LYAM2_HORSE
ID LYAM2_HORSE Reviewed; 610 AA.
AC Q95LG1;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION
RP BY LIPOPOLYSACCHARIDE.
RX PubMed=11529941; DOI=10.1046/j.1365-2567.2001.01262.x;
RA Hedges J.F., Demaula C.D., Moore B.D., McLaughlin B.E., Simon S.I.,
RA MacLachlan N.J.;
RT "Characterization of equine E-selectin.";
RL Immunology 103:498-504(2001).
CC -!- FUNCTION: Cell-surface glycoprotein having a role in immunoadhesion
CC (PubMed:11529941). Mediates in the adhesion of blood neutrophils in
CC cytokine-activated endothelium through interaction with SELPLG/PSGL1.
CC May have a role in capillary morphogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P16581, ECO:0000269|PubMed:11529941}.
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:11529941};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated in endothelial cells after exposure to
CC bacterial lipopolysaccharide (LPS). {ECO:0000269|PubMed:11529941}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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DR EMBL; AF307972; AAK48712.1; -; mRNA.
DR RefSeq; NP_001075324.1; NM_001081855.2.
DR AlphaFoldDB; Q95LG1; -.
DR SMR; Q95LG1; -.
DR STRING; 9796.ENSECAP00000006957; -.
DR PaxDb; Q95LG1; -.
DR GeneID; 100033910; -.
DR KEGG; ecb:100033910; -.
DR CTD; 6401; -.
DR InParanoid; Q95LG1; -.
DR Proteomes; UP000002281; 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; 2.
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..610
FT /note="E-selectin"
FT /id="PRO_0000017491"
FT TOPO_DOM 22..555
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..138
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 139..174
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 177..238
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 239..300
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 314..363
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 365..426
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 428..489
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 490..548
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT BINDING 101..108
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 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 112..117
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 125..127
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..137
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 110..129
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 142..153
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 147..162
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 164..173
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 179..223
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 192..205
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 209..236
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 241..285
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 254..267
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 271..298
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 303..348
FT /evidence="ECO:0000250"
FT DISULFID 334..361
FT /evidence="ECO:0000250"
FT DISULFID 366..411
FT /evidence="ECO:0000250"
FT DISULFID 397..424
FT /evidence="ECO:0000250"
FT DISULFID 429..474
FT /evidence="ECO:0000250"
FT DISULFID 460..487
FT /evidence="ECO:0000250"
FT DISULFID 492..533
FT /evidence="ECO:0000250"
FT DISULFID 519..546
FT /evidence="ECO:0000250"
SQ SEQUENCE 610 AA; 66191 MW; F9D3DED12C445382 CRC64;
MIASQFLSAL TLVLLIKESG AWSYSASTTN MTFDEASAYC QQRYTHLVAI QNQEEIKYLN
SIFNHSPSYY WIGIRKVNDK WVWIGTQKPL TEEAKNWAPG EPNNKQNEDC VEIYIKRYKD
AGKWNDENCN KKKLALCYTA ACTHTSCSGH GECVETINNY TCQCHPGFTG LRCEQVVTCQ
AQEAPEHGRL VCTHPLGNFS YNSSCSVSCE EGYLPSRTEA MQCTSSGEWS APPPACHVVE
CDALTNPANG VMQCSQSPGS FPWNTTCTFD CQEGFELTGP QHLQCTPSGN WDNEKPTCKA
VTCGAGGHPQ NGFVNCSHSS AGEFTFNSSC NFTCEEGFVL QGPAQVECTA QGQWTQQVPV
CKALQCKALS RPERGYMSCR PSTSGSFQSG SSCEFSCEQG FVLKGSKKLR CGPTGEWDSE
KPTCEAVRCD AVRQPQGGLV RCTHSAAGEF TYKSSCAFSC EEGFELRGSA QLECTLQGQW
TQEVPSCQVV QCASLAVPGK VSMSCSGEPV FGAVCTFACP EGWTLNGSAA LTCGATGHWS
GMLPTCEATA KSNIPLTVGL SAAGTSLLTL ASFLFWLLKR LRRKAKKFVP ASSYQSLQSD
GSYQMPSESA
