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E-selectin (CD62 antigen-like family member E) (Endothelial leukocyte adhesion molecule 1) (ELAM-1) (Leukocyte-endothelial cell adhesion molecule 2) (LECAM2) (CD antigen CD62E)

 LYAM2_HUMAN             Reviewed;         610 AA.
P16581; A2RRD6; P16111;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
18-JUL-2018, entry version 211.
RecName: Full=E-selectin;
AltName: Full=CD62 antigen-like family member E;
AltName: Full=Endothelial leukocyte adhesion molecule 1;
Short=ELAM-1;
AltName: Full=Leukocyte-endothelial cell adhesion molecule 2;
Short=LECAM2;
AltName: CD_antigen=CD62E;
Flags: Precursor;
Name=SELE; Synonyms=ELAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
TISSUE=Umbilical vein endothelial cell;
PubMed=1689848; DOI=10.1073/pnas.87.5.1673;
Hession C., Osborn L., Goff D., Chi-Rosso G., Vassallo C., Pasek M.,
Pittack C., Tizard R., Goelz S., McCarthy K., Hopple S., Lobb R.;
"Endothelial leukocyte adhesion molecule 1: direct expression cloning
and functional interactions.";
Proc. Natl. Acad. Sci. U.S.A. 87:1673-1677(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2466335; DOI=10.1126/science.2466335;
Bevilacqua M.P., Stengelin S., Gimbrone M.A. Jr., Seed B.;
"Endothelial leukocyte adhesion molecule 1: an inducible receptor for
neutrophils related to complement regulatory proteins and lectins.";
Science 243:1160-1165(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1703529;
Collins T., Williams A., Johnston G.I., Kim J., Eddy R., Shows T.,
Gimbrone M.A. Jr., Bevilacqua M.P.;
"Structure and chromosomal location of the gene for endothelial-
leukocyte adhesion molecule 1.";
J. Biol. Chem. 266:2466-2473(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-21; ILE-31;
ARG-149; PRO-257; LYS-295; GLN-421; TYR-468; SER-550 AND PHE-575.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
LIGAND.
PubMed=1701274; DOI=10.1126/science.1701274;
Phillips M.L., Nudelman E., Gaeta F.C., Perez M., Singhal A.K.,
Hakomori S., Paulson J.C.;
"ELAM-1 mediates cell adhesion by recognition of a carbohydrate
ligand, sialyl-Lex.";
Science 250:1130-1132(1990).
[9]
INTERACTION WITH PODXL2.
PubMed=18606703; DOI=10.4049/jimmunol.181.2.1480;
Kerr S.C., Fieger C.B., Snapp K.R., Rosen S.D.;
"Endoglycan, a member of the CD34 family of sialomucins, is a ligand
for the vascular selectins.";
J. Immunol. 181:1480-1490(2008).
[10]
SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-109, AND FUNCTION.
PubMed=28011641; DOI=10.1074/jbc.M116.767186;
Mehta-D'souza P., Klopocki A.G., Oganesyan V., Terzyan S., Mather T.,
Li Z., Panicker S.R., Zhu C., McEver R.P.;
"Glycan Bound to the Selectin Low Affinity State Engages Glu-88 to
Stabilize the High Affinity State under Force.";
J. Biol. Chem. 292:2510-2518(2017).
[11]
3D-STRUCTURE MODELING OF LECTIN DOMAIN.
PubMed=7681016; DOI=10.1016/0014-5793(93)80026-Q;
Mills A.;
"Modelling the carbohydrate recognition domain of human E-selectin.";
FEBS Lett. 319:5-11(1993).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-178.
PubMed=7509040; DOI=10.1038/367532a0;
Graves B.J., Crowther R.L., Chandran C., Rumberger J.M., Li S.,
Huang K.-S., Presky D.H., Familletti P.C., Wolitzky B.A., Burns D.K.;
"Insight into E-selectin/ligand interaction from the crystal structure
and mutagenesis of the lec/EGF domains.";
Nature 367:532-538(1994).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 22-178 IN COMPLEX WITH
CALCIUM IONS AND SELPLG, SUBUNIT, AND DISULFIDE BONDS.
