ID   LYAM1_RAT               Reviewed;         372 AA.
AC   P30836;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   04-NOV-2026, entry version 154.
DE   RecName: Full=L-selectin;
DE   AltName: Full=CD62 antigen-like family member L;
DE   AltName: Full=Leukocyte adhesion molecule 1;
DE            Short=LAM-1;
DE   AltName: Full=Leukocyte-endothelial cell adhesion molecule 1;
DE            Short=LECAM1 {ECO:0000303|PubMed:1378303};
DE   AltName: Full=Lymph node homing receptor;
DE   AltName: Full=Lymphocyte antigen 22;
DE            Short=Ly-22;
DE   AltName: Full=Lymphocyte surface MEL-14 antigen;
DE   AltName: CD_antigen=CD62L;
DE   Flags: Precursor;
GN   Name=Sell; Synonyms=Lnhr, Ly-22;
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], SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=1378303; DOI=10.1016/0167-4781(92)90033-v;
RA   Watanabe T., Song Y., Hirayama Y., Tamatani T., Kuida K., Miyasaka M.;
RT   "Sequence and expression of a rat cDNA for LECAM-1.";
RL   Biochim. Biophys. Acta 1131:321-324(1992).
CC   -!- FUNCTION: Calcium-dependent lectin that mediates cell adhesion by
CC       binding to glycoproteins on neighboring cells. Mediates the adherence
CC       of lymphocytes to endothelial cells of high endothelial venules in
CC       peripheral lymph nodes. Promotes initial tethering and rolling of
CC       leukocytes in endothelia. {ECO:0000250|UniProtKB:P14151}.
CC   -!- SUBUNIT: Interaction with SELPLG/PSGL1 and PODXL2 is required for
CC       promoting recruitment and rolling of leukocytes. This interaction is
CC       dependent on the sialyl Lewis X glycan modification of SELPLG and
CC       PODXL2, and tyrosine sulfation modifications of SELPLG. Sulfation on
CC       'Tyr-51' of SELPLG is important for L-selectin binding.
CC       {ECO:0000250|UniProtKB:P14151}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1378303};
CC       Single-pass type I membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in peripheral blood mononuclear cells
CC       (PBMC), spleen and thymus. {ECO:0000269|PubMed:1378303}.
CC   -!- INDUCTION: Down-regulated by mitogen stimulation of PBMC and spleen T-
CC       cells. {ECO:0000269|PubMed:1378303}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
CC   -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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DR   EMBL; D10831; BAA01613.1; -; mRNA.
DR   PIR; S23936; S23936.
DR   AlphaFoldDB; P30836; -.
DR   BMRB; P30836; -.
DR   SMR; P30836; -.
DR   FunCoup; P30836; 139.
DR   STRING; 10116.ENSRNOP00000003733; -.
DR   GlyCosmos; P30836; 6 sites, No reported glycans.
DR   GlyGen; P30836; 6 sites.
DR   PhosphoSitePlus; P30836; -.
DR   SwissPalm; P30836; -.
DR   PaxDb; 10116-ENSRNOP00000003733; -.
DR   UCSC; RGD:3655; rat.
DR   AGR; RGD:3655; -.
DR   RGD; 3655; Sell.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; P30836; -.
DR   PhylomeDB; P30836; -.
DR   Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:P30836; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; EXP:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR   GO; GO:0051861; F:glycolipid binding; IDA:RGD.
DR   GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR   GO; GO:0002020; F:protease binding; ISO:RGD.
DR   GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0098759; P:cellular response to interleukin-8; IEP:RGD.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; IDA:RGD.
DR   GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR   GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; IMP:RGD.
DR   GO; GO:1904999; P:positive regulation of leukocyte adhesion to arterial endothelial cell; IMP:RGD.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:RGD.
DR   GO; GO:0070960; P:positive regulation of neutrophil mediated cytotoxicity; IMP:RGD.
DR   GO; GO:0043117; P:positive regulation of vascular permeability; IMP:RGD.
DR   GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
DR   GO; GO:0033198; P:response to ATP; ISO:RGD.
DR   GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0070543; P:response to linoleic acid; IEP:RGD.
DR   GO; GO:0034201; P:response to oleic acid; IEP:RGD.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd03592; CLECT_selectins_like; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   FunFam; 3.10.100.10:FF:000007; L-selectin; 1.
DR   FunFam; 2.10.70.10:FF:000001; Selectin P; 2.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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; IPR050350; Compl-Cell_Adhes-Reg.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR016348; L-selectin.
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   PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR19325:SF543; L-SELECTIN; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   PIRSF; PIRSF002421; L-selectin; 1.
DR   PRINTS; PR00343; SELECTIN.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
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; 2.
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..28
FT                   /evidence="ECO:0000250"
FT   PROPEP          29..38
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000017487"
FT   CHAIN           39..372
FT                   /note="L-selectin"
FT                   /id="PRO_0000017488"
FT   TOPO_DOM        39..332
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        356..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          55..155
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DOMAIN          156..192
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          195..256
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          257..318
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   BINDING         118
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   BINDING         126
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   BINDING         144
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..155
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   DISULFID        128..160
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   DISULFID        128..147
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   DISULFID        160..171
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   DISULFID        165..180
FT                   /evidence="ECO:0000250"
FT   DISULFID        182..191
FT                   /evidence="ECO:0000250|UniProtKB:P14151"
FT   DISULFID        197..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        227..254
FT                   /evidence="ECO:0000250"
FT   DISULFID        259..303
FT                   /evidence="ECO:0000250"
FT   DISULFID        289..316
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  42441 MW;  3B88AE0F1E4D191A CRC64;
     MVFPWRCQSA QRGSWSFLKL WIRTLLCCDL LPHHGTHCWT YHYSERSMNW ENARKFCKHN
     YTDLVAIQNK REIEYLEKTL PKNPTYYWIG IRKIGKTWTW VGTNKTLTKE AENWGTGEPN
     NKKSKEDCVE IYIKRERDSG KWNDDACHKR KAALCYTASC QPESCNRHGE CVETINNNTC
     ICDPGYYGPQ CQYVIQCEPL KAPELGTMNC IHPLGDFSFQ SQCAFNCSEG SELLGNAKTE
     CGASGNWTYL EPICQVIQCM PLAAPDLGTM ECSHPLANFS FTSACTFTCS EETDLIGERK
     TVCRSSGSWS SPSPICQKTK RSFSKIKEGD YNPLFIPVAV MVTAFSGLAF IIWLARRLKK
     GKKSQERMDD PY
//