LYAM2_CANLF
ID LYAM2_CANLF Reviewed; 611 AA.
AC P33730;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Jugular vein;
RA Manning A.M., Lane C.L., Auchampach J.A., Kukielka G.L., Rosenbloom C.L.,
RA Anderson D.C.;
RT "Molecular cloning of canine E-selectin and regulation of expression.";
RL Submitted (AUG-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; L23087; AAA30843.1; -; mRNA.
DR AlphaFoldDB; P33730; -.
DR SMR; P33730; -.
DR STRING; 9615.ENSCAFP00000022347; -.
DR PaxDb; P33730; -.
DR PRIDE; P33730; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P33730; -.
DR Proteomes; UP000002254; Unplaced.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070492; F:oligosaccharide binding; IBA:GO_Central.
DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
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:0034097; P:response to cytokine; IBA:GO_Central.
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; 3.
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..22
FT /evidence="ECO:0000250"
FT CHAIN 23..611
FT /note="E-selectin"
FT /id="PRO_0000017490"
FT TOPO_DOM 23..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..611
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..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 316..365
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 367..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 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 26
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 204
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 333
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 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..225
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 194..207
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 211..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 611 AA; 66315 MW; 35DA9E3DF225E4F6 CRC64;
MITSQLLPAL TLVLLLFKEG GAWSYNASTE AMTFDEASTY CQQRYTHLVA IQNQEEIKYL
NSMFTYTPTY YWIGIRKVNK KWTWIGTQKL LTEEAKNWAP GEPNNKQNDE DCVEIYIKRD
KDSGKWNDER CDKKKLALCY TAACTPTSCS GHGECVETVN NYTCKCHPGF RGLRCEQVVT
CQAQEAPEHG SLVCTHPLGT FSYNSSCFVS CDKGYLPSST EATQCTSTGE WSASPPACNV
VECSALTNPC HGVMDCLQSS GNFPWNMTCT FECEEGFELM GPKRLQCTSS GNWDNRKPTC
KAVTCGAIGH PQNGSVSCSH SPAGEFSVRS SCNFTCNEGF LMQGPAQIEC TAQGQWSQQV
PVCKASQCKA LSSPERGYMS CLPGASGSFQ SGSSCEFFCE KGFVLKGSKT LQCGLTGKWD
SEEPTCEAVK CDAVQQPQDG LVRCAHSSTG EFTYKSSCAF SCEEGFELHG SAQLECTSQG
QGVTGGPSCQ VVQCFKSGSF RKDEHKLQGE PVFGAVCAFA CPEGWTLNGS AALMCDATGH
WSGMLPTCEA PTESSIPLAV GLTAGGTSLL TVASFLLWLL KRLRKRAKKF VPASSCQSLQ
SDGSYHMPCS I