PubMed=11081633; DOI=10.1016/S0092-8674(00)00138-0;
Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
"Insights into the molecular basis of leukocyte tethering and rolling
revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-
1.";
Cell 103:467-479(2000).
[14]
ERRATUM.
Somers W.S., Tang J., Shaw G.D., Camphausen R.T.;
Cell 105:971-971(2001).
[15] {ECO:0000244|PDB:4C16, ECO:0000244|PDB:4CSY}
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 22-301 IN COMPLEX WITH
CALCIUM AND CARBOHYDRATE, GLYCOSYLATION AT ASN-25; ASN-145; ASN-160;
ASN-179; ASN-199; ASN-203 AND ASN-265, AND DISULFIDE BONDS.
PubMed=26117840; DOI=10.1093/JMCB/MJV046;
Preston R.C., Jakob R.P., Binder F.P., Sager C.P., Ernst B., Maier T.;
"E-selectin ligand complexes adopt an extended high-affinity
conformation.";
J. Mol. Cell Biol. 8:62-72(2016).
[16]
VARIANT ARG-149.
PubMed=7533025; DOI=10.1093/hmg/3.11.1935;
Wenzel K., Felix S., Kleber F.X., Brachold R., Menke T., Schattke S.,
Schulte K.L., Glaser C., Rohde K., Baumann G., Speer A.;
"E-selectin polymorphism and atherosclerosis: an association study.";
Hum. Mol. Genet. 3:1935-1937(1994).
[17]
VARIANTS ARG-149 AND PHE-575.
PubMed=8557254; DOI=10.1007/BF00218826;
Wenzel K., Ernst M., Rohde K., Baumann G., Speer A.;
"DNA polymorphisms in adhesion molecule genes -- a new risk factor for
early atherosclerosis.";
Hum. Genet. 97:15-20(1996).
[18]
VARIANT ARG-149.
PubMed=9933738; DOI=10.1007/BF02256419;
Ye S.Q., Usher D., Virgil D., Zhang L.Q., Yochim S.E., Gupta R.;
"A PstI polymorphism detects the mutation of serine-128 to arginine in
CD 62E gene - a risk factor for coronary artery disease.";
J. Biomed. Sci. 6:18-21(1999).
[19]
VARIANTS ARG-149; TYR-468 AND PHE-575.
PubMed=10391210; DOI=10.1038/10297;
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
Cooper R., Lipshutz R., Chakravarti A.;
"Patterns of single-nucleotide polymorphisms in candidate genes for
blood-pressure homeostasis.";
Nat. Genet. 22:239-247(1999).
[20]
VARIANT PHE-575.
PubMed=10982036; DOI=10.1007/s004390000325;
Sass C., Pallaud C., Zannad F., Visvikis S.;
"Relationship between E-selectin L/F554 polymorphism and blood
pressure in the Stanislas cohort.";
Hum. Genet. 107:58-61(2000).
[21]
VARIANT ARG-149, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT
ARG-149.
PubMed=12649084; DOI=10.1161/01.ATV.0000067427.40133.59;
Yoshida M., Takano Y., Sasaoka T., Izumi T., Kimura A.;
"E-selectin polymorphism associated with myocardial infarction causes
enhanced leukocyte-endothelial interactions under flow conditions.";
Arterioscler. Thromb. Vasc. Biol. 23:783-788(2003).
[22]
CHARACTERIZATION OF VARIANT ARG-149.
PubMed=24688092; DOI=10.1093/glycob/cwu026;
Preston R.C., Rabbani S., Binder F.P., Moes S., Magnani J.L.,
Ernst B.;
"Implications of the E-selectin S128R mutation for drug discovery.";
Glycobiology 24:592-601(2014).
[23]
VARIANT LEU-545.
PubMed=25787250; DOI=10.1073/pnas.1503696112;
Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D.,
Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T.,
Bjoerklund P., Lifton R.P.;
"Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
insulin-producing adenomas.";
Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
-!- FUNCTION: Cell-surface glycoprotein having a role in
immunoadhesion. Mediates in the adhesion of blood neutrophils in
cytokine-activated endothelium through interaction with
SELPLG/PSGL1. May have a role in capillary morphogenesis.
{ECO:0000269|PubMed:1689848, ECO:0000269|PubMed:28011641}.
