LYAM2_BOVIN
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 03-AUG-2022, entry version 156.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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 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 immunoadhesion.
CC Mediates in the adhesion of blood neutrophils in cytokine-activated
CC endothelium through interaction with SELPLG/PSGL1. May have a role in
CC capillary morphogenesis. {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 this
CC interaction. {ECO:0000250|UniProtKB:P16581}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16581};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16581}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P98107; -.
DR SMR; P98107; -.
DR PaxDb; P98107; -.
DR Ensembl; ENSBTAT00000009612; ENSBTAP00000009612; ENSBTAG00000007307.
DR GeneID; 281484; -.
DR KEGG; bta:281484; -.
DR CTD; 6401; -.
DR VEuPathDB; HostDB:ENSBTAG00000007307; -.
DR VGNC; VGNC:34421; SELE.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000160168; -.
DR HOGENOM; CLU_020848_1_0_1; -.
DR InParanoid; P98107; -.
DR OMA; AGMWNDE; -.
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 neutrophil and 32 other tissues.
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:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IBA:GO_Central.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
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; 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; Disulfide bond; EGF-like domain;
KW Glycoprotein; Lectin; Membrane; Metal-binding; Reference proteome; Repeat;
KW Signal; Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..485
FT /note="E-selectin"
FT /id="PRO_0000017489"
FT TOPO_DOM 23..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..140
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 141..176
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 179..239
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 240..301
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 302..364
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 365..423
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 466..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..110
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 114..119
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 127..129
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..139
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 112..131
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 144..155
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 149..164
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 166..175
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 181..224
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 194..206
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 210..237
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 242..286
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 255..268
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 272..299
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 304..349
FT /evidence="ECO:0000250"
FT DISULFID 335..362
FT /evidence="ECO:0000250"
FT DISULFID 367..408
FT /evidence="ECO:0000250"
FT DISULFID 394..421
FT /evidence="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
