ID LYAM1_HUMAN Reviewed; 372 AA. AC P14151; A0A024R8Z0; B2R6Q8; P15023; Q9UJ43; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 02-SEP-2026, entry version 250. 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 {ECO:0000303|PubMed:2473156}; DE AltName: Full=Leukocyte surface antigen Leu-8; DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 1; DE Short=LECAM1; DE AltName: Full=Lymph node homing receptor {ECO:0000303|PubMed:2663882}; DE AltName: Full=TQ1 {ECO:0000303|PubMed:1692315, ECO:0000303|PubMed:2509939}; DE AltName: Full=gp90-MEL; DE AltName: CD_antigen=CD62L; DE Flags: Precursor; GN Name=SELL; Synonyms=LNHR, LYAM1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-193. RC TISSUE=Lymphocyte; RX PubMed=2664786; DOI=10.1073/pnas.86.14.5562; RA Siegelman M.H., Weissman I.L.; RT "Human homologue of mouse lymph node homing receptor: evolutionary RT conservation at tandem cell interaction domains."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5562-5566(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Tonsil; RX PubMed=2473156; DOI=10.1084/jem.170.1.123; RA Tedder T.F., Isaacs C.M., Ernst T.J., Demetri G.D., Adler D.A., RA Disteche C.M.; RT "Isolation and chromosomal localization of cDNAs encoding a novel human RT lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte RT homing receptor and other human adhesion proteins."; RL J. Exp. Med. 170:123-133(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND VARIANT RP SER-213. RC TISSUE=Lymphocyte; RX PubMed=2509939; DOI=10.1038/342078a0; RA Camerini D., James S.P., Stamenkovic I., Seed B.; RT "Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing RT receptor."; RL Nature 342:78-82(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, RP GLYCOSYLATION, AND VARIANT LEU-193. RC TISSUE=Lymphocyte; RX PubMed=2663882; DOI=10.1083/jcb.109.1.421; RA Bowen B.R., Nguyen T., Lasky L.A.; RT "Characterization of a human homologue of the murine peripheral lymph node RT homing receptor."; RL J. Cell Biol. 109:421-427(1989). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1692315; DOI=10.1016/s0021-9258(19)38994-x; RA Ord D.C., Ernst T.J., Zhou L.J., Rambaldi A., Spertini O., Griffin J., RA Tedder T.F.; RT "Structure of the gene encoding the human leukocyte adhesion molecule-1 RT (TQ1, Leu-8) of lymphocytes and neutrophils."; RL J. Biol. Chem. 265:7760-7767(1990). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Hematopoietic; RA Fieger C.B.; RL Thesis (1998), Freie Universtiaet Berlin, Germany. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-193; GLN-201; SER-213 RP AND ASP-369. RG SeattleSNPs variation discovery resource; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [12] RP INTERACTION WITH SELPLG, AND FUNCTION. RX PubMed=12403782; DOI=10.1074/jbc.m204360200; RA Bernimoulin M.P., Zeng X.-L., Abbal C., Giraud S., Martinez M., RA Michielin O., Schapira M., Spertini O.; RT "Molecular basis of leukocyte rolling on PSGL-1. Predominant role of core-2 RT O-glycans and of tyrosine sulfate residue 51."; RL J. Biol. Chem. 278:37-47(2003). RN [13] RP INTERACTION WITH SELPLG. RX PubMed=12736247; DOI=10.1074/jbc.m303551200; RA Leppaenen A., Yago T., Otto V.I., McEver R.P., Cummings R.D.; RT "Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require RT tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin."; RL J. Biol. Chem. 278:26391-26400(2003). RN [14] RP INTERACTION WITH PODXL2. RX PubMed=18606703; DOI=10.4049/jimmunol.181.2.1480; RA Kerr S.C., Fieger C.B., Snapp K.R., Rosen S.D.; RT "Endoglycan, a member of the CD34 family of sialomucins, is a ligand for RT the vascular selectins."; RL J. Immunol. 181:1480-1490(2008). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60 AND ASN-104. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [16] RP 3D-STRUCTURE MODELING. RX PubMed=7488174; DOI=10.1006/bbrc.1995.2722; RA Bajorath J., Aruffo A.; RT "A template for generation and comparison of three-dimensional selectin RT models."; RL Biochem. Biophys. Res. Commun. 