LYAM1_RAT
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 03-AUG-2022, entry version 141.
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 STRING; 10116.ENSRNOP00000003733; -.
DR GlyGen; P30836; 6 sites.
DR SwissPalm; P30836; -.
DR PaxDb; P30836; -.
DR PRIDE; P30836; -.
DR UCSC; RGD:3655; rat.
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:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; 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: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 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; 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 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; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
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