-!- SUBUNIT: Interacts with SELPLG/PSGL1 and PODXL2 through the sialyl
Lewis X epitope. SELPLG sulfation appears not to be required for
this interaction. {ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:18606703}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12649084,
ECO:0000269|PubMed:28011641}; Single-pass type I membrane protein.
-!- POLYMORPHISM: A polymorphism in position 149 is associated with a
higher risk of coronary artery disease (CAD). A significantly
higher mutation frequency (Arg-149) is observed in patients with
angiographically proven severe atherosclerosis compared with an
unselected population (Ser-149). {ECO:0000269|PubMed:12649084,
ECO:0000269|PubMed:7533025}.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SELEID42247ch1q22.html";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/sele/";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=E-selectin;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_233";
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EMBL; M30640; AAA52377.1; -; mRNA.
EMBL; M61893; AAA52375.1; -; Genomic_DNA.
EMBL; M61895; AAA52375.1; JOINED; Genomic_DNA.
EMBL; M61887; AAA52375.1; JOINED; Genomic_DNA.
EMBL; M61888; AAA52375.1; JOINED; Genomic_DNA.
EMBL; M61890; AAA52375.1; JOINED; Genomic_DNA.
EMBL; M61891; AAA52375.1; JOINED; Genomic_DNA.
EMBL; M61892; AAA52375.1; JOINED; Genomic_DNA.
EMBL; M24736; AAA52376.1; -; mRNA.
EMBL; AF540378; AAN01237.1; -; Genomic_DNA.
EMBL; AL021940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW90860.1; -; Genomic_DNA.
EMBL; BC131551; AAI31552.1; -; mRNA.
EMBL; BC142677; AAI42678.1; -; mRNA.
EMBL; BC142711; AAI42712.1; -; mRNA.
CCDS; CCDS1283.1; -.
PIR; A38615; A35046.
RefSeq; NP_000441.2; NM_000450.2.
UniGene; Hs.82848; -.
PDB; 1ESL; X-ray; 2.00 A; A=22-183.
PDB; 1G1T; X-ray; 1.50 A; A=22-178.
PDB; 1KJA; Model; -; A=22-141.
PDB; 4C16; X-ray; 1.93 A; A/B=22-301.
PDB; 4CSY; X-ray; 2.41 A; A/B=22-301.
PDBsum; 1ESL; -.
PDBsum; 1G1T; -.
PDBsum; 1KJA; -.
PDBsum; 4C16; -.
PDBsum; 4CSY; -.
ProteinModelPortal; P16581; -.
SMR; P16581; -.
BioGrid; 112301; 16.
DIP; DIP-58639N; -.
IntAct; P16581; 5.
MINT; P16581; -.
STRING; 9606.ENSP00000331736; -.
BindingDB; P16581; -.
ChEMBL; CHEMBL3890; -.
DrugBank; DB01136; Carvedilol.
DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
UniLectin; P16581; -.
iPTMnet; P16581; -.
PhosphoSitePlus; P16581; -.
BioMuta; SELE; -.
DMDM; 126180; -.
PaxDb; P16581; -.
PeptideAtlas; P16581; -.
PRIDE; P16581; -.
ProteomicsDB; 53381; -.
Ensembl; ENST00000333360; ENSP00000331736; ENSG00000007908.
GeneID; 6401; -.
KEGG; hsa:6401; -.
UCSC; uc001ggm.5; human.
CTD; 6401; -.
DisGeNET; 6401; -.
EuPathDB; HostDB:ENSG00000007908.15; -.
GeneCards; SELE; -.
HGNC; HGNC:10718; SELE.
HPA; CAB002143; -.
MalaCards; SELE; -.
MIM; 131210; gene.
neXtProt; NX_P16581; -.
OpenTargets; ENSG00000007908; -.
Orphanet; 34145; Berger disease.
PharmGKB; PA35640; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00910000143999; -.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; P16581; -.
KO; K06494; -.
OMA; QGQWTQQ; -.
OrthoDB; EOG091G04KC; -.
PhylomeDB; P16581; -.
TreeFam; TF326910; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
SIGNOR; P16581; -.
ChiTaRS; SELE; human.
EvolutionaryTrace; P16581; -.
GeneWiki; E-selectin; -.
