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   27-MAR-2024, entry version 202.
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   GlyCosmos; P18337; 10 sites, No reported glycans.
DR   GlyGen; P18337; 10 sites.
DR   iPTMnet; P18337; -.
DR   PhosphoSitePlus; P18337; -.
DR   CPTAC; non-CPTAC-3589; -.
DR   EPD; P18337; -.
DR   PaxDb; 10090-ENSMUSP00000027871; -.
DR   PeptideAtlas; P18337; -.
DR   ProteomicsDB; 290201; -.
DR   Antibodypedia; 3683; 1813 antibodies from 50 providers.
DR   DNASU; 20343; -.
DR   Ensembl; ENSMUST00000027871.13; ENSMUSP00000027871.8; ENSMUSG00000026581.15.
DR   GeneID; 20343; -.
DR   KEGG; mmu:20343; -.
DR   UCSC; uc007dhy.2; mouse.
DR   AGR; MGI:98279; -.
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; EPSCQVI; -.
DR   OrthoDB; 3035244at2759; -.
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 80 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 cell types or tissues.
DR   ExpressionAtlas; P18337; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0033691; F:sialic acid binding; IBA:GO_Central.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
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   GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00054; EGF_CA; 1.
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; 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   PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR19325:SF543; L-SELECTIN; 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.
DR   Genevisible; P18337; MM.
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
//