LYAM2_MOUSE
ID LYAM2_MOUSE Reviewed; 612 AA.
AC Q00690;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E-selectin;
DE AltName: Full=CD62 antigen-like family member E;
DE AltName: Full=Endothelial leukocyte adhesion molecule 1 {ECO:0000303|PubMed:1375914};
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; Synonyms=Elam-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1375914; DOI=10.1111/j.1432-1033.1992.tb16940.x;
RA Becker-Andre M., van Huijsduijnen R.H., Losberger C., Whelan J.,
RA Delamarter J.F.;
RT "Murine endothelial leukocyte-adhesion molecule 1 is a close structural and
RT functional homologue of the human protein.";
RL Eur. J. Biochem. 206:401-411(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1378846; DOI=10.1016/s0021-9258(18)42162-x;
RA Weller A., Isenmann S., Vestweber D.;
RT "Cloning of the mouse endothelial selectins. Expression of both E- and P-
RT selectin is inducible by tumor necrosis factor alpha.";
RL J. Biol. Chem. 267:15176-15183(1992).
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 (PubMed:1375914). May
CC have a role in capillary morphogenesis. {ECO:0000250|UniProtKB:P16581,
CC ECO:0000269|PubMed:1375914}.
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:0000269|PubMed:1375914};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16581}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37577.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=E-selectin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_171";
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DR EMBL; M80778; AAA37547.1; -; Genomic_DNA.
DR EMBL; M87862; AAA37577.1; ALT_INIT; mRNA.
DR PIR; S23174; B42755.
DR RefSeq; NP_035475.1; NM_011345.2.
DR RefSeq; XP_006496778.1; XM_006496715.2.
DR AlphaFoldDB; Q00690; -.
DR SMR; Q00690; -.
DR DIP; DIP-59328N; -.
DR IntAct; Q00690; 3.
DR STRING; 10090.ENSMUSP00000027874; -.
DR BindingDB; Q00690; -.
DR ChEMBL; CHEMBL2545; -.
DR GlyGen; Q00690; 9 sites.
DR iPTMnet; Q00690; -.
DR PhosphoSitePlus; Q00690; -.
DR PaxDb; Q00690; -.
DR PRIDE; Q00690; -.
DR ProteomicsDB; 291975; -.
DR ABCD; Q00690; 1 sequenced antibody.
DR DNASU; 20339; -.
DR GeneID; 20339; -.
DR KEGG; mmu:20339; -.
DR CTD; 6401; -.
DR MGI; MGI:98278; Sele.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q00690; -.
DR OrthoDB; 445079at2759; -.
DR PhylomeDB; Q00690; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 20339; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q00690; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q00690; protein.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070492; F:oligosaccharide binding; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0033691; F:sialic acid binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:MGI.
DR GO; GO:0030029; P:actin filament-based process; ISO:MGI.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISO:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0050900; P:leukocyte migration; IGI:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IGI:MGI.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR CDD; cd00033; CCP; 6.
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; 6.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 6.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 6.
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; 6.
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..21
FT /evidence="ECO:0000250"
FT CHAIN 22..612
FT /note="E-selectin"
FT /id="PRO_0000017493"
FT TOPO_DOM 22..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..139
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 140..175
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 178..240
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 241..302
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 303..365
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 366..428
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 430..491
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 492..550
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT BINDING 101..109
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 113..118
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 126..128
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
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 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..138
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 111..130
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 143..154
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 148..163
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 165..174
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 180..225
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 193..206
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 210..238
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 243..287
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 256..269
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 273..300
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 305..350
FT /evidence="ECO:0000250"
FT DISULFID 336..363
FT /evidence="ECO:0000250"
FT DISULFID 368..413
FT /evidence="ECO:0000250"
FT DISULFID 399..426
FT /evidence="ECO:0000250"
FT DISULFID 431..476
FT /evidence="ECO:0000250"
FT DISULFID 462..489
FT /evidence="ECO:0000250"
FT DISULFID 494..535
FT /evidence="ECO:0000250"
FT DISULFID 521..548
FT /evidence="ECO:0000250"
SQ SEQUENCE 612 AA; 66750 MW; 86F05713F0EC2C3D CRC64;
MNASRFLSAL VFVLLAGEST AWYYNASSEL MTYDEASAYC QRDYTHLVAI QNKEEINYLN
SNLKHSPSYY WIGIRKVNNV WIWVGTGKPL TEEAQNWAPG EPNNKQRNED CVEIYIQRTK
DSGMWNDERC NKKKLALCYT ASCTNASCSG HGECIETINS YTCKCHPGFL GPNCEQAVTC
KPQEHPDYGS LNCSHPFGPF SYNSSCSFGC KRGYLPSSME TTVRCTSSGE WSAPAPACHV
VECEALTHPA HGIRKCSSNP GSYPWNTTCT FDCVEGYRRV GAQNLQCTSS GIWDNETPSC
KAVTCDAIPQ PQNGFVSCSH STAGELAFKS SCNFTCEQSF TLQGPAQVEC SAQGQWTPQI
PVCKAVQCEA LSAPQQGNMK CLPSASGPFQ NGSSCEFSCE EGFELKGSRR LQCGPRGEWD
SKKPTCSAVK CDDVPRPQNG VMECAHATTG EFTYKSSCAF QCNEGFSLHG SAQLECTSQG
KWTQEVPSCQ VVQCPSLDVP GKMNMSCSGT AVFGTVCEFT CPDDWTLNGS AVLTCGATGR
WSGMPPTCEA PVSPTRPLVV ALSAAGTSLL TSSSLLYLLM RYFRKKAKKF VPASSCQSLQ
SFENYHVPSY NV
