ID B1B507_MOUSE Unreviewed; 387 AA.
AC B1B507;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=L-selectin {ECO:0000256|ARBA:ARBA00014208};
DE AltName: Full=CD62 antigen-like family member L {ECO:0000256|ARBA:ARBA00030282};
DE AltName: Full=Leukocyte adhesion molecule 1 {ECO:0000256|ARBA:ARBA00031844};
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 1 {ECO:0000256|ARBA:ARBA00032968};
DE AltName: Full=Lymph node homing receptor {ECO:0000256|ARBA:ARBA00030610};
GN Name=Sell {ECO:0000313|EMBL:BAG12831.1,
GN ECO:0000313|Ensembl:ENSMUSP00000095099.5, ECO:0000313|MGI:MGI:98279};
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 {ECO:0000313|EMBL:BAG12831.1};
RN [1] {ECO:0000313|EMBL:BAG12831.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18332130; DOI=10.1074/jbc.M801745200;
RA Furukawa Y., Umemoto E., Jang M.H., Tohya K., Miyasaka M., Hirata T.;
RT "Identification of novel isoforms of mouse L-selectin with different
RT carboxyl-terminal tails.";
RL J. Biol. Chem. 283:12112-12119(2008).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000095099.5, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000095099.5,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000095099.5}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000095099.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00011813}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family.
CC {ECO:0000256|ARBA:ARBA00007360}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AB353768; BAG12831.1; -; mRNA.
DR RefSeq; XP_006496779.1; XM_006496716.1.
DR ProteomicsDB; 336672; -.
DR Antibodypedia; 3683; 1813 antibodies from 50 providers.
DR Ensembl; ENSMUST00000097491.10; ENSMUSP00000095099.5; ENSMUSG00000026581.15.
DR UCSC; uc011wuw.1; mouse.
DR AGR; MGI:98279; -.
DR MGI; MGI:98279; Sell.
DR VEuPathDB; HostDB:ENSMUSG00000026581; -.
DR GeneTree; ENSGT00940000162076; -.
DR OrthoDB; 3035244at2759; -.
DR BioGRID-ORCS; 20343; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Sell; mouse.
DR Proteomes; UP000000589; Chromosome 1.
DR Bgee; ENSMUSG00000026581; Expressed in granulocyte and 51 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0070492; F:oligosaccharide binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
DR CDD; cd00033; CCP; 2.
DR CDD; cd03592; CLECT_selectins_like; 1.
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; 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; 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.
PE 1: Evidence at protein level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR002421-2};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR002421-1};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000313|EMBL:BAG12831.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR002421-2};
KW Proteomics identification {ECO:0007829|EPD:B1B507,
KW ECO:0007829|MaxQB:B1B507};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..387
FT /note="L-selectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015087044"
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..156
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 156..192
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 195..256
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 257..318
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3"
FT DISULFID 57..155
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 128..147
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 160..171
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 165..180
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 182..191
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 197..241
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 227..254
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 259..303
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 289..316
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 387 AA; 43585 MW; 84611E373FC80E8A 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
GRTNAPATGP QSAAVLRCAL PHLSTFI
//
