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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_CANLF             Reviewed;         611 AA.
P33730;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
10-MAY-2017, entry version 117.
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;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Jugular vein;
Manning A.M., Lane C.L., Auchampach J.A., Kukielka G.L.,
Rosenbloom C.L., Anderson D.C.;
"Molecular cloning of canine E-selectin and regulation of
expression.";
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
-!- 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.
-!- SUBUNIT: Interacts with PSGL1/SELPLG and PODXL2 through the sialyl
Lewis X epitope. PSGL1 sulfation appears not to be required for
this interaction (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P16581}; Single-pass type I membrane
protein.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L23087; AAA30843.1; -; mRNA.
UniGene; Cfa.3868; -.
ProteinModelPortal; P33730; -.
SMR; P33730; -.
STRING; 9615.ENSCAFP00000022350; -.
PaxDb; P33730; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; P33730; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR033991; Selectin_CTLD.
InterPro; IPR002396; Selectin_superfamily.
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; 3.
SMART; SM00179; EGF_CA; 1.
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.
2: Evidence at transcript level;
Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Lectin; Membrane; Reference proteome;
Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 611 E-selectin.
/FTId=PRO_0000017490.
TOPO_DOM 23 557 Extracellular. {ECO:0000255}.
TRANSMEM 558 579 Helical. {ECO:0000255}.
TOPO_DOM 580 611 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 140 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 141 176 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 179 240 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 241 302 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 316 365 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 367 428 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 430 491 Sushi 5. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 492 550 Sushi 6. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 313 313 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 528 528 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 139 {ECO:0000250}.
DISULFID 112 131 {ECO:0000250}.
DISULFID 144 155 {ECO:0000250}.
DISULFID 149 164 {ECO:0000250}.
DISULFID 166 175 {ECO:0000250}.
DISULFID 181 225 {ECO:0000250}.
DISULFID 211 238 {ECO:0000250}.
DISULFID 243 287 {ECO:0000250}.
DISULFID 273 300 {ECO:0000250}.
DISULFID 305 350 {ECO:0000250}.
DISULFID 336 363 {ECO:0000250}.
DISULFID 368 413 {ECO:0000250}.
DISULFID 399 426 {ECO:0000250}.
DISULFID 431 476 {ECO:0000250}.
DISULFID 462 489 {ECO:0000250}.
DISULFID 494 535 {ECO:0000250}.
DISULFID 521 548 {ECO:0000250}.
SEQUENCE 611 AA; 66315 MW; 35DA9E3DF225E4F6 CRC64;
MITSQLLPAL TLVLLLFKEG GAWSYNASTE AMTFDEASTY CQQRYTHLVA IQNQEEIKYL
NSMFTYTPTY YWIGIRKVNK KWTWIGTQKL LTEEAKNWAP GEPNNKQNDE DCVEIYIKRD
KDSGKWNDER CDKKKLALCY TAACTPTSCS GHGECVETVN NYTCKCHPGF RGLRCEQVVT
CQAQEAPEHG SLVCTHPLGT FSYNSSCFVS CDKGYLPSST EATQCTSTGE WSASPPACNV
VECSALTNPC HGVMDCLQSS GNFPWNMTCT FECEEGFELM GPKRLQCTSS GNWDNRKPTC
KAVTCGAIGH PQNGSVSCSH SPAGEFSVRS SCNFTCNEGF LMQGPAQIEC TAQGQWSQQV
PVCKASQCKA LSSPERGYMS CLPGASGSFQ SGSSCEFFCE KGFVLKGSKT LQCGLTGKWD
SEEPTCEAVK CDAVQQPQDG LVRCAHSSTG EFTYKSSCAF SCEEGFELHG SAQLECTSQG
QGVTGGPSCQ VVQCFKSGSF RKDEHKLQGE PVFGAVCAFA CPEGWTLNGS AALMCDATGH
WSGMLPTCEA PTESSIPLAV GLTAGGTSLL TVASFLLWLL KRLRKRAKKF VPASSCQSLQ
SDGSYHMPCS I


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