| IED ID | IndEnz0002013536 |
| Enzyme Type ID | protease013536 |
| Protein Name |
Vitronectin VN S-protein Serum-spreading factor V75 Cleaved into: Vitronectin V65 subunit; Vitronectin V10 subunit; Somatomedin-B |
| Gene Name | VTN |
| 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 | MAPLRPLLILALLAWVALADQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTMPEDEYTVYDDGEEKNNATVHEQVGGPSLTSDLQAQSKGNPEQTPVLKPEEEAPAPEVGASKPEGIDSRPETLHPGRPQPPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDEKAVRPGYPKLIRDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISDGFDGIPDNVDAALALPAHSYSGRERVYFFKGKQYWEYQFQHQPSQEECEGSSLSAVFEHFAMMQRDSWEDIFELLFWGRTSAGTRQPQFISRDWHGVPGQVDAAMAGRIYISGMAPRPSLAKKQRFRHRNRKGYRSQRGHSRGRNQNSRRPSRATWLSLFSSEESNLGANNYDDYRMDWLVPATCEPIQSVFFFSGDKYYRVNLRTRRVDTVDPPYPRSIAQYWLGCPAPGHL |
| Enzyme Length | 478 |
| Uniprot Accession Number | P04004 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; FUNCTION: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (19); Chain (3); Compositional bias (2); Disulfide bond (8); Domain (1); Glycosylation (3); Helix (6); Modified residue (11); Motif (1); Mutagenesis (4); Natural variant (3); Peptide (1); Region (3); Repeat (4); Sequence conflict (4); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Cell adhesion;Direct protein sequencing;Disulfide bond;Glycoprotein;Heparin-binding;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Sulfation |
| Interact With | Q07021; Q15700; Q92796; Q9HD26; Q9HD26-2; Q9NSN8; Q9UHD9; P75358; P75167; P78007; A0A024A2C9; P75390; P75391; P78031; P75611; Q4KTX9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:2448300, ECO:0000269|PubMed:29567995}.; SUBCELLULAR LOCATION: Parasitophorous vacuole {ECO:0000269|PubMed:29567995}. Note=(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage (PubMed:29567995). Colocalizes with SERA5 at the schizont stage and with SERA5 P47 at the merozoite surface (PubMed:29567995). {ECO:0000269|PubMed:29567995}. |
| Modified Residue | MOD_RES 69; /note="Phosphothreonine; by CK2; in vitro"; /evidence="ECO:0000269|PubMed:9733784"; MOD_RES 75; /note="Sulfotyrosine"; /evidence="ECO:0000269|PubMed:17558413"; MOD_RES 76; /note="Phosphothreonine; by CK2; in vitro"; /evidence="ECO:0000269|PubMed:9733784"; MOD_RES 78; /note="Sulfotyrosine"; /evidence="ECO:0000269|PubMed:17558413"; MOD_RES 130; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 137; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 282; /note="Sulfotyrosine"; /evidence="ECO:0000255"; MOD_RES 312; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:17558413, ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:24275569"; MOD_RES 397; /note="Phosphoserine; by PKA"; /evidence="ECO:0000269|PubMed:1696913, ECO:0000269|PubMed:2448300"; MOD_RES 417; /note="Sulfotyrosine"; /evidence="ECO:0000255"; MOD_RES 420; /note="Sulfotyrosine"; /evidence="ECO:0000255" |
| Post Translational Modification | PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:17558413, ECO:0000269|PubMed:2479556, ECO:0000269|PubMed:25136834}.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading. {ECO:0000269|PubMed:9733784}.; PTM: It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.; PTM: Phosphorylation sites are present in the extracellular medium. |
| Signal Peptide | SIGNAL 1..19; /evidence="ECO:0000269|PubMed:631332, ECO:0000269|PubMed:7522053" |
| Structure 3D | NMR spectroscopy (3); X-ray crystallography (5) |
| Cross Reference PDB | 1OC0; 1S4G; 1SSU; 2JQ8; 3BT1; 3BT2; 4K24; 6O5E; |
| Mapped Pubmed ID | 10424889; 11034322; 11744726; 11756447; 11785953; 11795878; 11796716; 11864711; 12071840; 12091360; 12437099; 12757937; 12810534; 12913402; 1376317; 14586734; 14681059; 15069014; 15123712; 15123885; 15140223; 15157085; 15641781; 15717924; 15777802; 15843372; 15905170; 15914035; 16237761; 16815299; 1694173; 1708799; 17344041; 17766387; 17968485; 18174166; 18200066; 18340378; 18362146; 18376415; 18516040; 18624398; 18658131; 18781095; 18842294; 19118218; 19162023; 19193026; 19288063; 19408099; 19635912; 19657137; 19730683; 19893454; 19913121; 19998373; 20031688; 20066177; 20121701; 20199596; 20358426; 20492459; 20502634; 20562859; 20600001; 20628086; 21048021; 21193465; 21253761; 21316840; 21418524; 21516116; 21542857; 21800006; 21988832; 22050461; 22106087; 22810367; 23041018; 23124223; 23300094; 23327926; 23387957; 23474333; 23603906; 23722547; 23811340; 23899674; 2412224; 2420006; 24286496; 2430969; 24465541; 24603119; 24625558; 2465906; 2466593; 24687613; 24770328; 24823429; 24999757; 25168639; 25179307; 25181963; 25374123; 25416956; 25609649; 25768308; 26028330; 26047937; 26101327; 26368530; 26377177; 26548921; 26572616; 26617861; 26709396; 27189837; 27802203; 27871448; 28186697; 29123267; 29222114; 29463024; 29780059; 30396333; 31117974; 31307158; 31535027; 32499371; 32699145; 33105833; 33211735; 33259607; 33444672; 33750855; 34103584; 7525578; 7542572; 7542669; 7559467; 7685013; 9030777; 9251239; 9443892; |
| Motif | MOTIF 64..66; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 54,306 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |