ID A2V6R9_FELCA Unreviewed; 376 AA. AC A2V6R9; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 31-JAN-2018, entry version 83. 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; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC 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: Cell surface adhesion protein. 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. {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 CC of 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 ProteinModelPortal; A2V6R9; -. DR GeneID; 100037404; -. DR KEGG; fca:100037404; -. DR CTD; 6402; -. DR eggNOG; ENOG410IS3T; Eukaryota. DR eggNOG; ENOG410YB82; LUCA. DR HOGENOM; HOG000236254; -. DR HOVERGEN; HBG052375; -. DR KO; K06495; -. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl. DR GO; GO:0050839; F:cell adhesion molecule 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 GO; GO:0033198; P:response to ATP; IEA:Ensembl. 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 Cell adhesion {ECO:0000256|PIRNR:PIRNR002421}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002421-1, ECO:0000256|PROSITE- KW ProRule:PRU00076, ECO:0000256|SAAS:SAAS00601599}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076, KW ECO:0000256|SAAS:SAAS00798080}; Lectin {ECO:0000313|EMBL:BAF46391.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Repeat {ECO:0000256|SAAS:SAAS00887150}; KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302, KW ECO:0000256|SAAS:SAAS00937752}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 338 359 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 38 160 C-type lectin. {ECO:0000259|PROSITE: FT PS50041}. FT DOMAIN 160 196 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DOMAIN 199 260 Sushi. {ECO:0000259|PROSITE:PS50923}. FT DOMAIN 261 322 Sushi. {ECO:0000259|PROSITE:PS50923}. FT DISULFID 61 159 {ECO:0000256|PIRSR:PIRSR002421-1}. FT DISULFID 132 151 {ECO:0000256|PIRSR:PIRSR002421-1}. FT DISULFID 164 175 {ECO:0000256|PIRSR:PIRSR002421-1}. FT DISULFID 169 184 {ECO:0000256|PIRSR:PIRSR002421-1}. FT DISULFID 186 195 {ECO:0000256|PIRSR:PIRSR002421-1, FT ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 201 245 {ECO:0000256|PIRSR:PIRSR002421-1}. FT DISULFID 231 258 {ECO:0000256|PIRSR:PIRSR002421-1, FT ECO:0000256|PROSITE-ProRule:PRU00302}. FT DISULFID 263 307 {ECO:0000256|PIRSR:PIRSR002421-1}. FT DISULFID 293 320 {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 //