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Database: UniProt
Entry: P18337
LinkDB: P18337
Original site: P18337 
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   13-FEB-2019, entry version 175.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   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
RT   cell surface marker Ly-22: role of the EGF domain in endothelial
RT   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
RT   project: 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
RT   correspondence 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
RT   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
CC       adherence of lymphocytes to endothelial cells of high endothelial
CC       venules in peripheral lymph nodes (PubMed:1693096). Promotes
CC       initial tethering and rolling of leukocytes in endothelia (By
CC       similarity). {ECO:0000250|UniProtKB:P14151,
CC       ECO:0000269|PubMed:1693096}.
CC   -!- SUBUNIT: Interaction with SELPLG/PSGL1 and PODXL2 is required for
CC       promoting recruitment and rolling of leukocytes. This interaction
CC       is dependent on the sialyl Lewis X glycan modification of SELPLG
CC       and PODXL2, and tyrosine sulfation modifications of SELPLG.
CC       Sulfation on 'Tyr-51' of SELPLG is important for L-selectin
CC       binding. {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";
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   UniGene; Mm.1461; -.
DR   ProteinModelPortal; P18337; -.
DR   SMR; P18337; -.
DR   STRING; 10090.ENSMUSP00000027871; -.
DR   BindingDB; P18337; -.
DR   ChEMBL; CHEMBL3162; -.
DR   iPTMnet; P18337; -.
DR   PhosphoSitePlus; P18337; -.
DR   EPD; P18337; -.
DR   PaxDb; P18337; -.
DR   PeptideAtlas; P18337; -.
DR   PRIDE; P18337; -.
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   eggNOG; ENOG410IS3T; Eukaryota.
DR   eggNOG; ENOG410YB82; LUCA.
DR   GeneTree; ENSGT00940000162076; -.
DR   HOVERGEN; HBG052375; -.
DR   InParanoid; P18337; -.
DR   KO; K06495; -.
DR   OMA; DLGTMDC; -.
DR   OrthoDB; 445079at2759; -.
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   ChiTaRS; Sell; mouse.
DR   PRO; PR:P18337; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026581; Expressed in 62 organ(s), highest expression level in lymph node.
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; IPR013032; EGF-like_CS.
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; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Signal; Sushi;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28
FT   PROPEP       29     38
FT                                /FTId=PRO_0000017479.
FT   CHAIN        39    372       L-selectin.
FT                                /FTId=PRO_0000017480.
FT   TOPO_DOM     39    332       Extracellular. {ECO:0000255}.
FT   TRANSMEM    333    355       Helical. {ECO:0000255}.
FT   TOPO_DOM    356    372       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       55    155       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      156    192       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      195    256       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      257    318       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   METAL       118    118       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   METAL       120    120       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   METAL       126    126       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   METAL       143    143       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   METAL       144    144       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   CARBOHYD     60     60       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    177    177       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    216    216       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    278    278       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    308    308       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    320    320       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57    155       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    128    160       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    128    147       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    160    171       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    165    180       {ECO:0000250}.
FT   DISULFID    182    191       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    197    241       {ECO:0000250}.
FT   DISULFID    227    254       {ECO:0000250}.
FT   DISULFID    259    303       {ECO:0000250}.
FT   DISULFID    289    316       {ECO:0000250}.
FT   CONFLICT     32     32       I -> T (in Ref. 5; AAA75651).
FT                                {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
//
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