| IED ID | IndEnz0002010320 |
| Enzyme Type ID | protease010320 |
| Protein Name |
Collectin-11 Collectin kidney protein 1 CL-K1 |
| Gene Name | COLEC11 UNQ596/PRO1182 |
| 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 | MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLKGDAGEKGDKGAPGRPGRVGPTGEKGDMGDKGQKGSVGRHGKIGPIGSKGEKGDSGDIGPPGPNGEPGLPCECSQLRKAIGEMDNQVSQLTSELKFIKNAVAGVRETESKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRTFNKWRSGEPNNAYDEEDCVEMVASGGWNDVACHTTMYFMCEFDKENM |
| Enzyme Length | 271 |
| Uniprot Accession Number | Q9BWP8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 200; /note="Carbohydrate"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YMD"; BINDING 240; /note="Carbohydrate"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YMD"; BINDING 244; /note="Carbohydrate"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YMD" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Lectin that plays a role in innate immunity, apoptosis and embryogenesis (PubMed:23954398, PubMed:25912189, PubMed:21258343). Calcium-dependent lectin that binds self and non-self glycoproteins presenting high mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope (PubMed:25912189). Primarily recognizes the terminal disaccharide of the glycan (PubMed:25912189). Also recognizes a subset of fucosylated glycans and lipopolysaccharides (PubMed:17179669, PubMed:25912189). Plays a role in innate immunity through its ability to bind non-self sugars presented by microorganisms and to activate the complement through the recruitment of MAPS1 (PubMed:20956340, PubMed:25912189). Also plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding (Probable). Finally, plays a role in development, probably serving as a guidance cue during the migration of neural crest cells and other cell types during embryogenesis (PubMed:21258343, PubMed:28301481). {ECO:0000269|PubMed:17179669, ECO:0000269|PubMed:20956340, ECO:0000269|PubMed:21258343, ECO:0000269|PubMed:23954398, ECO:0000269|PubMed:25912189, ECO:0000269|PubMed:28301481, ECO:0000305|PubMed:20956340, ECO:0000305|PubMed:23954398}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (10); Beta strand (6); Binding site (3); Chain (1); Coiled coil (1); Disulfide bond (2); Domain (2); Helix (4); Metal binding (13); Natural variant (5); Region (2); Sequence conflict (2); Signal peptide (1) |
| Keywords | 3D-structure;Alternative splicing;Calcium;Coiled coil;Collagen;Developmental protein;Disease variant;Disulfide bond;Immunity;Innate immunity;Lectin;Mannose-binding;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | P07911 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25912189}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4YLI; 4YMD; |
| Mapped Pubmed ID | 10925294; 12396008; 14280442; 15199963; 19724895; 19851296; 20198315; 20237496; 21893516; 23220946; 24174618; 24474086; 25710878; 26154564; 26173080; 26789649; 27341702; 28772263; 30108587; 30237800; 30995222; 32041782; 32045104; 6019133; 70787; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,665 |
| Kinetics | |
| Metal Binding | METAL 207; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 211; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 211; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 232; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 234; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 235; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 238; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI"; METAL 240; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 240; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 241; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 241; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 252; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"; METAL 253; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD" |
| Rhea ID | |
| Cross Reference Brenda |