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L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (Lymphocyte antigen 22) (Ly-22) (Lymphocyte surface MEL-14 antigen) (CD antigen CD62L)

 LYAM1_RAT               Reviewed;         372 AA.
P30836;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
31-JAN-2018, entry version 129.
RecName: Full=L-selectin;
AltName: Full=CD62 antigen-like family member L;
AltName: Full=Leukocyte adhesion molecule 1;
Short=LAM-1;
AltName: Full=Leukocyte-endothelial cell adhesion molecule 1;
Short=LECAM1 {ECO:0000303|PubMed:1378303};
AltName: Full=Lymph node homing receptor;
AltName: Full=Lymphocyte antigen 22;
Short=Ly-22;
AltName: Full=Lymphocyte surface MEL-14 antigen;
AltName: CD_antigen=CD62L;
Flags: Precursor;
Name=Sell; Synonyms=Lnhr, Ly-22;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=1378303; DOI=10.1016/0167-4781(92)90033-V;
Watanabe T., Song Y., Hirayama Y., Tamatani T., Kuida K., Miyasaka M.;
"Sequence and expression of a rat cDNA for LECAM-1.";
Biochim. Biophys. Acta 1131:321-324(1992).
-!- FUNCTION: Calcium-dependent lectin that mediates cell adhesion by
binding to glycoproteins on neighboring cells. Mediates the
adherence of lymphocytes to endothelial cells of high endothelial
venules in peripheral lymph nodes. Promotes initial tethering and
rolling of leukocytes in endothelia.
{ECO:0000250|UniProtKB:P14151}.
-!- SUBUNIT: Interaction with SELPLG/PSGL1 and PODXL2 is required for
promoting recruitment and rolling of leukocytes. This interaction
is dependent on the sialyl Lewis X glycan modification of SELPLG
and PODXL2, and tyrosine sulfation modifications of SELPLG.
Sulfation on 'Tyr-51' of SELPLG is important for L-selectin
binding. {ECO:0000250|UniProtKB:P14151}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1378303};
Single-pass type I membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in peripheral blood mononuclear
cells (PBMC), spleen and thymus. {ECO:0000269|PubMed:1378303}.
-!- INDUCTION: Down-regulated by mitogen stimulation of PBMC and
spleen T-cells. {ECO:0000269|PubMed:1378303}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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EMBL; D10831; BAA01613.1; -; mRNA.
PIR; S23936; S23936.
UniGene; Rn.10461; -.
ProteinModelPortal; P30836; -.
SMR; P30836; -.
STRING; 10116.ENSRNOP00000003733; -.
SwissPalm; P30836; -.
PaxDb; P30836; -.
PRIDE; P30836; -.
UCSC; RGD:3655; rat.
RGD; 3655; Sell.
eggNOG; ENOG410IS3T; Eukaryota.
eggNOG; ENOG410YB82; LUCA.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; P30836; -.
PhylomeDB; P30836; -.
PRO; PR:P30836; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
GO; GO:0051861; F:glycolipid binding; IDA:RGD.
GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
GO; GO:0002020; F:protease binding; ISO:RGD.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:RGD.
GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
GO; GO:0033198; P:response to ATP; ISO:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0070543; P:response to linoleic acid; IEP:RGD.
GO; GO:0034201; P:response to oleic acid; IEP:RGD.
CDD; cd00033; CCP; 1.
CDD; cd03592; CLECT_selectins_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR016348; L-selectin.
InterPro; IPR033991; Selectin_CTLD.
InterPro; IPR002396; Selectin_superfamily.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 2.
PIRSF; PIRSF002421; L-selectin; 1.
PRINTS; PR00343; SELECTIN.
SMART; SM00032; CCP; 2.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57535; SSF57535; 2.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50923; SUSHI; 2.
2: Evidence at transcript level;
Calcium; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane;
Metal-binding; Reference proteome; Repeat; Signal; Sushi;
Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000250}.
PROPEP 29 38 {ECO:0000250}.
/FTId=PRO_0000017487.
CHAIN 39 372 L-selectin.
/FTId=PRO_0000017488.
TOPO_DOM 39 332 Extracellular. {ECO:0000255}.
TRANSMEM 333 355 Helical. {ECO:0000255}.
TOPO_DOM 356 372 Cytoplasmic. {ECO:0000255}.
DOMAIN 55 155 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 156 192 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 195 256 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 257 318 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
METAL 118 118 Calcium. {ECO:0000250|UniProtKB:P14151}.
METAL 120 120 Calcium. {ECO:0000250|UniProtKB:P14151}.
METAL 126 126 Calcium. {ECO:0000250|UniProtKB:P14151}.
METAL 143 143 Calcium. {ECO:0000250|UniProtKB:P14151}.
METAL 144 144 Calcium. {ECO:0000250|UniProtKB:P14151}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 155 {ECO:0000250|UniProtKB:P14151}.
DISULFID 128 160 {ECO:0000250|UniProtKB:P14151}.
DISULFID 128 147 {ECO:0000250|UniProtKB:P14151}.
DISULFID 160 171 {ECO:0000250|UniProtKB:P14151}.
DISULFID 165 180 {ECO:0000250}.
DISULFID 182 191 {ECO:0000250|UniProtKB:P14151}.
DISULFID 197 241 {ECO:0000250}.
DISULFID 227 254 {ECO:0000250}.
DISULFID 259 303 {ECO:0000250}.
DISULFID 289 316 {ECO:0000250}.
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


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