Reviewed, UniProtKB/Swiss-Prot P16581 (LYAM2_HUMAN)

Names and origin

Protein names

Recommended name:
    E-selectin
Alternative name(s):
    Endothelial leukocyte adhesion molecule 1
      Short name=ELAM-1
    Leukocyte-endothelial cell adhesion molecule 2
      Short name=LECAM2
    CD62 antigen-like family member E
    CD_antigen=CD62E

Gene names

Name:	SELE
Synonyms:	ELAM1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	610 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with PSGL1/SELPLG. May have a role in capillary morphogenesis. Ref.1
Subunit structure	Interacts with PSGL1/SELPLG through the sialyl Lewis X epitope. PSGL1 sulfation appears not to be required for this interaction. Ref.9
Subcellular location	Membrane; 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).
Sequence similarities	Belongs to the selectin/LECAM family. Contains 1 C-type lectin domain. Contains 1 EGF-like domain. Contains 6 Sushi (CCP/SCR) domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal Sushi Transmembrane
Ligand	Lectin
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	actin filament-based process Inferred from direct assay. Source: UniProtKB activation of phospholipase C activity Inferred from mutant phenotype. Source: UniProtKB calcium-mediated signaling Traceable author statement. Source: UniProtKB heterophilic cell adhesion Inferred from mutant phenotype. Source: UniProtKB leukocyte migration during inflammatory response Traceable author statement. Source: UniProtKB leukocyte tethering or rolling Inferred from mutant phenotype. Source: UniProtKB positive regulation of receptor internalization Inferred from direct assay. Source: UniProtKB regulation of inflammatory response Traceable author statement. Source: UniProtKB response to lipopolysaccharide Traceable author statement. Source: UniProtKB response to tumor necrosis factor Traceable author statement. Source: UniProtKB
Cellular component	caveola Inferred from direct assay. Source: UniProtKB coated pit Inferred from direct assay. Source: UniProtKB cortical cytoskeleton Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	oligosaccharide binding Inferred from direct assay. Source: UniProtKB phospholipase binding Inferred from direct assay. Source: UniProtKB sialic acid binding Inferred from direct assay. Source: UniProtKB transmembrane receptor activity Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 610

589

E-selectin

PRO_0000017492

Regions

Topological domain

22 – 556

535

Extracellular Potential

Transmembrane

557 – 578

22

Potential

Topological domain

579 – 610

32

Cytoplasmic Potential

Domain

22 – 139

118

C-type lectin

Domain

140 – 175

36

EGF-like

Domain

178 – 239

62

Sushi 1

Domain

240 – 301

62

Sushi 2

Domain

303 – 364

62

Sushi 3

Domain

366 – 427

62

Sushi 4

Domain

429 – 490

62

Sushi 5

Domain

491 – 549

59

Sushi 6

Amino acid modifications

Glycosylation

25

1

N-linked (GlcNAc...) Potential

Glycosylation

145

1

N-linked (GlcNAc...) Potential

Glycosylation

160

1

N-linked (GlcNAc...) Potential

Glycosylation

179

1

N-linked (GlcNAc...) Potential

Glycosylation

199

1

N-linked (GlcNAc...) Potential

Glycosylation

203

1

N-linked (GlcNAc...) Potential

Glycosylation

265

1

N-linked (GlcNAc...) Potential

Glycosylation

312

1

N-linked (GlcNAc...) Potential

Glycosylation

332

1

N-linked (GlcNAc...) Potential

Glycosylation

503

1

N-linked (GlcNAc...) Potential

Glycosylation

527

1

N-linked (GlcNAc...) Potential

Disulfide bond

40 ↔ 138

Ref.9

Disulfide bond

111 ↔ 130

Ref.9

Disulfide bond

143 ↔ 154

Ref.9

Disulfide bond

148 ↔ 163

Ref.9

Disulfide bond

165 ↔ 174

Ref.9

Disulfide bond

180 ↔ 224

By similarity

Disulfide bond

210 ↔ 237

By similarity

Disulfide bond

242 ↔ 286

By similarity

Disulfide bond

272 ↔ 299

By similarity

Disulfide bond

304 ↔ 349

By similarity

Disulfide bond

335 ↔ 362

By similarity

Disulfide bond

367 ↔ 412

By similarity

Disulfide bond

398 ↔ 425

By similarity

Disulfide bond

430 ↔ 475

By similarity

Disulfide bond

461 ↔ 488

By similarity

Disulfide bond

493 ↔ 534

By similarity

Disulfide bond

520 ↔ 547

By similarity

Natural variations

Natural variant

21

1

A → S: dbSNP rs3917407. Ref.4

VAR_014300

Natural variant

31

1

M → I: dbSNP rs3917408. Ref.4

VAR_014301

Natural variant

130

1

C → W: dbSNP rs5360.

