LYAM2_PIG
ID LYAM2_PIG Reviewed; 484 AA.
AC P98110;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Aortic endothelium;
RX PubMed=7526854; DOI=10.1006/bbrc.1994.2525;
RA Rollins S.A., Evans M.J., Johnson K.K., Elliot E.A., Squinto S.P.,
RA Matis L.A., Rother R.P.;
RT "Molecular and functional analysis of porcine E-selectin reveals a
RT potential role in xenograft rejection.";
RL Biochem. Biophys. Res. Commun. 204:763-771(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic endothelium;
RX PubMed=7516159; DOI=10.1006/bbrc.1994.1772;
RA Tsang Y.T.M., Haskard D.O., Robinson M.K.;
RT "Cloning and expression kinetics of porcine vascular cell adhesion
RT molecule.";
RL Biochem. Biophys. Res. Commun. 201:805-812(1994).
CC -!- FUNCTION: Cell-surface glycoprotein having a role in immunoadhesion
CC (PubMed:7526854). 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:7526854}.
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:7526854};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Important in acute cellular allograft rejection and
CC probably also in xenograft rejection. {ECO:0000269|PubMed:7526854}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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DR EMBL; L39076; AAA61545.1; -; mRNA.
DR EMBL; U08350; AAA21541.1; -; mRNA.
DR RefSeq; NP_999433.1; NM_214268.1.
DR AlphaFoldDB; P98110; -.
DR SMR; P98110; -.
DR STRING; 9823.ENSSSCP00000006699; -.
DR PaxDb; P98110; -.
DR PRIDE; P98110; -.
DR Ensembl; ENSSSCT00015018437; ENSSSCP00015007307; ENSSSCG00015013883.
DR Ensembl; ENSSSCT00030070356; ENSSSCP00030032085; ENSSSCG00030050466.
DR Ensembl; ENSSSCT00050093099; ENSSSCP00050040160; ENSSSCG00050068229.
DR Ensembl; ENSSSCT00060093921; ENSSSCP00060040635; ENSSSCG00060068755.
DR Ensembl; ENSSSCT00065004958; ENSSSCP00065002143; ENSSSCG00065003630.
DR GeneID; 397508; -.
DR KEGG; ssc:397508; -.
DR CTD; 6401; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P98110; -.
DR OrthoDB; 445079at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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; 4.
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; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 4.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 4.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 4.
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; 4.
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:0000255"
FT CHAIN 23..484
FT /note="E-selectin"
FT /id="PRO_0000017494"
FT TOPO_DOM 23..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..484
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..237
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 251..300
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 301..363
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 364..422
FT /note="Sushi 4"
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 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
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 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
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..222
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 194..204
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 208..235
FT /evidence="ECO:0000250|UniProtKB:P16581"
FT DISULFID 240..285
FT /evidence="ECO:0000250"
FT DISULFID 271..298
FT /evidence="ECO:0000250"
FT DISULFID 303..348
FT /evidence="ECO:0000250"
FT DISULFID 334..361
FT /evidence="ECO:0000250"
FT DISULFID 366..407
FT /evidence="ECO:0000250"
FT DISULFID 393..420
FT /evidence="ECO:0000250"
FT CONFLICT 253
FT /note="C -> Y (in Ref. 2; AAA21541)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="L -> F (in Ref. 2; AAA21541)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="T -> N (in Ref. 2; AAA21541)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="K -> N (in Ref. 2; AAA21541)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="V -> A (in Ref. 2; AAA21541)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="V -> M (in Ref. 2; AAA21541)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..484
FT /note="KFVPSSSSECLQPNGSYQMPSDLI -> NLFLPAAPNAFNPMDPTKCLLT
FT (in Ref. 2; AAA21541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 52567 MW; AFF74FE25C1FD013 CRC64;
MIASQFLSAL PLVLLLLRES GAWSYSASTE TMTFDDASAY CQQRYTHLVA IQNHAEIEYL
NSTFNYSASY YWIGIRKING TWTWIGTKKA LTPEATNWAP GEPNNKQSNE DCVEIYIKRD
KDSGKWNDER CSKKKLALCY TAACTPTSCS GHGECIETIN SSTCQCYPGF RGLQCEQVVE
CDALENPVNG VVTCPQSLPW NTTCAFECKE GFELIGPEHL QCTSSGSWDG KKPTCKAVTC
DTVGHPQNGD VSCNHSSIGE FAYKSTCHFT CAEGFGLQGP AQIECTAQGQ WTQQAPVCKA
VKCPAVSQPK NGLVKFTHSP TGEFTYKSSC AFSCEEGFEL RGSAQLACTS QGQWTQEVPS
CQVVQCSSLE VPREINMSCS GEPVFGAVCT FACPEGWMLN GSVALTCGAT GHWSGMLPTC
EAPAESKIPL AMGLAAGGVS FMTSASFLLW LLKRLRKRAK KFVPSSSSEC LQPNGSYQMP
SDLI
