| IED ID | IndEnz0002015961 |
| Enzyme Type ID | protease015961 |
| Protein Name |
L-selectin CD62 antigen-like family member L Leukocyte adhesion molecule 1 LAM-1 Leukocyte surface antigen Leu-8 Leukocyte-endothelial cell adhesion molecule 1 LECAM1 Lymph node homing receptor TQ1 gp90-MEL CD antigen CD62L |
| Gene Name | SELL LNHR LYAM1 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MIFPWKCQSTQRDLWNIFKLWGWTMLCCDFLAHHGTDCWTYHYSEKPMNWQRARRFCRDNYTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPNNKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTCNCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFSCSEGTNLTGIEETTCGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKKTICESSGIWSNPSPICQKLDKSFSMIKEGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKKGKKSKRSMNDPY |
| Enzyme Length | 372 |
| Uniprot Accession Number | P14151 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells (PubMed:12403782, PubMed:28489325, PubMed:28011641). Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia (PubMed:12403782, PubMed:28011641). {ECO:0000269|PubMed:12403782, ECO:0000269|PubMed:28011641, ECO:0000305|PubMed:28489325}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (11); Chain (1); Disulfide bond (9); Domain (4); Glycosylation (6); Helix (4); Metal binding (5); Mutagenesis (4); Natural variant (4); Propeptide (1); Sequence conflict (5); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) |
| Keywords | 3D-structure;Alternative initiation;Calcium;Cell adhesion;Cell membrane;Disulfide bond;EGF-like domain;Glycoprotein;Lectin;Membrane;Metal-binding;Reference proteome;Repeat;Signal;Sushi;Transmembrane;Transmembrane helix |
| Interact With | Q9BRI3 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2509939, ECO:0000269|PubMed:2663882, ECO:0000269|PubMed:28011641}; Single-pass type I membrane protein {ECO:0000305|PubMed:2663882}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:2663882, ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325}. |
| Signal Peptide | SIGNAL 1..28 |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (2) |
| Cross Reference PDB | 2LGF; 3CFW; 5VC1; |
| Mapped Pubmed ID | 11064106; 11466384; 11821431; 11828340; 11907045; 12042326; 12063026; 12144128; 12147693; 12165498; 12186696; 12200076; 12200386; 12202158; 12370391; 12431911; 12496379; 12532021; 12588680; 12595908; 12609846; 12738381; 12844406; 12871600; 12874338; 14533031; 14576059; 14585903; 14597772; 14615387; 14737745; 15093751; 15178693; 15192100; 15470072; 15506984; 15776384; 15831305; 16270299; 16352650; 16357481; 16565092; 16585636; 16690519; 16738933; 16740600; 16916660; 16974056; 17028146; 17055225; 17056762; 17322099; 17407075; 17465998; 17515951; 17525255; 17698668; 17703412; 17706337; 17765649; 17890399; 17954174; 18028430; 18032547; 18089680; 18182036; 18191640; 18250165; 18375392; 18385135; 18496641; 18582506; 18665829; 18713749; 18713968; 18829897; 18973547; 18974842; 19052753; 19064610; 19074885; 19088176; 19118161; 19129194; 19212205; 19240957; 19258923; 19419934; 19451621; 19462221; 19536175; 19654311; 19670701; 19837408; 19913121; 19954409; 20065025; 20212041; 20220571; 20306662; 20469932; 20485444; 20503287; 20507883; 20580062; 20628086; 20708610; 20925194; 21197561; 21237580; 21316337; 21465128; 21484243; 21521525; 21546114; 21584225; 21664913; 21869829; 22068558; 22119815; 22159147; 22711531; 22836626; 22921892; 22941246; 22977256; 23028631; 23319734; 23442851; 23487023; 23571167; 23573259; 23650620; 23658780; 23796515; 23925765; 23927766; 24127491; 24399259; 24516598; 24595810; 24606340; 24631064; 24829027; 25095634; 25209910; 25498912; 25576479; 25618296; 25775539; 25822027; 26162407; 26329844; 26361072; 26432858; 26693907; 26852488; 27003497; 27183388; 27406841; 27620619; 27775438; 28478085; 28765940; 28811304; 28842197; 29218606; 29356883; 30119013; 30443903; 30504420; 31608057; 31644306; 31814717; 32048570; 32433445; 33408247; 33482019; 33537175; 33728641; 7521878; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,187 |
| Kinetics | |
| Metal Binding | METAL 118; /note="Calcium"; /evidence="ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, ECO:0007744|PDB:5VC1"; METAL 120; /note="Calcium"; /evidence="ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, ECO:0007744|PDB:5VC1"; METAL 126; /note="Calcium"; /evidence="ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, ECO:0007744|PDB:5VC1"; METAL 143; /note="Calcium"; /evidence="ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, ECO:0007744|PDB:5VC1"; METAL 144; /note="Calcium"; /evidence="ECO:0000269|PubMed:28011641, ECO:0000269|PubMed:28489325, ECO:0007744|PDB:3CFW, ECO:0007744|PDB:5VC1" |
| Rhea ID | |
| Cross Reference Brenda |