VAR_011790

Natural variant

149

1

S → R Polymorphism associated with coronary artery disease. dbSNP rs5361. Ref.4 Ref.11 Ref.12 Ref.13 Ref.14

VAR_004191

Natural variant

257

1

Q → P: dbSNP rs3917422. Ref.4

VAR_014302

Natural variant

295

1

E → K: dbSNP rs5364. Ref.4

VAR_011791

Natural variant

421

1

E → Q: dbSNP rs5366. Ref.4

VAR_011792

Natural variant

468

1

H → Y: dbSNP rs5368. Ref.4 Ref.14

VAR_011793

Natural variant

550

1

P → S: dbSNP rs3917429. Ref.4

VAR_014303

Natural variant

575

1

L → F: dbSNP rs5355. Ref.4 Ref.12 Ref.14 Ref.15

VAR_011794

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

610

Helix Strand Turn

Details...

Beta strand

23 – 26

4

Helix

33 – 43

11

Beta strand

44 – 47

4

Helix

53 – 62

10

Beta strand

70 – 77

8

Beta strand

80 – 83

4

Turn

84 – 86

3

Turn

92 – 94

3

Beta strand

111 – 114

4

Beta strand

119 – 121

3

Beta strand

125 – 128

4

Beta strand

134 – 140

7

Helix

147 – 150

4

Beta strand

151 – 157

7

Beta strand

160 – 165

6

Beta strand

169 – 171

3

Sequences

	Sequence		Length	Mass (Da)
	P16581-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 7D43E3C0D1229229	FASTA	610	66,655
	10 20 30 40 50 60 MIASQFLSAL TLVLLIKESG AWSYNTSTEA MTYDEASAYC QQRYTHLVAI QNKEEIEYLN 70 80 90 100 110 120 SILSYSPSYY WIGIRKVNNV WVWVGTQKPL TEEAKNWAPG EPNNRQKDED CVEIYIKREK 130 140 150 160 170 180 DVGMWNDERC SKKKLALCYT AACTNTSCSG HGECVETINN YTCKCDPGFS GLKCEQIVNC 190 200 210 220 230 240 TALESPEHGS LVCSHPLGNF SYNSSCSISC DRGYLPSSME TMQCMSSGEW SAPIPACNVV 250 260 270 280 290 300 ECDAVTNPAN GFVECFQNPG SFPWNTTCTF DCEEGFELMG AQSLQCTSSG NWDNEKPTCK 310 320 330 340 350 360 AVTCRAVRQP QNGSVRCSHS PAGEFTFKSS CNFTCEEGFM LQGPAQVECT TQGQWTQQIP 370 380 390 400 410 420 VCEAFQCTAL SNPERGYMNC LPSASGSFRY GSSCEFSCEQ GFVLKGSKRL QCGPTGEWDN 430 440 450 460 470 480 EKPTCEAVRC DAVHQPPKGL VRCAHSPIGE FTYKSSCAFS CEEGFELHGS TQLECTSQGQ 490 500 510 520 530 540 WTEEVPSCQV VKCSSLAVPG KINMSCSGEP VFGTVCKFAC PEGWTLNGSA ARTCGATGHW 550 560 570 580 590 600 SGLLPTCEAP TESNIPLVAG LSAAGLSLLT LAPFLLWLRK CLRKAKKFVP ASSCQSLESD 610 GSYQKPSYIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Endothelial leukocyte adhesion molecule 1: direct expression cloning and functional interactions." 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. Proc. Natl. Acad. Sci. U.S.A. 87:1673-1677(1990) [PubMed: 1689848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION. Tissue: Umbilical vein endothelial cell.
[2]	"Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins." Bevilacqua M.P., Stengelin S., Gimbrone M.A. Jr., Seed B. Science 243:1160-1165(1989) [PubMed: 2466335] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure and chromosomal location of the gene for endothelial-leukocyte adhesion molecule 1." Collins T., Williams A., Johnston G.I., Kim J., Eddy R., Shows T., Gimbrone M.A. Jr., Bevilacqua M.P. J. Biol. Chem. 266:2466-2473(1991) [PubMed: 1703529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	SeattleSNPs variation discovery resource Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-21; ILE-31; ARG-149; PRO-257; LYS-295; GLN-421; TYR-468; SER-550 AND PHE-575.
[5]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"ELAM-1 mediates cell adhesion by recognition of a carbohydrate ligand, sialyl-Lex." Phillips M.L., Nudelman E., Gaeta F.C., Perez M., Singhal A.K., Hakomori S., Paulson J.C. Science 250:1130-1132(1990) [PubMed: 1701274] [Abstract] Cited for: LIGAND.
[7]	"Modelling the carbohydrate recognition domain of human E-selectin." Mills A. FEBS Lett. 319:5-11(1993) [PubMed: 7681016] [Abstract] Cited for: 3D-STRUCTURE MODELING OF LECTIN DOMAIN.
[8]	"Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains." 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. Nature 367:532-538(1994) [PubMed: 7509040] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-178.
[9]	"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." Somers W.S., Tang J., Shaw G.D., Camphausen R.T. Cell 103:467-479(2000) [PubMed: 11081633] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 22-178 IN COMPLEX WITH CALCIUM IONS, SELPLG, SUBUNIT, DISULFIDE BONDS.
[10]	Erratum Somers W.S., Tang J., Shaw G.D., Camphausen R.T. Cell 105:971-971(2001)
[11]	"E-selectin polymorphism and atherosclerosis: an association study." Wenzel K., Felix S., Kleber F.X., Brachold R., Menke T., Schattke S., Schulte K.L., Glaser C., Rohde K., Baumann G., Speer A. Hum. Mol. Genet. 3:1935-1937(1994) [PubMed: 7533025] [Abstract] Cited for: VARIANT ARG-149.
[12]	"DNA polymorphisms in adhesion molecule genes -- a new risk factor for early atherosclerosis." Wenzel K., Ernst M., Rohde K., Baumann G., Speer A. Hum. Genet. 97:15-20(1996) [PubMed: 8557254] [Abstract] Cited for: VARIANTS ARG-149 AND PHE-575.
[13]	"A PstI polymorphism detects the mutation of serine-128 to arginine in CD 62E gene - a risk factor for coronary artery disease." Ye S.Q., Usher D., Virgil D., Zhang L.Q., Yochim S.E., Gupta R. J. Biomed. Sci. 6:18-21(1999) [PubMed: 9933738] [Abstract] Cited for: VARIANT ARG-149.
[14]	"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis." Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A. Nat. Genet. 22:239-247(1999) [PubMed: 10391210] [Abstract] Cited for: VARIANTS ARG-149; TYR-468 AND PHE-575.
[15]	"Relationship between E-selectin L/F554 polymorphism and blood pressure in the Stanislas cohort." Sass C., Pallaud C., Zannad F., Visvikis S. Hum. Genet. 107:58-61(2000) [PubMed: 10982036] [Abstract] Cited for: VARIANT PHE-575.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

