Detail Information for IndEnz0002005837
IED ID IndEnz0002005837
Enzyme Type ID protease005837
Protein Name Ficolin-1
Collagen/fibrinogen domain-containing protein 1
Ficolin-A
Ficolin-alpha
M-ficolin
Gene Name FCN1 FCNM
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 MELSGATMARGLAVLLVLFLHIKNLPAQAADTCPEVKVVGLEGSDKLTILRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAGQSQSCATGPRNCKDLLDRGYFLSGWHTIYLPDCRPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNIHALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFVGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEKFQGAWWYADCHASNLNGLYLMGPHESYANGINWSAAKGYKYSYKVSEMKVRPA
Enzyme Length 326
Uniprot Accession Number O00602
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8 (PubMed:21037097). Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage. {ECO:0000269|PubMed:20032467, ECO:0000269|PubMed:21037097}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (16); Chain (1); Disulfide bond (3); Domain (2); Erroneous initiation (1); Glycosylation (1); Helix (7); Metal binding (4); Mutagenesis (3); Natural variant (3); Region (5); Sequence conflict (2); Signal peptide (1); Site (2); Turn (2)
Keywords 3D-structure;Calcium;Cell membrane;Collagen;Direct protein sequencing;Disulfide bond;Glycoprotein;Immunity;Innate immunity;Lectin;Membrane;Metal-binding;Reference proteome;Repeat;Secreted;Signal
Interact With P02741; P26022; Q2TS39; O15552; P26022; P02769; P9WQP3; P9WQP1
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}. Cell membrane {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Peripheral membrane protein {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Extracellular side {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}. Note=Found on the monocyte and granulocyte surface (PubMed:20400674).
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..29; /evidence=ECO:0000269|PubMed:15340161
Structure 3D X-ray crystallography (7)
Cross Reference PDB 2D39; 2JHH; 2JHI; 2JHK; 2JHL; 2JHM; 2WNP;
Mapped Pubmed ID 10639434; 10925294; 11012776; 11532276; 12396008; 14280442; 15117939; 15199963; 15728497; 16116205; 16305643; 17581635; 17928056; 17938215; 18032536; 18343499; 19539995; 19741154; 19853918; 20237496; 20375634; 21112665; 21490156; 21689722; 21730084; 21974696; 22236007; 22391637; 22673311; 22941510; 23184524; 23209787; 23650620; 23817411; 24022747; 24161415; 25069872; 26154564; 26792363; 26984723; 27734336; 27981461; 27994205; 28060571; 28601054; 28900133; 30619357; 32142211; 32601370; 32915797; 33591573; 6019133; 70787;
Motif
Gene Encoded By
Mass 35,078
Kinetics
Metal Binding METAL 262; /note="Calcium"; /evidence="ECO:0000269|PubMed:17148457, ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467, ECO:0007744|PDB:2D39, ECO:0007744|PDB:2WNP"; METAL 264; /note="Calcium"; /evidence="ECO:0000269|PubMed:17148457, ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467, ECO:0007744|PDB:2D39, ECO:0007744|PDB:2WNP"; METAL 266; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:17148457, ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467, ECO:0007744|PDB:2D39, ECO:0007744|PDB:2WNP"; METAL 268; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:17148457, ECO:0000269|PubMed:17897951, ECO:0000269|PubMed:20032467, ECO:0007744|PDB:2D39, ECO:0007744|PDB:2WNP"
Rhea ID
Cross Reference Brenda