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Database: UniProt
Entry: P98107
LinkDB: P98107
Original site: P98107 
ID   LYAM2_BOVIN             Reviewed;         485 AA.
AC   P98107; A6QP78;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   13-FEB-2019, entry version 144.
DE   RecName: Full=E-selectin;
DE   AltName: Full=CD62 antigen-like family member E;
DE   AltName: Full=Endothelial leukocyte adhesion molecule 1;
DE            Short=ELAM-1;
DE   AltName: Full=Leukocyte-endothelial cell adhesion molecule 2;
DE            Short=LECAM2;
DE   AltName: CD_antigen=CD62E;
DE   Flags: Precursor;
GN   Name=SELE;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Adrenal gland;
RX   PubMed=7690465; DOI=10.1038/365267a0;
RA   Nguyen M., Strubel N.A., Bischoff J.;
RT   "A role for sialyl Lewis-X/A glycoconjugates in capillary
RT   morphogenesis.";
RL   Nature 365:267-269(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell-surface glycoprotein having a role in
CC       immunoadhesion. Mediates in the adhesion of blood neutrophils in
CC       cytokine-activated endothelium through interaction with
CC       SELPLG/PSGL1. May have a role in capillary morphogenesis.
CC       {ECO:0000269|PubMed:7690465}.
CC   -!- SUBUNIT: Interacts with SELPLG/PSGL1 and PODXL2 through the sialyl
CC       Lewis X epitope. SELPLG sulfation appears not to be required for
CC       this interaction. {ECO:0000250|UniProtKB:P16581}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P16581}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P16581}.
CC   -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
DR   EMBL; L12039; AAA02991.1; -; mRNA.
DR   EMBL; BC149190; AAI49191.1; -; mRNA.
DR   PIR; S36772; S36772.
DR   RefSeq; NP_776606.1; NM_174181.2.
DR   UniGene; Bt.197; -.
DR   ProteinModelPortal; P98107; -.
DR   SMR; P98107; -.
DR   STRING; 9913.ENSBTAP00000055695; -.
DR   PaxDb; P98107; -.
DR   PRIDE; P98107; -.
DR   Ensembl; ENSBTAT00000009612; ENSBTAP00000009612; ENSBTAG00000007307.
DR   GeneID; 281484; -.
DR   KEGG; bta:281484; -.
DR   CTD; 6401; -.
DR   VGNC; VGNC:34421; SELE.
DR   eggNOG; KOG4297; Eukaryota.
DR   eggNOG; ENOG410XPJ1; LUCA.
DR   GeneTree; ENSGT00940000160168; -.
DR   HOGENOM; HOG000236254; -.
DR   HOVERGEN; HBG052375; -.
DR   InParanoid; P98107; -.
DR   KO; K06494; -.
DR   OrthoDB; 445079at2759; -.
DR   Reactome; R-BTA-202733; Cell surface interactions at the vascular wall.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000007307; Expressed in 3 organ(s), highest expression level in spleen.
DR   ExpressionAtlas; P98107; baseline and differential.
DR   GO; GO:0005901; C:caveola; IEA:Ensembl.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR   GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0070492; F:oligosaccharide binding; IEA:Ensembl.
DR   GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR   GO; GO:0033691; F:sialic acid binding; IEA:Ensembl.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:Ensembl.
DR   GO; GO:0030029; P:actin filament-based process; IEA:Ensembl.
DR   GO; GO:0007202; P:activation of phospholipase C activity; IEA:Ensembl.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR   GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR   GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
DR   CDD; cd00033; CCP; 4.
DR   CDD; cd03592; CLECT_selectins_like; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR033991; Selectin_CTLD.
DR   InterPro; IPR002396; Selectin_superfamily.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 4.
DR   PRINTS; PR00343; SELECTIN.
DR   SMART; SM00032; CCP; 4.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   SUPFAM; SSF57535; SSF57535; 4.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50923; SUSHI; 4.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Signal; Sushi;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000250}.
FT   CHAIN        23    485       E-selectin.
FT                                /FTId=PRO_0000017489.
FT   TOPO_DOM     23    430       Extracellular. {ECO:0000255}.
FT   TRANSMEM    431    453       Helical. {ECO:0000255}.
FT   TOPO_DOM    454    485       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       23    140       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      141    176       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      179    239       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      240    301       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      302    364       Sushi 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      365    423       Sushi 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION      102    110       Carbohydrate binding.
FT                                {ECO:0000250|UniProtKB:P16581}.
FT   REGION      114    119       Carbohydrate binding.
FT                                {ECO:0000250|UniProtKB:P16581}.
FT   REGION      127    129       Carbohydrate binding.
FT                                {ECO:0000250|UniProtKB:P16581}.
FT   METAL       102    102       Calcium. {ECO:0000250|UniProtKB:P16581}.
FT   METAL       104    104       Calcium. {ECO:0000250|UniProtKB:P16581}.
FT   METAL       110    110       Calcium. {ECO:0000250|UniProtKB:P16581}.
FT   METAL       127    127       Calcium. {ECO:0000250|UniProtKB:P16581}.
FT   METAL       128    128       Calcium. {ECO:0000250|UniProtKB:P16581}.
FT   CARBOHYD     61     61       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     88     88       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    161    161       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    203    203       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    265    265       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    312    312       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    316    316       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    379    379       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     41    139       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    112    131       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    144    155       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    149    164       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    166    175       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    181    224       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    194    206       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    210    237       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    242    286       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    255    268       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    272    299       {ECO:0000250|UniProtKB:P16581}.
FT   DISULFID    304    349       {ECO:0000250}.
FT   DISULFID    335    362       {ECO:0000250}.
FT   DISULFID    367    408       {ECO:0000250}.
FT   DISULFID    394    421       {ECO:0000250}.
SQ   SEQUENCE   485 AA;  53200 MW;  AE931C9B521E3904 CRC64;
     MIVSQYLSAL TFVLLLFKES RTWSYHASTE MMTFEEARDY CQKTYTALVA IQNQEEIEYL
     NSTFSYSPSY YWIGIRKING TWTWIGTNKS LTKEATNWAP GEPNNKQSDE DCVEIYIKRE
     KDSGKWNDEK CTKQKLALCY KAACNPTPCG SHGECVETIN NYTCQCHPGF KGLKCEQVVT
     CPAQKHPEHG HLVCNPLGKF TYNSSCSISC AEGYLPSSTE ATRCMSSGEW STPLPKCNVV
     KCDALSNLDN GVVNCSPNHG SLPWNTTCTF ECQEGYKLTG PQHLQCTSSG IWDNKQPTCK
     AVSCAAISHP QNGTVNCSHS VVGDFAFKSS CHFTCAEGFT LQGPTQVECT AQGQWTQRVP
     VCEVVRCSRL DVSGKLNMNC SGEPVLGTEC TFACPERWTL NGSVVLTCGA TGHWSGMLPT
     CEAPTVSQTP LAVGLSTAGV SLVTIPSFLF WLLKRLQKKA KKFSPASSCS SLKSNGCYST
     PSKLI
//
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