ID A2V6R9_FELCA Unreviewed; 376 AA. AC A2V6R9; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 26-FEB-2020, entry version 95. 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 -!- SIMILARITY: Belongs to the selectin/LECAM family. CC {ECO:0000256|PIRNR:PIRNR002421}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}. 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 eggNOG; ENOG410IS3T; Eukaryota. DR eggNOG; ENOG410YB82; LUCA. DR KO; K06495; -. DR OrthoDB; 445079at2759; -. DR GO; GO:0016020; C:membrane; IEA:InterPro. 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; IPR013032; EGF-like_CS. 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}; KW Cell adhesion {ECO:0000256|PIRNR:PIRNR002421}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00302}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Lectin {ECO:0000313|EMBL:BAF46391.1}; KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}. FT DISULFID 186..195 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 231..258 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302" FT DISULFID 293..320 FT /evidence="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 //