216:1018-1023(1995). RN [17] {ECO:0007744|PDB:5VC1} RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 39-195 IN COMPLEX WITH CALCIUM RP IONS, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-60; ASN-104 AND RP ASN-177, AND MUTAGENESIS OF ASN-60; ASN-104 AND ASN-177. RX PubMed=28489325; DOI=10.1002/cbic.201700220; RA Wedepohl S., Dernedde J., Vahedi-Faridi A., Tauber R., Saenger W., RA Bulut H.; RT "Reducing Macro- and Microheterogeneity of N-Glycans Enables the Crystal RT Structure of the Lectin and EGF-Like Domains of Human L-Selectin To Be RT Solved at 1.9 A Resolution."; RL ChemBioChem 18:1338-1345(2017). RN [18] {ECO:0007744|PDB:3CFW} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 39-194 IN COMPLEX WITH CALCIUM RP IONS, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-60 AND ASN-104, RP MUTAGENESIS OF GLU-126, AND DISULFIDE BONDS. RX PubMed=28011641; DOI=10.1074/jbc.m116.767186; RA Mehta-D'souza P., Klopocki A.G., Oganesyan V., Terzyan S., Mather T., RA Li Z., Panicker S.R., Zhu C., McEver R.P.; RT "Glycan Bound to the Selectin Low Affinity State Engages Glu-88 to RT Stabilize the High Affinity State under Force."; RL J. Biol. Chem. 292:2510-2518(2017). CC -!- FUNCTION: Calcium-dependent lectin that mediates cell adhesion by CC binding to glycoproteins on neighboring cells (PubMed:12403782, CC PubMed:28011641, PubMed:28489325). Mediates the adherence of CC lymphocytes to endothelial cells of high endothelial venules in CC peripheral lymph nodes. Promotes initial tethering and rolling of CC leukocytes in endothelia (PubMed:12403782, PubMed:28011641). CC {ECO:0000269|PubMed:12403782, ECO:0000269|PubMed:28011641, CC ECO:0000305|PubMed:28489325}. 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:0000269|PubMed:12403782, ECO:0000269|PubMed:12736247, CC ECO:0000269|PubMed:18606703}. CC -!- INTERACTION: CC P14151-2; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-17865914, EBI-8644112; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2509939, CC ECO:0000269|PubMed:2663882, ECO:0000269|PubMed:28011641}; Single-pass CC type I membrane protein {ECO:0000305|PubMed:2663882}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Comment=The start of isoform 1 corresponds to the N-terminus of CC mammalian orthologs. The start codon for isoform 2 is in the same CC exon and reading frame as that for isoform 1, suggesting alternative CC initiation. {ECO:0000305}; CC Name=1; CC IsoId=P14151-1; Sequence=Displayed; CC Name=2; CC IsoId=P14151-2; Sequence=VSP_042650; CC -!- TISSUE SPECIFICITY: Expressed in B-cell lines and T-lymphocytes. CC {ECO:0000269|PubMed:2473156}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:2663882, CC ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325}. 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_hum_Ctlect_234"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M25280; AAC63053.1; -; mRNA. DR EMBL; X16150; CAA34275.1; -; mRNA. DR EMBL; X17519; CAB43536.1; -; mRNA. DR EMBL; X17519; CAB43537.1; -; mRNA. DR EMBL; X16070; CAA34203.1; -; mRNA. DR EMBL; M32414; AAB60700.1; -; Genomic_DNA. DR EMBL; M32406; AAB60700.1; JOINED; Genomic_DNA. DR EMBL; M32407; AAB60700.1; JOINED; Genomic_DNA. DR EMBL; M32408; AAB60700.1; JOINED; Genomic_DNA. DR EMBL; M32409; AAB60700.1; JOINED; Genomic_DNA. DR EMBL; M32410; AAB60700.1; JOINED; Genomic_DNA. DR EMBL; M32411; AAB60700.1; JOINED; Genomic_DNA. DR EMBL; M32412; AAB60700.1; JOINED; Genomic_DNA. DR EMBL; M32413; AAB60700.1; JOINED; Genomic_DNA. DR EMBL; AJ246000; CAB55488.1; -; mRNA. DR EMBL; AK312673; BAG35555.1; -; mRNA. DR EMBL; AY233976; AAO48272.1; -; Genomic_DNA. DR EMBL; AL021940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW90856.1; -; Genomic_DNA. DR EMBL; CH471067; EAW90858.1; -; Genomic_DNA. DR CCDS; CCDS53427.2; -. [P14151-1] DR RefSeq; NP_000646.3; NM_000655.5. [P14151-1] DR PDB; 2LGF; NMR; -; B=349-363. DR PDB; 3CFW; X-ray; 2.20 A; A=39-194. DR PDB; 5VC1; X-ray; 1.94 A; A=39-195. DR AlphaFoldDB; P14151; -. DR BMRB; P14151; -. DR MDRepo; P14151; -. DR SMR; P14151; -. DR BioGRID; 112302; 16. DR FunCoup; P14151; 274. DR IntAct; P14151; 4. DR