SeattleSNPs

Functional Glycomics Gateway - Glycan Binding

E-selectin

Cross-references

Sequence databases

EMBLGenBankDDBJ

M30640 mRNA. Translation: AAA52377.1.
M61893 , M61895, M61887, M61888, M61890, M61891, M61892 Genomic DNA. Translation: AAA52375.1.
M24736 mRNA. Translation: AAA52376.1.
AF540378 Genomic DNA. Translation: AAN01237.1.
AL021940 Genomic DNA. Translation: CAA17434.1.

IPI

IPI00296542.

PIR

A35046. A38615.

RefSeq

NP_000441.2.

UniGene

Hs.82848

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ESL	X-ray	2.00	A	22-183	[»]
1G1T	X-ray	1.50	A	22-178	[»]
1KJA	model	-	A	22-141	[»]

ModBase

Search...

Proteomic databases

PRIDE

P16581.

Genome annotation databases

Ensembl

ENSG00000007908. Homo sapiens. [Contig view]

GeneID

6401.

KEGG

hsa:6401.

Organism-specific databases

GeneCards

GC01M167958.

H-InvDB

HIX0028687.

HGNC

HGNC:10718. SELE.

HPA

CAB002143.

MIM

131210. gene.

Orphanet

34145. Berger disease.

PharmGKB

PA35640.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P16581.

HOVERGEN

P16581.

OMA

P16581. KSSCAFS.

Enzyme and pathway databases

Pathway_Interaction_DB

txa2pathway. Thromboxane A2 receptor signaling.

Gene expression databases

ArrayExpress

P16581.

Bgee

P16581.

GermOnline

ENSG00000007908. Homo sapiens.

Family and domain databases

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016060. Complement_control_module.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR002396. Selectin.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.
G3DSA:2.10.70.10. Complement_control_module. 6 hits.

Pfam

PF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 6 hits.
[Graphical view]

PRINTS

PR00343. SELECTIN.

SMART

SM00032. CCP. 6 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]

PROSITE

PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50923. SUSHI. 6 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

24870.

SOURCE

Search...

Entry information

Entry name

LYAM2_HUMAN

Accession

Primary (citable) accession number: P16581
Secondary accession number(s): P16111

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)