LYAM1_MOUSE
ID LYAM1_MOUSE Reviewed; 372 AA.
AC P18337;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 193.
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;
DE AltName: Full=Lymph node homing receptor {ECO:0000303|PubMed:2646713};
DE AltName: Full=Lymphocyte antigen 22 {ECO:0000303|PubMed:1693096};
DE Short=Ly-22 {ECO:0000303|PubMed:1693096};
DE AltName: Full=Lymphocyte surface MEL-14 antigen;
DE AltName: CD_antigen=CD62L;
DE Flags: Precursor;
GN Name=Sell; Synonyms=Lnhr, Ly-22, Ly22;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Lymph node;
RX PubMed=2646713; DOI=10.1126/science.2646713;
RA Siegelman M.H., van de Rijn M., Weissman I.L.;
RT "Mouse lymph node homing receptor cDNA clone encodes a glycoprotein
RT revealing tandem interaction domains.";
RL Science 243:1165-1172(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=1693096; DOI=10.1016/0092-8674(90)90473-r;
RA Siegelman M.H., Cheng I.C., Weissman I.L., Wakeland E.K.;
RT "The mouse lymph node homing receptor is identical with the lymphocyte cell
RT surface marker Ly-22: role of the EGF domain in endothelial binding.";
RL Cell 61:611-622(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=2647302; DOI=10.1016/0092-8674(89)90637-5;
RA Lasky L.A., Singer M.S., Yednock T.A., Dowbenko D., Fennie C.,
RA Rodriguez H., Nguyen T., Stachel S., Rosen S.D.;
RT "Cloning of a lymphocyte homing receptor reveals a lectin domain.";
RL Cell 56:1045-1055(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hematopoietic;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-360.
RX PubMed=2004776; DOI=10.1016/0888-7543(91)90252-a;
RA Dowbenko D.J., Diep A., Taylor B.A., Lusis A.J., Lasky L.A.;
RT "Characterization of the murine homing receptor gene reveals correspondence
RT between protein domains and coding exons.";
RL Genomics 9:270-277(1991).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (PubMed:1693096). Promotes initial tethering and
CC rolling of leukocytes in endothelia (By similarity).
CC {ECO:0000250|UniProtKB:P14151, ECO:0000269|PubMed:1693096}.
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:1693096,
CC ECO:0000269|PubMed:2646713}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissue.
CC {ECO:0000269|PubMed:2646713}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=L-selectin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_172";
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DR EMBL; X14772; CAA32880.1; -; mRNA.
DR EMBL; M36005; AAA39722.1; -; mRNA.
DR EMBL; M36058; AAA39723.1; -; mRNA.
DR EMBL; M25324; AAA39431.1; -; mRNA.
DR EMBL; AH003204; AAA75651.1; -; Genomic_DNA.
DR EMBL; BC052681; AAH52681.1; -; mRNA.
DR CCDS; CCDS35753.1; -.
DR PIR; A32375; A32375.
DR RefSeq; NP_035476.1; NM_011346.2.
DR AlphaFoldDB; P18337; -.
DR SMR; P18337; -.
DR BioGRID; 203158; 2.
DR STRING; 10090.ENSMUSP00000027871; -.
DR BindingDB; P18337; -.
DR ChEMBL; CHEMBL3162; -.
DR GlyGen; P18337; 10 sites.
DR iPTMnet; P18337; -.
DR PhosphoSitePlus; P18337; -.
DR CPTAC; non-CPTAC-3589; -.
DR EPD; P18337; -.
DR PaxDb; P18337; -.
DR PeptideAtlas; P18337; -.
DR PRIDE; P18337; -.
DR ProteomicsDB; 290201; -.
DR Antibodypedia; 3683; 1543 antibodies from 49 providers.
DR DNASU; 20343; -.
DR Ensembl; ENSMUST00000027871; ENSMUSP00000027871; ENSMUSG00000026581.
DR GeneID; 20343; -.
DR KEGG; mmu:20343; -.
DR UCSC; uc007dhy.2; mouse.
DR CTD; 6402; -.
DR MGI; MGI:98279; Sell.
DR VEuPathDB; HostDB:ENSMUSG00000026581; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162076; -.
DR HOGENOM; CLU_065067_0_0_1; -.
DR InParanoid; P18337; -.
DR OMA; WVWTVLC; -.
DR PhylomeDB; P18337; -.
DR TreeFam; TF326910; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 20343; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Sell; mouse.
DR PRO; PR:P18337; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P18337; protein.
DR Bgee; ENSMUSG00000026581; Expressed in granulocyte and 51 other tissues.
DR ExpressionAtlas; P18337; baseline and differential.
DR Genevisible; P18337; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:MGI.
DR GO; GO:0051861; F:glycolipid binding; ISO:MGI.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0033198; P:response to ATP; IDA:MGI.
DR CDD; cd00033; CCP; 2.
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; 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 1: Evidence at protein 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 PROPEP 29..38
FT /id="PRO_0000017479"
FT CHAIN 39..372
FT /note="L-selectin"
FT /id="PRO_0000017480"
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 216
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 CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
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"
FT CONFLICT 32
FT /note="I -> T (in Ref. 5; AAA75651)"
FT /evidence="ECO:0000305"
SQ 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