NDEx; IQUERY-CP-SELL; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000498227; -. DR BindingDB; P14151; -. DR ChEMBL; CHEMBL3161; -. DR DrugBank; DB16101; Baicalein. DR DrugBank; DB12778; Rivipansel. DR UniLectin; P14151; -. DR GlyConnect; P14151; 27 N-Linked glycans (2 sites). DR GlyCosmos; P14151; 6 sites, 46 glycans. DR GlyGen; P14151; 7 sites, 52 N-linked glycans (2 sites). DR iPTMnet; P14151; -. DR PhosphoSitePlus; P14151; -. DR BioMuta; SELL; -. DR DMDM; 126178; -. DR MassIVE; P14151; -. DR PaxDb; 9606-ENSP00000498227; -. DR PeptideAtlas; P14151; -. DR ProteomicsDB; 53028; -. [P14151-1] DR ProteomicsDB; 53029; -. [P14151-2] DR ABCD; P14151; 4 sequenced antibodies. DR Antibodypedia; 3683; 1698 antibodies from 51 providers. DR DNASU; 6402; -. DR Ensembl; ENST00000236147.6; ENSP00000236147.5; ENSG00000188404.11. [P14151-1] DR Ensembl; ENST00000650983.1; ENSP00000498227.1; ENSG00000188404.11. [P14151-2] DR Ensembl; ENST00000878074.1; ENSP00000548133.1; ENSG00000188404.11. [P14151-1] DR Ensembl; ENST00000878075.1; ENSP00000548134.1; ENSG00000188404.11. [P14151-1] DR GeneID; 6402; -. DR KEGG; hsa:6402; -. DR MANE-Select; ENST00000236147.6; ENSP00000236147.5; NM_000655.5; NP_000646.3. DR UCSC; uc001ggk.4; human. [P14151-1] DR AGR; HGNC:10720; -. DR ClinPGx; PA35642; -. DR CTD; 6402; -. DR DisGeNET; 6402; -. DR GeneCards; SELL; -. DR HGNC; HGNC:10720; SELL. DR HPA; ENSG00000188404; Group enriched (bone marrow, lymphoid tissue). DR MIM; 153240; gene. DR OpenTargets; ENSG00000188404; -. DR VEuPathDB; HostDB:ENSG00000188404; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00940000162076; -. DR HOGENOM; CLU_065067_0_0_1; -. DR InParanoid; P14151; -. DR OrthoDB; 406096at2759; -. DR PAN-GO; P14151; 8 GO annotations based on evolutionary models. DR PhylomeDB; P14151; -. DR PathwayCommons; P14151; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P14151; -. DR SIGNOR; P14151; -. DR Agora; ENSG00000188404; -. DR BioGRID-ORCS; 6402; 4 hits in 1143 CRISPR screens. DR ChiTaRS; SELL; human. DR EvolutionaryTrace; P14151; -. DR GeneWiki; L-selectin; -. DR GenomeRNAi; 6402; -. DR Pharos; P14151; Tchem. DR PRO; PR:P14151; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P14151; protein. DR Bgee; ENSG00000188404; Expressed in blood and 144 other cell types or tissues. DR ExpressionAtlas; P14151; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc. DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl. DR GO; GO:0043208; F:glycosphingolipid binding; TAS:BHF-UCL. DR GO; GO:0008201; F:heparin binding; TAS:BHF-UCL. DR GO; GO:0070492; F:oligosaccharide binding; IMP:UniProtKB. DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL. DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007157; P:heterophilic cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007159; P:leukocyte cell-cell adhesion; TAS:BHF-UCL. DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB. DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central. DR CDD; cd00033; CCP; 2. DR CDD; cd03592; CLECT_selectins_like; 1. DR CDD; cd00054; EGF_CA; 1. DR FunFam; 3.10.100.10:FF:000007; L-selectin; 1. DR FunFam; 2.10.25.10:FF:000176; Selectin P; 1. DR FunFam; 2.10.70.10:FF:000001; Selectin P; 2. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2. DR Gene3D; 2.10.25.10; Laminin; 1. 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; IPR050350; Compl-Cell_Adhes-Reg. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR000742; EGF. DR InterPro; IPR016348; L-selectin. DR InterPro; IPR033991; Selectin_CTLD. 