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UniProtKB/Swiss-Prot entry P14151


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LYAM1_HUMAN
Primary accession number P14151
Secondary accession numbers B2R6Q8 P15023
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on February 1, 1991 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 118)
Name and origin of the protein
Protein name L-selectin [Precursor]
Synonyms Lymph node homing receptor
Leukocyte adhesion molecule 1
LAM-1
Leukocyte surface antigen Leu-8
TQ1
gp90-MEL
Leukocyte-endothelial cell adhesion molecule 1
LECAM1
CD62 antigen-like family member L
CD62L antigen
Gene name
Name: SELL
Synonyms: LNHR, LYAM1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-193.
TISSUE=Lymphocyte;
DOI=10.1073/pnas.86.14.5562; PubMed=2664786 [NCBI, ExPASy, EBI, Israel, Japan]
Siegelman M.H., Weissman I.L.;
"Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains.";
Proc. Natl. Acad. Sci. U.S.A. 86:5562-5566(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Tonsil;
DOI=10.1084/jem.170.1.123; PubMed=2473156 [NCBI, ExPASy, EBI, Israel, Japan]
Tedder T.F., Isaacs C.M., Ernst T.J., Demetri G.D., Adler D.A., Disteche C.M.;
"Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins.";
J. Exp. Med. 170:123-133(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-213.
TISSUE=Lymphocyte;
DOI=10.1038/342078a0; PubMed=2509939 [NCBI, ExPASy, EBI, Israel, Japan]
Camerini D., James S.P., Stamenkovic I., Seed B.;
"Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor.";
Nature 342:78-82(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-193.
TISSUE=Lymphocyte;
DOI=10.1083/jcb.109.1.421; PubMed=2663882 [NCBI, ExPASy, EBI, Israel, Japan]
Bowen B.R., Nguyen T., Lasky L.A.;
"Characterization of a human homologue of the murine peripheral lymph node homing receptor.";
J. Cell Biol. 109:421-427(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1692315 [NCBI, ExPASy, EBI, Israel, Japan]
Ord D.C., Ernst T.J., Zhou L.J., Rambaldi A., Spertini O., Griffin J., Tedder T.F.;
"Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils.";
J. Biol. Chem. 265:7760-7767(1990).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-193; GLN-201; SER-213 AND ASP-369.
SeattleSNPs variation discovery resource;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[10]
INTERACTION WITH SELPLG, AND FUNCTION.
DOI=10.1074/jbc.M204360200; PubMed=12403782 [NCBI, ExPASy, EBI, Israel, Japan]
Bernimoulin M.P., Zeng X.-L., Abbal C., Giraud S., Martinez M., Michielin O., Schapira M., Spertini O.;
"Molecular basis of leukocyte rolling on PSGL-1. Predominant role of core-2 O-glycans and of tyrosine sulfate residue 51.";
J. Biol. Chem. 278:37-47(2003).
[11]
INTERACTION WITH SELPLG.
DOI=10.1074/jbc.M303551200; PubMed=12736247 [NCBI, ExPASy, EBI, Israel, Japan]
Leppaenen A., Yago T., Otto V.I., McEver R.P., Cummings R.D.;
"Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin.";
J. Biol. Chem. 278:26391-26400(2003).
[12]
3D-STRUCTURE MODELING.
DOI=10.1006/bbrc.1995.2722; PubMed=7488174 [NCBI, ExPASy, EBI, Israel, Japan]
Bajorath J., Aruffo A.;
"A template for generation and comparison of three-dimensional selectin models.";
Biochem. Biophys. Res. Commun. 216:1018-1023(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M25280; AAC63053.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16150; CAA34275.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X17519; CAB43536.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X17519; CAB43537.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16070; CAA34203.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32414; AAB60700.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32406; AAB60700.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32407; AAB60700.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32408; AAB60700.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32409; AAB60700.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32410; AAB60700.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32411; AAB60700.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32412; AAB60700.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32413; AAB60700.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312673; BAG35555.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY233976; AAO48272.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL021940; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
IPI IPI00218795; -.
RefSeq NP_000646.1; -.
UniGene Hs.714696
3D structure databases
PDB
1KJB; Model; -; A=39-158.[ExPASy / RCSB / EBI]
3CFW; X-ray; 2.20 A; A=39-194.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1KJB; -.
3CFW; -.
ModBase P14151.
PTM databases
GlycoSuiteDB P14151; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC01M167926; -.
H-InvDB HIX0001317; -.
HGNC HGNC:10720; SELL.
GenAtlas SELL.
MIM 153240; gene. [NCBI / EBI]
Orphanet 34145; Berger disease.
PharmGKB PA35642; -.
Gene expression databases
ArrayExpress P14151; -.
Bgee P14151; -.
CleanEx HS_SELL; -.
