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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_RAT               Reviewed;         549 AA.
P98105;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
28-FEB-2018, entry version 134.
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=Elam-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
Rosenbloom C.L., Auchampach J.A., Anderson D.C., Manning A.M.;
Submitted (NOV-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
SELPLG/PSGL1. May have a role in capillary morphogenesis.
{ECO:0000250|UniProtKB:P16581}.
-!- SUBUNIT: Interacts with SELPLG/PSGL1 and PODXL2 through the sialyl
Lewis X epitope. SELPLG sulfation appears not to be required for
this interaction. {ECO:0000250|UniProtKB:P16581}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P16581}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P16581}.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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EMBL; L25527; AAA41113.1; -; mRNA.
RefSeq; NP_620234.1; NM_138879.1.
UniGene; Rn.10359; -.
ProteinModelPortal; P98105; -.
SMR; P98105; -.
STRING; 10116.ENSRNOP00000034797; -.
BindingDB; P98105; -.
ChEMBL; CHEMBL2554; -.
PaxDb; P98105; -.
PRIDE; P98105; -.
Ensembl; ENSRNOT00000076757; ENSRNOP00000068171; ENSRNOG00000002723.
GeneID; 25544; -.
KEGG; rno:25544; -.
UCSC; RGD:3654; rat.
CTD; 6401; -.
RGD; 3654; Sele.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00910000143999; -.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; P98105; -.
KO; K06494; -.
OrthoDB; EOG091G04KC; -.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
PRO; PR:P98105; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000002723; -.
ExpressionAtlas; P98105; baseline and differential.
Genevisible; P98105; RN.
GO; GO:0005901; C:caveola; ISO:RGD.
GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070492; F:oligosaccharide binding; ISO:RGD.
GO; GO:0043274; F:phospholipase binding; ISO:RGD.
GO; GO:0033691; F:sialic acid binding; ISO:RGD.
GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
GO; GO:0030029; P:actin filament-based process; ISO:RGD.
GO; GO:0007202; P:activation of phospholipase C activity; ISO:RGD.
GO; GO:0007155; P:cell adhesion; TAS:RGD.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
GO; GO:0006954; P:inflammatory response; IMP:RGD.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
GO; GO:0050900; P:leukocyte migration; IEP:RGD.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:RGD.
GO; GO:0002092; P:positive regulation of receptor internalization; ISO:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0070555; P:response to interleukin-1; ISO:RGD.
CDD; cd00033; CCP; 5.
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; 5.
PRINTS; PR00343; SELECTIN.
SMART; SM00032; CCP; 5.
SMART; SM00034; CLECT; 1.
SMART; SM00181; EGF; 2.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57535; SSF57535; 5.
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; 5.
2: Evidence at transcript level;
Calcium; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane;
Metal-binding; Reference proteome; Repeat; Signal; Sushi;
Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 549 E-selectin.
/FTId=PRO_0000017496.
TOPO_DOM 22 494 Extracellular. {ECO:0000255}.
TRANSMEM 495 516 Helical. {ECO:0000255}.
TOPO_DOM 517 549 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 178 240 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 241 302 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 303 365 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 366 428 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 429 487 Sushi 5. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 101 109 Carbohydrate binding.
{ECO:0000250|UniProtKB:P16581}.
REGION 113 118 Carbohydrate binding.
{ECO:0000250|UniProtKB:P16581}.
REGION 126 128 Carbohydrate binding.
{ECO:0000250|UniProtKB:P16581}.
METAL 101 101 Calcium. {ECO:0000250|UniProtKB:P16581}.
METAL 103 103 Calcium. {ECO:0000250|UniProtKB:P16581}.
METAL 109 109 Calcium. {ECO:0000250|UniProtKB:P16581}.
METAL 126 126 Calcium. {ECO:0000250|UniProtKB:P16581}.
METAL 127 127 Calcium. {ECO:0000250|UniProtKB:P16581}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 203 203 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 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 441 441 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 465 465 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 40 138 {ECO:0000250|UniProtKB:P16581}.
DISULFID 111 130 {ECO:0000250|UniProtKB:P16581}.
DISULFID 143 154 {ECO:0000250|UniProtKB:P16581}.
DISULFID 148 163 {ECO:0000250|UniProtKB:P16581}.
DISULFID 165 174 {ECO:0000250|UniProtKB:P16581}.
DISULFID 180 225 {ECO:0000250|UniProtKB:P16581}.
DISULFID 193 206 {ECO:0000250|UniProtKB:P16581}.
DISULFID 210 238 {ECO:0000250|UniProtKB:P16581}.
DISULFID 243 287 {ECO:0000250|UniProtKB:P16581}.
DISULFID 256 269 {ECO:0000250|UniProtKB:P16581}.
DISULFID 273 300 {ECO:0000250|UniProtKB:P16581}.
DISULFID 305 350 {ECO:0000250}.
DISULFID 336 363 {ECO:0000250}.
DISULFID 368 413 {ECO:0000250}.
DISULFID 399 426 {ECO:0000250}.
DISULFID 431 472 {ECO:0000250}.
DISULFID 458 485 {ECO:0000250}.
SEQUENCE 549 AA; 60080 MW; 85CEECDB7B0144C8 CRC64;
MNASCFLSAL TFVLLIGKSI AWYYNASSEL MTYDEASAYC QRDYTHLVAI QNKEEINYLN
STLRYSPSYY WIGIRKVNNV WIWVGTQKPL TEEAKNWAPG EPNNKQRNED CVEIYIQRPK
DSGMWNDERC DKKKLALCYT ASCTNTSCSG HGECVETINS YTCKCHPGFL GPKCDQVVTC
QEQEYPDHGS LNCTHPFGLF SYNSSCSFSC ERGYVPSSME TTVRCTSSGE WSAPAPACHV
VECKALTQPA HGVRKCSSNP GSYPWNTTCT FDCEEGYRRV GAQNLQCTSS GVWDNEKPSC
KAVTCDAIPR PQNGSVSCSN STAGALAFKS SCNFTCEHSF TLQGPAQVEC SAQGQWTPQI
PVCKASQCEA LSAPQRGHMK CLPSASAPFQ SGSSCKFSCD EGFELKGSRR LQCGPRGEWD
SEKPTCAGVQ CSSLDLPGKM NMSCSGPAVF GTVCEFTCPE GWTLNGSSIL TCGATGRWSA
MLPTCEAPAN PPRPLVVALS VAATSLLTLS SLIYVLKRFF WKKAKKFVPA SSCQSLQSFE
NYQGPSYII


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