:0000244|PDB:4C16}.
FT   STRAND      222    224       {ECO:0000244|PDB:4C16}.
FT   STRAND      230    232       {ECO:0000244|PDB:4C16}.
FT   STRAND      237    239       {ECO:0000244|PDB:4C16}.
FT   STRAND      251    254       {ECO:0000244|PDB:4C16}.
FT   STRAND      256    258       {ECO:0000244|PDB:6EYJ}.
FT   STRAND      267    272       {ECO:0000244|PDB:4C16}.
FT   STRAND      277    280       {ECO:0000244|PDB:4C16}.
FT   STRAND      282    286       {ECO:0000244|PDB:4C16}.
FT   STRAND      292    294       {ECO:0000244|PDB:4C16}.
FT   STRAND      298    300       {ECO:0000244|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
//
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