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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_MOUSE             Reviewed;         372 AA.
P18337;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
28-FEB-2018, entry version 169.
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;
AltName: Full=Lymph node homing receptor {ECO:0000303|PubMed:2646713};
AltName: Full=Lymphocyte antigen 22 {ECO:0000303|PubMed:1693096};
Short=Ly-22 {ECO:0000303|PubMed:1693096};
AltName: Full=Lymphocyte surface MEL-14 antigen;
AltName: CD_antigen=CD62L;
Flags: Precursor;
Name=Sell; Synonyms=Lnhr, Ly-22, Ly22;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Lymph node;
PubMed=2646713; DOI=10.1126/science.2646713;
Siegelman M.H., van de Rijn M., Weissman I.L.;
"Mouse lymph node homing receptor cDNA clone encodes a glycoprotein
revealing tandem interaction domains.";
Science 243:1165-1172(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=1693096; DOI=10.1016/0092-8674(90)90473-R;
Siegelman M.H., Cheng I.C., Weissman I.L., Wakeland E.K.;
"The mouse lymph node homing receptor is identical with the lymphocyte
cell surface marker Ly-22: role of the EGF domain in endothelial
binding.";
Cell 61:611-622(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=2647302; DOI=10.1016/0092-8674(89)90637-5;
Lasky L.A., Singer M.S., Yednock T.A., Dowbenko D., Fennie C.,
Rodriguez H., Nguyen T., Stachel S., Rosen S.D.;
"Cloning of a lymphocyte homing receptor reveals a lectin domain.";
Cell 56:1045-1055(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Hematopoietic;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-360.
PubMed=2004776; DOI=10.1016/0888-7543(91)90252-A;
Dowbenko D.J., Diep A., Taylor B.A., Lusis A.J., Lasky L.A.;
"Characterization of the murine homing receptor gene reveals
correspondence between protein domains and coding exons.";
Genomics 9:270-277(1991).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (PubMed:1693096). Promotes
initial tethering and rolling of leukocytes in endothelia (By
similarity). {ECO:0000250|UniProtKB:P14151,
ECO:0000269|PubMed:1693096}.
-!- 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:1693096,
ECO:0000269|PubMed:2646713}; Single-pass type I membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissue.
{ECO:0000269|PubMed:2646713}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=L-selectin;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_172";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X14772; CAA32880.1; -; mRNA.
EMBL; M36005; AAA39722.1; -; mRNA.
EMBL; M36058; AAA39723.1; -; mRNA.
EMBL; M25324; AAA39431.1; -; mRNA.
EMBL; AH003204; AAA75651.1; -; Genomic_DNA.
EMBL; BC052681; AAH52681.1; -; mRNA.
CCDS; CCDS35753.1; -.
PIR; A32375; A32375.
RefSeq; NP_035476.1; NM_011346.2.
UniGene; Mm.1461; -.
ProteinModelPortal; P18337; -.
SMR; P18337; -.
STRING; 10090.ENSMUSP00000027871; -.
BindingDB; P18337; -.
ChEMBL; CHEMBL3162; -.
iPTMnet; P18337; -.
PhosphoSitePlus; P18337; -.
EPD; P18337; -.
PaxDb; P18337; -.
PeptideAtlas; P18337; -.
PRIDE; P18337; -.
Ensembl; ENSMUST00000027871; ENSMUSP00000027871; ENSMUSG00000026581.
GeneID; 20343; -.
KEGG; mmu:20343; -.
UCSC; uc007dhy.2; mouse.
CTD; 6402; -.
MGI; MGI:98279; Sell.
eggNOG; ENOG410IS3T; Eukaryota.
eggNOG; ENOG410YB82; LUCA.
GeneTree; ENSGT00910000143999; -.
HOVERGEN; HBG052375; -.
InParanoid; P18337; -.
KO; K06495; -.
PhylomeDB; P18337; -.
TreeFam; TF326910; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Sell; mouse.
PRO; PR:P18337; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026581; -.
CleanEx; MM_SELL; -.
ExpressionAtlas; P18337; baseline and differential.
Genevisible; P18337; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:MGI.
GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
GO; GO:0002020; F:protease binding; ISO:MGI.
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:0033198; P:response to ATP; IDA:MGI.
CDD; cd00033; CCP; 2.
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; 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.
1: Evidence at protein 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
PROPEP 29 38
/FTId=PRO_0000017479.
CHAIN 39 372 L-selectin.
/FTId=PRO_0000017480.
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 216 216 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}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 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}.
CONFLICT 32 32 I -> T (in Ref. 5; AAA75651).
{ECO:0000305}.
SEQUENCE 372 AA; 42288 MW; 4433EDF6E4CB2B78 CRC64;
MVFPWRCEGT YWGSRNILKL WVWTLLCCDF LIHHGTHCWT YHYSEKPMNW ENARKFCKQN
YTDLVAIQNK REIEYLENTL PKSPYYYWIG IRKIGKMWTW VGTNKTLTKE AENWGAGEPN
NKKSKEDCVE IYIKRERDSG KWNDDACHKR KAALCYTASC QPGSCNGRGE CVETINNHTC
ICDAGYYGPQ CQYVVQCEPL EAPELGTMDC IHPLGNFSFQ SKCAFNCSEG RELLGTAETQ
CGASGNWSSP EPICQVVQCE PLEAPELGTM DCIHPLGNFS FQSKCAFNCS EGRELLGTAE
TQCGASGNWS SPEPICQETN RSFSKIKEGD YNPLFIPVAV MVTAFSGLAF LIWLARRLKK
GKKSQERMDD PY


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