GermOnline ENSG00000188404; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0043208; Molecular function: glycosphingolipid binding (traceable author statement from UniProtKB).
GO:0008201; Molecular function: heparin binding (traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005529; Molecular function: sugar binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007155; Biological process: cell adhesion (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001304; C-type_lectin.
IPR016186; C-type_lectin-like.
IPR018378; C-type_lectin_CS.
IPR016060; Complement_control_module.
IPR006209; EGF.
IPR006210; EGF-like.
IPR013032; EGF-like_reg_CS.
IPR000742; EGF_3.
IPR016348; L-selectin.
IPR002396; Selectin.
IPR000436; Sushi_SCR_CCP.
Graphical view of domain structure.
Gene3D G3DSA:3.10.100.10; C-type_lectin-like; 1.
G3DSA:2.10.70.10; Complement_control_module; 1.
Pfam PF00008; EGF; 1.
PF00059; Lectin_C; 1.
PF00084; Sushi; 2.
Pfam graphical view of domain structure.
PIRSF PIRSF002421; L-selectin; 1.
PRINTS PR00343; SELECTIN.
SMART SM00032; CCP; 2.
SM00034; CLECT; 1.
SM00181; EGF; 1.
SMART graphical view of domain structure.
PROSITE PS00615; C_TYPE_LECTIN_1; 1.
PS50041; C_TYPE_LECTIN_2; 1.
PS00022; EGF_1; 1.
PS01186; EGF_2; 1.
PS50026; EGF_3; 1.
PS50923; SUSHI; 2.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSG00000188404; Homo sapiens. [Contig view]
GeneID 6402; -.
KEGG hsa:6402; -.
Phylogenomic databases
HOVERGEN P14151; -.
Other
NextBio 24874; -.
PMAP-CutDB P14151; -.
SOURCE SELL; Homo sapiens.
ProtoNet P14151.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane; Polymorphism; Repeat; Signal; Sushi; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    28  28      
PROPEP   29    38  10      PRO_0000017475
CHAIN   39   372  334     L-selectin. PRO_0000017476
TOPO_DOM   39   332  294     Extracellular (Potential). 
TRANSMEM   333   355  23     Potential. 
TOPO_DOM   356   372  17     Cytoplasmic (Potential). 
DOMAIN   55   155  101     C-type lectin. 
DOMAIN   156   192  37     EGF-like. 
DOMAIN   195   256  62     Sushi 1. 
DOMAIN   257   318  62     Sushi 2. 
CARBOHYD   60    60        N-linked (GlcNAc...). 
CARBOHYD   104   104        N-linked (GlcNAc...) (Potential). 
CARBOHYD   177   177        N-linked (GlcNAc...) (Potential). 
CARBOHYD   232   232        N-linked (GlcNAc...) (Potential). 
CARBOHYD   246   246        N-linked (GlcNAc...) (Potential). 
CARBOHYD   271   271        N-linked (GlcNAc...) (Potential). 
CARBOHYD   311   311        N-linked (GlcNAc...) (Potential). 
DISULFID   57   155        By similarity. 
DISULFID   128   147        By similarity. 
DISULFID   160   171        By similarity. 
DISULFID   165   180        By similarity. 
DISULFID   182   191        By similarity. 
DISULFID   197   241        By similarity. 
DISULFID   227   254        By similarity. 
DISULFID   259   303        By similarity. 
DISULFID   289   316        By similarity. 
VARIANT   193   193  1     F -> L (in dbSNP:rs1131498 [NCBI]). VAR_019134 [3D]
VARIANT   201   201  1     E -> Q (in dbSNP:rs2229568 [NCBI]). VAR_019135 
VARIANT   213   213  1     P -> S (in dbSNP:rs2229569 [NCBI]). VAR_019136 
VARIANT   369   369  1     N -> D (in dbSNP:rs4987382 [NCBI]). VAR_019137 
CONFLICT   37    37        D -> Y (in Ref. 4; CAA34203). 
CONFLICT   178   178        Y -> H (in Ref. 4; CAA34203). 
CONFLICT   214   214        L -> F (in Ref. 4; CAA34203). 
CONFLICT   218   220        SFS -> NFN (in Ref. 2; CAA34275). 
CONFLICT   242   242        G -> E (in Ref. 2; CAA34275). 
STRAND   40    48  9      
HELIX   50    60  11      
STRAND   61    64  4      
HELIX   70    79  10      
STRAND   87    94  8      
STRAND   97   100  4      
TURN   101   103  3      
TURN   109   111  3      
HELIX   122   124  3      
STRAND   128   131  4      
STRAND   136   138  3      
STRAND   142   145  4      
STRAND   151   157  7      
STRAND   167   174  8      
STRAND   177   182  6      
STRAND   187   191  5      
Sequence information
Length: 372 AA [This is the length of the unprocessed precursor] Molecular weight: 42187 Da [This is the MW of the unprocessed precursor] CRC64: 6EA9918ECA2D3643 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIFPWKCQST QRDLWNIFKL WGWTMLCCDF LAHHGTDCWT YHYSEKPMNW QRARRFCRDN 

        70         80         90        100        110        120 
YTDLVAIQNK AEIEYLEKTL PFSRSYYWIG IRKIGGIWTW VGTNKSLTEE AENWGDGEPN 

       130        140        150        160        170        180 
NKKNKEDCVE IYIKRNKDAG KWNDDACHKL KAALCYTASC QPWSCSGHGE CVEIINNYTC 

       190        200        210        220        230        240 
NCDVGYYGPQ CQFVIQCEPL EAPELGTMDC THPLGNFSFS SQCAFSCSEG TNLTGIEETT 

       250        260        270        280        290        300 
CGPFGNWSSP EPTCQVIQCE PLSAPDLGIM NCSHPLASFS FTSACTFICS EGTELIGKKK 

       310        320        330        340        350        360 
TICESSGIWS NPSPICQKLD KSFSMIKEGD YNPLFIPVAV MVTAFSGLAF IIWLARRLKK 

       370 
GKKSKRSMND PY 

P14151 in FASTA format

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