GenomeRNAi; 6401; -.
PRO; PR:P16581; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000007908; -.
ExpressionAtlas; P16581; baseline and differential.
Genevisible; P16581; HS.
GO; GO:0005901; C:caveola; IDA:BHF-UCL.
GO; GO:0005905; C:clathrin-coated pit; IDA:BHF-UCL.
GO; GO:0030863; C:cortical cytoskeleton; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070492; F:oligosaccharide binding; IDA:BHF-UCL.
GO; GO:0043274; F:phospholipase binding; IDA:BHF-UCL.
GO; GO:0033691; F:sialic acid binding; IDA:BHF-UCL.
GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:BHF-UCL.
GO; GO:0030029; P:actin filament-based process; IDA:BHF-UCL.
GO; GO:0007202; P:activation of phospholipase C activity; IMP:BHF-UCL.
GO; GO:0019722; P:calcium-mediated signaling; TAS:BHF-UCL.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:BHF-UCL.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; TAS:BHF-UCL.
GO; GO:0050901; P:leukocyte tethering or rolling; IMP:BHF-UCL.
GO; GO:0002092; P:positive regulation of receptor internalization; IDA:BHF-UCL.
GO; GO:0050727; P:regulation of inflammatory response; TAS:BHF-UCL.
GO; GO:0070555; P:response to interleukin-1; IDA:BHF-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; TAS:BHF-UCL.
GO; GO:0034612; P:response to tumor necrosis factor; TAS:BHF-UCL.
CDD; cd00033; CCP; 6.
CDD; cd03592; CLECT_selectins_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR033991; Selectin_CTLD.
InterPro; IPR002396; Selectin_superfamily.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00008; EGF; 1.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 6.
PRINTS; PR00343; SELECTIN.
SMART; SM00032; CCP; 6.
SMART; SM00034; CLECT; 1.
SMART; SM00181; EGF; 2.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57535; SSF57535; 6.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50923; SUSHI; 6.
1: Evidence at protein level;
3D-structure; Calcium; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
Lectin; Membrane; Metal-binding; Polymorphism; Reference proteome;
Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
SIGNAL 1 21
CHAIN 22 610 E-selectin.
/FTId=PRO_0000017492.
TOPO_DOM 22 556 Extracellular. {ECO:0000255}.
TRANSMEM 557 578 Helical. {ECO:0000255}.
TOPO_DOM 579 610 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 139 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 140 175 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 178 239 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 240 301 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 303 364 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 366 427 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 429 490 Sushi 5. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 491 549 Sushi 6. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 101 109 Carbohydrate binding.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
REGION 113 118 Carbohydrate binding.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
REGION 126 128 Carbohydrate binding.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
METAL 101 101 Calcium. {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
METAL 103 103 Calcium. {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:1G1T,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
METAL 109 109 Calcium. {ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
METAL 126 126 Calcium. {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:1G1T,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
METAL 127 127 Calcium. {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:1G1T,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 503 503 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 527 527 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 40 138 {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:1G1T,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
DISULFID 111 130 {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:1G1T,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
DISULFID 143 154 {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:1G1T,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
DISULFID 148 163 {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:1G1T,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
DISULFID 165 174 {ECO:0000244|PDB:1ESL,
ECO:0000244|PDB:1G1T,
ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:11081633,
ECO:0000269|PubMed:26117840}.
DISULFID 180 224 {ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
DISULFID 193 206 {ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
DISULFID 210 237 {ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
DISULFID 242 286 {ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
DISULFID 255 268 {ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
DISULFID 272 299 {ECO:0000244|PDB:4C16,
ECO:0000244|PDB:4CSY,
ECO:0000269|PubMed:26117840}.
DISULFID 304 349 {ECO:0000250}.
DISULFID 335 362 {ECO:0000250}.
DISULFID 367 412 {ECO:0000250}.
DISULFID 398 425 {ECO:0000250}.
DISULFID 430 475 {ECO:0000250}.
DISULFID 461 488 {ECO:0000250}.
DISULFID 493 534 {ECO:0000250}.
DISULFID 520 547 {ECO:0000250}.
VARIANT 21 21 A -> S (in dbSNP:rs3917407).
{ECO:0000269|Ref.4}.
/FTId=VAR_014300.