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; PF00008; EGF; 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 SMART; SM00181; EGF; 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 PDBsum; 2LGF; -. DR PDBsum; 3CFW; -. DR PDBsum; 5VC1; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Calcium; Cell adhesion; KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Lectin; KW Membrane; Metal-binding; Proteomics identification; Reference proteome; KW Repeat; Signal; Sushi; Transmembrane; Transmembrane helix. FT SIGNAL 1..28 FT PROPEP 29..38 FT /id="PRO_0000017475" FT CHAIN 39..372 FT /note="L-selectin" FT /id="PRO_0000017476" 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:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" FT BINDING 120 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" FT BINDING 126 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" FT BINDING 143 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" FT BINDING 144 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" FT CARBOHYD 60 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:28011641, FT ECO:0000305|PubMed:28489325, ECO:0007744|PDB:3CFW" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973, FT ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325, FT ECO:0007744|PDB:3CFW" FT CARBOHYD 177 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305|PubMed:28489325" FT CARBOHYD 232 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 271 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 57..155 FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" FT DISULFID 128..147 FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" FT DISULFID 160..171 FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" FT DISULFID 165..180 FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW" FT DISULFID 182..191 FT /evidence="ECO:0000269|PubMed:28011641, FT ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, FT ECO:0007744|PDB:5VC1" 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 VAR_SEQ 1 FT /note="M -> MGCRRTREGPSKAM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2509939, ECO:0000303|Ref.6" FT /id="VSP_042650" FT VARIANT 193 FT /note="F -> L (in dbSNP:rs1131498)" FT /evidence="ECO:0000269|PubMed:2663882, FT ECO:0000269|PubMed:2664786, ECO:0000269|Ref.8" FT /id="VAR_019134" FT VARIANT 201 FT /note="E -> Q (in dbSNP:rs2229568)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_019135" FT VARIANT 213 FT /note="P -> S (in dbSNP:rs2229569)" FT /evidence="ECO:0000269|PubMed:2509939, ECO:0000269|Ref.8" FT /id="VAR_019136" FT VARIANT 369 FT /note="N -> D (in dbSNP:rs4987382)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_019137" FT MUTAGEN 60 FT /note="N->Q: Loss of one glycosylation site." FT /evidence="ECO:0000269|PubMed:28489325" FT MUTAGEN 104 FT /note="N->Q: Loss of one glycosylation site." FT /evidence="ECO:0000269|PubMed:28489325" FT MUTAGEN 126 FT /note="E->D: Impairs interaction with cognate FT oligosaccharide. Abolishes cell rolling on glycan ligands." FT /evidence="ECO:0000269|PubMed:28011641" FT MUTAGEN 177 FT /note="N->Q: Loss of one glycosylation site." FT /evidence="ECO:0000269|PubMed:28489325" FT CONFLICT 37 FT /note="D -> Y (in Ref. 4; CAA34203)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="Y -> H (in Ref. 4; CAA34203)" FT /evidence="ECO:0000305" FT CONFLICT 214 FT /note="L -> F (in Ref. 4; CAA34203)" FT /evidence="ECO:0000305" FT CONFLICT 218..220 FT /note="SFS -> NFN (in Ref. 2; CAA34275)" FT /evidence="ECO:0000305" FT CONFLICT 242 FT /note="G -> E (in Ref. 2; CAA34275)" FT /evidence="ECO:0000305" FT STRAND 40..48 FT /evidence="ECO:0007829|PDB:5VC1" FT HELIX 50..60 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:5VC1" FT HELIX 70..79 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:5VC1" FT TURN 101..104 FT /evidence="ECO:0007829|PDB:5VC1" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:5VC1" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 151..157 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 167..174 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:5VC1" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:3CFW" FT HELIX 350..362 FT /evidence="ECO:0007829|PDB:2LGF" SQ SEQUENCE 372 AA; 42187 MW; 6EA9918ECA2D3643 CRC64; MIFPWKCQST QRDLWNIFKL WGWTMLCCDF LAHHGTDCWT YHYSEKPMNW QRARRFCRDN YTDLVAIQNK AEIEYLEKTL PFSRSYYWIG IRKIGGIWTW VGTNKSLTEE AENWGDGEPN NKKNKEDCVE IYIKRNKDAG KWNDDACHKL KAALCYTASC QPWSCSGHGE CVEIINNYTC NCDVGYYGPQ CQFVIQCEPL EAPELGTMDC THPLGNFSFS SQCAFSCSEG TNLTGIEETT CGPFGNWSSP EPTCQVIQCE PLSAPDLGIM NCSHPLASFS FTSACTFICS EGTELIGKKK TICESSGIWS NPSPICQKLD KSFSMIKEGD YNPLFIPVAV MVTAFSGLAF IIWLARRLKK GKKSKRSMND PY //