LYAM2_RABIT
ID LYAM2_RABIT Reviewed; 551 AA.
AC P27113;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 137.
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 {ECO:0000303|PubMed:1372169};
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 2;
DE Short=LECAM2;
DE AltName: CD_antigen=CD62E;
DE Flags: Precursor;
GN Name=SELE;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY CYTOKINES.
RC TISSUE=Heart;
RX PubMed=1372169; DOI=10.1089/dna.1992.11.149;
RA Larigan J.D., Tsang T.C., Rumberger J.M., Burns D.K.;
RT "Characterization of cDNA and genomic sequences encoding rabbit ELAM-1:
RT conservation of structure and functional interactions with leukocytes.";
RL DNA Cell Biol. 11:149-162(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. 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 -!- INDUCTION: By cytokines. {ECO:0000269|PubMed:1372169}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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DR EMBL; M91004; AAA31243.1; -; mRNA.
DR EMBL; M91005; AAA31244.1; -; mRNA.
DR PIR; I46709; I46709.
DR RefSeq; NP_001075781.1; NM_001082312.1.
DR AlphaFoldDB; P27113; -.
DR SMR; P27113; -.
DR STRING; 9986.ENSOCUP00000026008; -.
DR GeneID; 100009151; -.
DR KEGG; ocu:100009151; -.
DR CTD; 6401; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P27113; -.
DR OrthoDB; 445079at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
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; 1.
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..23
FT CHAIN 24..551
FT /note="E-selectin"
FT /id="PRO_0000017495"
FT TOPO_DOM 24..495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..141
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 142..177
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 180..241
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 242..303
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 305..366
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 368..429
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 430..488
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT BINDING 103..111
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
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 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 115..120
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT BINDING 128..130
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
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 BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..140
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 113..132
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 145..156
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 150..165
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 167..176
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 182..226
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 195..208
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 212..239
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 244..288
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 257..270
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 274..301
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 306..351
FT /evidence="ECO:0000250"
FT DISULFID 337..364
FT /evidence="ECO:0000250"
FT DISULFID 369..414
FT /evidence="ECO:0000250"
FT DISULFID 400..427
FT /evidence="ECO:0000250"
FT DISULFID 432..473
FT /evidence="ECO:0000250"
FT DISULFID 459..486
FT /evidence="ECO:0000250"
FT CONFLICT 308
FT /note="T -> A (in Ref. 1; AAA31244)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="T -> A (in Ref. 1; AAA31244)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="A -> V (in Ref. 1; AAA31244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 60347 MW; 23BC8A883B23240E CRC64;
MVASWLLSTL TFALVLLIKE TSTWTYHFSA ENMTYDEASA YCQQNYTHLV AIQNKEEIDY
LNSILDYSPS YYWIGIRKVN NVWIWVGTHK PLTEGAKNWA PGEPNNKQNN EDCVEIYIKR
PKDTGMWNDE RCSKKKLALC YTAACTEASC SGHGECIETI NNYSCKCYPG FSGLKCEQVV
TCEAQVQPQH GSLNCTHPLG NFSYNSSCSV SCERGYLPSS TETTWCTSSG EWSAPPATCK
VVECDTMGKP ANGDVKCSPS QGSAPWNTTC TFDCEEGFTL LGARSLQCTS SGSWDNEKPT
CKAVSCDTIH HPQNGSVSCS NSSEGKFTFR SSCNFTCEEN FLLRGPAQVE CTAQGQWTQQ
APVCEAVKCD PVHTLEDGFV KCTHPHTGEF TYKSSCTFNC REGFELHGSA QLECTSQGQW
AQELPSCQVV QCPSLAVLGK TNVSCSGEPV FGTVCNFACP EGWTLNGSAA LMCGAEGQWS
GMLPTCEEPI ASNVPLAVGL SVSGTSFLTL TSFLLWFLKY FRKKAKKFVP ASSRYVGLEA
HGNCQVPSHL I