VARIANT 31 31 M -> I (in dbSNP:rs3917408).
{ECO:0000269|Ref.4}.
/FTId=VAR_014301.
VARIANT 130 130 C -> W (in dbSNP:rs5360).
/FTId=VAR_011790.
VARIANT 149 149 S -> R (polymorphism associated with
coronary artery disease; no effect on
ligand-specificity; may increase levels
of rolling and adhesion of neutrophils
and peripheral blood mononuclear cells to
the endothelium; may induce constitutive
stimulation of the MAPK signaling
pathway, in the absence of leukocyte
adhesion; dbSNP:rs5361).
{ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:12649084,
ECO:0000269|PubMed:24688092,
ECO:0000269|PubMed:7533025,
ECO:0000269|PubMed:8557254,
ECO:0000269|PubMed:9933738,
ECO:0000269|Ref.4}.
/FTId=VAR_004191.
VARIANT 257 257 Q -> P (in dbSNP:rs3917422).
{ECO:0000269|Ref.4}.
/FTId=VAR_014302.
VARIANT 295 295 E -> K (in dbSNP:rs5364).
{ECO:0000269|Ref.4}.
/FTId=VAR_011791.
VARIANT 421 421 E -> Q (in dbSNP:rs5366).
{ECO:0000269|Ref.4}.
/FTId=VAR_011792.
VARIANT 468 468 H -> Y (in dbSNP:rs5368).
{ECO:0000269|PubMed:10391210,
ECO:0000269|Ref.4}.
/FTId=VAR_011793.
VARIANT 545 545 P -> L. {ECO:0000269|PubMed:25787250}.
/FTId=VAR_074189.
VARIANT 550 550 P -> S (in dbSNP:rs3917429).
{ECO:0000269|Ref.4}.
/FTId=VAR_014303.
VARIANT 575 575 L -> F (in dbSNP:rs5355).
{ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:10982036,
ECO:0000269|PubMed:8557254,
ECO:0000269|Ref.4}.
/FTId=VAR_011794.
MUTAGEN 109 109 E->D: Decreased adhesion to cells
expressing SELPLG.
{ECO:0000269|PubMed:28011641}.
STRAND 23 26 {ECO:0000244|PDB:1G1T}.
HELIX 33 43 {ECO:0000244|PDB:1G1T}.
STRAND 44 47 {ECO:0000244|PDB:1G1T}.
HELIX 53 62 {ECO:0000244|PDB:1G1T}.
STRAND 70 77 {ECO:0000244|PDB:1G1T}.
STRAND 80 83 {ECO:0000244|PDB:1G1T}.
TURN 84 86 {ECO:0000244|PDB:1G1T}.
TURN 92 94 {ECO:0000244|PDB:1G1T}.
STRAND 111 114 {ECO:0000244|PDB:1G1T}.
STRAND 119 121 {ECO:0000244|PDB:1G1T}.
STRAND 125 128 {ECO:0000244|PDB:1G1T}.
STRAND 134 140 {ECO:0000244|PDB:1G1T}.
HELIX 147 150 {ECO:0000244|PDB:1G1T}.
STRAND 151 157 {ECO:0000244|PDB:1G1T}.
STRAND 160 165 {ECO:0000244|PDB:1G1T}.
STRAND 169 171 {ECO:0000244|PDB:1G1T}.
STRAND 189 194 {ECO:0000244|PDB:4C16}.
STRAND 196 198 {ECO:0000244|PDB:4C16}.
STRAND 205 210 {ECO:0000244|PDB:4C16}.
STRAND 214 217 {ECO:0000244|PDB:4C16}.
STRAND 222 224 {ECO:0000244|PDB:4C16}.
STRAND 230 232 {ECO:0000244|PDB:4C16}.
STRAND 237 239 {ECO:0000244|PDB:4C16}.
STRAND 251 254 {ECO:0000244|PDB:4C16}.
STRAND 267 272 {ECO:0000244|PDB:4C16}.
STRAND 277 280 {ECO:0000244|PDB:4C16}.
STRAND 282 286 {ECO:0000244|PDB:4C16}.
STRAND 292 294 {ECO:0000244|PDB:4C16}.
STRAND 298 300 {ECO:0000244|PDB:4C16}.
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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