LYAM2_RAT
ID LYAM2_RAT Reviewed; 549 AA.
AC P98105;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
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; Synonyms=Elam-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Rosenbloom C.L., Auchampach J.A., Anderson D.C., Manning A.M.;
RL Submitted (NOV-1993) 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:0000250|UniProtKB:P16581}.
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}.
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DR EMBL; L25527; AAA41113.1; -; mRNA.
DR RefSeq; NP_620234.1; NM_138879.1.
DR AlphaFoldDB; P98105; -.
DR SMR; P98105; -.
DR STRING; 10116.ENSRNOP00000068171; -.
DR BindingDB; P98105; -.
DR ChEMBL; CHEMBL2554; -.
DR GlyGen; P98105; 11 sites.
DR PaxDb; P98105; -.
DR PRIDE; P98105; -.
DR GeneID; 25544; -.
DR KEGG; rno:25544; -.
DR UCSC; RGD:3654; rat.
DR CTD; 6401; -.
DR RGD; 3654; Sele.
DR VEuPathDB; HostDB:ENSRNOG00000002723; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_020848_1_0_1; -.
DR InParanoid; P98105; -.
DR OrthoDB; 445079at2759; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:P98105; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002723; Expressed in heart and 7 other tissues.
DR ExpressionAtlas; P98105; baseline and differential.
DR Genevisible; P98105; RN.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070492; F:oligosaccharide binding; ISO:RGD.
DR GO; GO:0043274; F:phospholipase binding; ISO:RGD.
DR GO; GO:0033691; F:sialic acid binding; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
DR GO; GO:0030029; P:actin filament-based process; ISO:RGD.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IMP:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0050900; P:leukocyte migration; IEP:RGD.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:RGD.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0070555; P:response to interleukin-1; ISO:RGD.
DR CDD; cd00033; CCP; 5.
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; 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; 5.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 5.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 5.
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; 5.
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:0000255"
FT CHAIN 22..549
FT /note="E-selectin"
FT /id="PRO_0000017496"
FT TOPO_DOM 22..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..549
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 429..487
FT /note="Sushi 5"
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 60
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 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
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 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
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..472
FT /evidence="ECO:0000250"
FT DISULFID 458..485
FT /evidence="ECO:0000250"
SQ 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
