Detail Information for IndEnz0002004921
IED ID IndEnz0002004921
Enzyme Type ID protease004921
Protein Name Ficolin-2
37 kDa elastin-binding protein
Collagen/fibrinogen domain-containing protein 2
EBP-37
Ficolin-B
Ficolin-beta
Hucolin
L-ficolin
Serum lectin p35
Gene Name FCN2 FCNL
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 MELDRAVGVLGAATLLLSFLGMAWALQAADTCPEVKMVGLEGSDKLTILRGCPGLPGAPGPKGEAGTNGKRGERGPPGPPGKAGPPGPNGAPGEPQPCLTGPRTCKDLLDRGHFLSGWHTIYLPDCRPLTVLCDMDTDGGGWTVFQRRVDGSVDFYRDWATYKQGFGSRLGEFWLGNDNIHALTAQGTSELRVDLVDFEDNYQFAKYRSFKVADEAEKYNLVLGAFVEGSAGDSLTFHNNQSFSTKDQDNDLNTGNCAVMFQGAWWYKNCHVSNLNGRYLRGTHGSFANGINWKSGKGYNYSYKVSEMKVRPA
Enzyme Length 313
Uniprot Accession Number Q15485
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an opsonic effect via the collagen region. {ECO:0000269|PubMed:10679061, ECO:0000269|PubMed:17215869}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Beta strand (21); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (2); Glycosylation (2); Helix (6); Metal binding (4); Modified residue (3); Natural variant (5); Region (2); Sequence conflict (3); Signal peptide (1); Turn (3)
Keywords 3D-structure;Alternative splicing;Calcium;Collagen;Complement activation lectin pathway;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydroxylation;Immunity;Innate immunity;Lectin;Metal-binding;Reference proteome;Repeat;Secreted;Signal
Interact With P17927; O75636; Q07954; P26022; P9WQP3; P9WQP1
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 77; /note=Hydroxyproline; /evidence=ECO:0000269|PubMed:8586615; MOD_RES 80; /note=Hydroxyproline; /evidence=ECO:0000269|PubMed:8586615; MOD_RES 86; /note=Hydroxyproline; /evidence=ECO:0000269|PubMed:8586615
Post Translational Modification
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000255
Structure 3D X-ray crystallography (13)
Cross Reference PDB 2J0G; 2J0H; 2J0Y; 2J1G; 2J2P; 2J3F; 2J3G; 2J3O; 2J3U; 2J61; 4NYT; 4R9J; 4R9T;
Mapped Pubmed ID 10925294; 12396008; 14280442; 14707097; 15078867; 15199963; 15804047; 17382393; 17581635; 17938215; 18596036; 20032467; 20375619; 20953506; 21054788; 25344472; 25447524; 6019133; 70787;
Motif
Gene Encoded By
Mass 34,001
Kinetics
Metal Binding METAL 249; /note="Calcium"; /evidence="ECO:0000269|PubMed:17215869, ECO:0007744|PDB:2J1G"; METAL 251; /note="Calcium"; /evidence="ECO:0000269|PubMed:17215869, ECO:0007744|PDB:2J1G"; METAL 253; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:17215869, ECO:0007744|PDB:2J1G"; METAL 255; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:17215869, ECO:0007744|PDB:2J1G"
Rhea ID
Cross Reference Brenda