LYAM1_HUMAN
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 03-AUG-2022, entry version 231.
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:28489325, PubMed:28011641). 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=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/sell/";
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";
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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; CCDS53427.1; -. [P14151-1]
DR RefSeq; NP_000646.2; NM_000655.4. [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 PDBsum; 2LGF; -.
DR PDBsum; 3CFW; -.
DR PDBsum; 5VC1; -.
DR AlphaFoldDB; P14151; -.
DR BMRB; P14151; -.
DR SMR; P14151; -.
DR BioGRID; 112302; 15.
DR IntAct; P14151; 1.
DR STRING; 9606.ENSP00000236147; -.
DR BindingDB; P14151; -.
DR ChEMBL; CHEMBL3161; -.
DR UniLectin; P14151; -.
DR GlyConnect; 346; 26 N-Linked glycans (1 site).
DR GlyGen; P14151; 7 sites, 46 N-linked glycans (2 sites).
DR iPTMnet; P14151; -.
DR PhosphoSitePlus; P14151; -.
DR BioMuta; SELL; -.
DR DMDM; 126178; -.
DR jPOST; P14151; -.
DR MassIVE; P14151; -.
DR MaxQB; P14151; -.
DR PaxDb; P14151; -.
DR PeptideAtlas; P14151; -.
DR PRIDE; P14151; -.
DR ProteomicsDB; 53028; -. [P14151-1]
DR ProteomicsDB; 53029; -. [P14151-2]
DR ABCD; P14151; 4 sequenced antibodies.
DR Antibodypedia; 3683; 1543 antibodies from 49 providers.
DR DNASU; 6402; -.
DR Ensembl; ENST00000236147.6; ENSP00000236147.5; ENSG00000188404.10. [P14151-1]
DR Ensembl; ENST00000650983.1; ENSP00000498227.1; ENSG00000188404.10. [P14151-2]
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 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 neXtProt; NX_P14151; -.
DR OpenTargets; ENSG00000188404; -.
DR PharmGKB; PA35642; -.
DR VEuPathDB; HostDB:ENSG00000188404; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162076; -.
DR HOGENOM; CLU_065067_0_0_1; -.
DR InParanoid; P14151; -.
DR OrthoDB; 445079at2759; -.
DR PhylomeDB; P14151; -.
DR TreeFam; TF326910; -.
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 BioGRID-ORCS; 6402; 4 hits in 1064 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 tissues.
DR ExpressionAtlas; P14151; baseline and differential.
DR Genevisible; P14151; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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: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:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; TAS:BHF-UCL.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
DR CDD; cd00033; CCP; 2.
DR CDD; cd03592; CLECT_selectins_like; 1.
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; IPR033991; Selectin_CTLD.
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 SMART; SM00181; EGF; 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 3D-structure; Alternative initiation; Calcium; Cell adhesion;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Lectin;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Sushi;
KW 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..43
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
