ID A2V6R9_FELCA Unreviewed; 376 AA. AC A2V6R9; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 02-DEC-2020, entry version 98. DE RecName: Full=L-selectin {ECO:0000256|PIRNR:PIRNR002421}; GN Name=SELL {ECO:0000313|EMBL:BAF46391.1}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|EMBL:BAF46391.1}; RN [1] {ECO:0000313|EMBL:BAF46391.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17283407; DOI=10.1292/jvms.69.81; RA Nishimura Y., Shimojima M., Tohya Y., Miyazawa T.; RT "Molecular cloning of a cDNA encoding the feline CD62L."; RL J. Vet. Med. Sci. 69:81-84(2007). CC -!- FUNCTION: Calcium-dependent lectin that mediates cell adhesion by CC binding to glycoproteins on neighboring cells. Mediates the adherence CC of lymphocytes to endothelial cells of high endothelial venules in CC peripheral lymph nodes. Promotes initial tethering and rolling of CC leukocytes in endothelia. {ECO:0000256|PIRNR:PIRNR002421}. 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, ECO:0000256|PIRNR:PIRNR002421}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. 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; AB259320; BAF46391.1; -; mRNA. DR RefSeq; NP_001082779.1; NM_001089310.1. DR GeneID; 100037404; -. DR KEGG; fca:100037404; -. DR CTD; 6402; -. DR OrthoDB; 445079at2759; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:UniProtKB-UniRule. DR GO; GO:0050900; P:leukocyte migration; IEA:InterPro. 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; IPR001881; EGF-like_Ca-bd_dom. 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; 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 SMART; SM00179; EGF_CA; 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 2: Evidence at transcript level; KW Calcium {ECO:0000256|PIRNR:PIRNR002421, ECO:0000256|PIRSR:PIRSR002421-2}; KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889, KW ECO:0000256|PIRNR:PIRNR002421}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR002421-1, ECO:0000256|PROSITE-ProRule:PRU00076}; KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE- KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000313|EMBL:BAF46391.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR002421-2}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT METAL 122 FT /note="Calcium" FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2" FT METAL 124 FT /note="Calcium" FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2" FT METAL 130 FT /note="Calcium" FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2" FT METAL 147 FT /note="Calcium" FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2" FT METAL 148 FT /note="Calcium" FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2" FT CARBOHYD 64 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3" FT CARBOHYD 108 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3" FT CARBOHYD 181 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3" FT DISULFID 61..159 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1" FT DISULFID 132..151 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1" FT DISULFID 164..175 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1" FT DISULFID 169..184 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1" FT DISULFID 186..195 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1, FT ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 201..245 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1" FT DISULFID 231..258 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1, FT ECO:0000256|PROSITE-ProRule:PRU00302" FT DISULFID 263..307 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1" FT DISULFID 293..320 FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1, FT ECO:0000256|PROSITE-ProRule:PRU00302" SQ SEQUENCE 376 AA; 42543 MW; 2390530BF9E857B5 CRC64; MSKAKVFPWK CQRAQRDSWN VFRLWVWTVL CCDFLARHGT DCWTYHYSET PMNWAKARKF CQENYTDLVA IQNKGEIEYL EQTLPFSRYY YWIGIRKVGG TWTWVGTNKS LTKEAENWGR GEPNNKKSKE DCVEIYIKRA KDAGKWNDDS CHKQKRALCY TASCQPSSCS NHGECVETIN NYTCNCDVGY YGPQCQFVVQ CEPLEAPDLG TMDCSHPVGT FSFSSQCTFN CSKGTDLIGV EETTCGPFGN WSSLEPTCQT ISCKPLMAPD LGTMDCSHPL ANFSFTSTCT FNCLEGTELI GERKIICGPS GIWSSPSPIC QKVDQSFSMI KEGNYNPLFI PVAVMVTAFS GLAFIIWLAR RLKKGKKSRE SVDDPY //