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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_PIG               Reviewed;         484 AA.
P98110;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
28-FEB-2018, entry version 122.
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;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Aortic endothelium;
PubMed=7526854; DOI=10.1006/bbrc.1994.2525;
Rollins S.A., Evans M.J., Johnson K.K., Elliot E.A., Squinto S.P.,
Matis L.A., Rother R.P.;
"Molecular and functional analysis of porcine E-selectin reveals a
potential role in xenograft rejection.";
Biochem. Biophys. Res. Commun. 204:763-771(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Aortic endothelium;
PubMed=7516159; DOI=10.1006/bbrc.1994.1772;
Tsang Y.T.M., Haskard D.O., Robinson M.K.;
"Cloning and expression kinetics of porcine vascular cell adhesion
molecule.";
Biochem. Biophys. Res. Commun. 201:805-812(1994).
-!- FUNCTION: Cell-surface glycoprotein having a role in
immunoadhesion (PubMed:7526854). Mediates in the adhesion of blood
neutrophils in cytokine-activated endothelium through interaction
with SELPLG/PSGL1. May have a role in capillary morphogenesis (By
similarity). {ECO:0000250|UniProtKB:P16581,
ECO:0000269|PubMed:7526854}.
-!- 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:0000269|PubMed:7526854};
Single-pass type I membrane protein {ECO:0000305}.
-!- MISCELLANEOUS: Important in acute cellular allograft rejection and
probably also in xenograft rejection.
{ECO:0000269|PubMed:7526854}.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L39076; AAA61545.1; -; mRNA.
EMBL; U08350; AAA21541.1; -; mRNA.
RefSeq; NP_999433.1; NM_214268.1.
UniGene; Ssc.16297; -.
ProteinModelPortal; P98110; -.
SMR; P98110; -.
STRING; 9823.ENSSSCP00000006699; -.
PaxDb; P98110; -.
PRIDE; P98110; -.
GeneID; 397508; -.
KEGG; ssc:397508; -.
CTD; 6401; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; P98110; -.
KO; K06494; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
CDD; cd00033; CCP; 4.
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; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 4.
PRINTS; PR00343; SELECTIN.
SMART; SM00032; CCP; 4.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57535; SSF57535; 4.
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; 4.
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 22 {ECO:0000255}.
CHAIN 23 484 E-selectin.
/FTId=PRO_0000017494.
TOPO_DOM 23 429 Extracellular. {ECO:0000255}.
TRANSMEM 430 451 Helical. {ECO:0000255}.
TOPO_DOM 452 484 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 179 237 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 251 300 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 301 363 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 364 422 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 102 110 Carbohydrate binding.
{ECO:0000250|UniProtKB:P16581}.
REGION 114 119 Carbohydrate binding.
{ECO:0000250|UniProtKB:P16581}.
REGION 127 129 Carbohydrate binding.
{ECO:0000250|UniProtKB:P16581}.
METAL 102 102 Calcium. {ECO:0000250|UniProtKB:P16581}.
METAL 104 104 Calcium. {ECO:0000250|UniProtKB:P16581}.
METAL 110 110 Calcium. {ECO:0000250|UniProtKB:P16581}.
METAL 127 127 Calcium. {ECO:0000250|UniProtKB:P16581}.
METAL 128 128 Calcium. {ECO:0000250|UniProtKB:P16581}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 254 254 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 376 376 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 139 {ECO:0000250|UniProtKB:P16581}.
DISULFID 112 131 {ECO:0000250|UniProtKB:P16581}.
DISULFID 144 155 {ECO:0000250|UniProtKB:P16581}.
DISULFID 149 164 {ECO:0000250|UniProtKB:P16581}.
DISULFID 166 175 {ECO:0000250|UniProtKB:P16581}.
DISULFID 181 222 {ECO:0000250|UniProtKB:P16581}.
DISULFID 194 204 {ECO:0000250|UniProtKB:P16581}.
DISULFID 208 235 {ECO:0000250|UniProtKB:P16581}.
DISULFID 240 285 {ECO:0000250}.
DISULFID 271 298 {ECO:0000250}.
DISULFID 303 348 {ECO:0000250}.
DISULFID 334 361 {ECO:0000250}.
DISULFID 366 407 {ECO:0000250}.
DISULFID 393 420 {ECO:0000250}.
CONFLICT 253 253 C -> Y (in Ref. 2; AAA21541).
{ECO:0000305}.
CONFLICT 313 313 L -> F (in Ref. 2; AAA21541).
{ECO:0000305}.
CONFLICT 321 321 T -> N (in Ref. 2; AAA21541).
{ECO:0000305}.
CONFLICT 327 327 K -> N (in Ref. 2; AAA21541).
{ECO:0000305}.
CONFLICT 363 363 V -> A (in Ref. 2; AAA21541).
{ECO:0000305}.
CONFLICT 384 384 V -> M (in Ref. 2; AAA21541).
{ECO:0000305}.
CONFLICT 461 484 KFVPSSSSECLQPNGSYQMPSDLI -> NLFLPAAPNAFNP
MDPTKCLLT (in Ref. 2; AAA21541).
{ECO:0000305}.
SEQUENCE 484 AA; 52567 MW; AFF74FE25C1FD013 CRC64;
MIASQFLSAL PLVLLLLRES GAWSYSASTE TMTFDDASAY CQQRYTHLVA IQNHAEIEYL
NSTFNYSASY YWIGIRKING TWTWIGTKKA LTPEATNWAP GEPNNKQSNE DCVEIYIKRD
KDSGKWNDER CSKKKLALCY TAACTPTSCS GHGECIETIN SSTCQCYPGF RGLQCEQVVE
CDALENPVNG VVTCPQSLPW NTTCAFECKE GFELIGPEHL QCTSSGSWDG KKPTCKAVTC
DTVGHPQNGD VSCNHSSIGE FAYKSTCHFT CAEGFGLQGP AQIECTAQGQ WTQQAPVCKA
VKCPAVSQPK NGLVKFTHSP TGEFTYKSSC AFSCEEGFEL RGSAQLACTS QGQWTQEVPS
CQVVQCSSLE VPREINMSCS GEPVFGAVCT FACPEGWMLN GSVALTCGAT GHWSGMLPTC
EAPAESKIPL AMGLAAGGVS FMTSASFLLW LLKRLRKRAK KFVPSSSSEC LQPNGSYQMP
SDLI


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