| IED ID | IndEnz0002003205 |
| Enzyme Type ID | protease003205 |
| Protein Name |
Hyaluronan-binding protein 2 EC 3.4.21.- Factor VII-activating protease Factor seven-activating protease FSAP Hepatocyte growth factor activator-like protein Plasma hyaluronan-binding protein Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form |
| Gene Name | HABP2 HGFAL PHBP |
| 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 | MFARMSDLHVLLLMALVGKTACGFSLMSLLESLDPDWTPDQYDYSYEDYNQEENTSSTLTHAENPDWYYTEDQADPCQPNPCEHGGDCLVHGSTFTCSCLAPFSGNKCQKVQNTCKDNPCGRGQCLITQSPPYYRCVCKHPYTGPSCSQVVPVCRPNPCQNGATCSRHKRRSKFTCACPDQFKGKFCEIGSDDCYVGDGYSYRGKMNRTVNQHACLYWNSHLLLQENYNMFMEDAETHGIGEHNFCRNPDADEKPWCFIKVTNDKVKWEYCDVSACSAQDVAYPEESPTEPSTKLPGFDSCGKTEIAERKIKRIYGGFKSTAGKHPWQASLQSSLPLTISMPQGHFCGGALIHPCWVLTAAHCTDIKTRHLKVVLGDQDLKKEEFHEQSFRVEKIFKYSHYNERDEIPHNDIALLKLKPVDGHCALESKYVKTVCLPDGSFPSGSECHISGWGVTETGKGSRQLLDAKVKLIANTLCNSRQLYDHMIDDSMICAGNLQKPGQDTCQGDSGGPLTCEKDGTYYVYGIVSWGLECGKRPGVYTQVTKFLNWIKATIKSESGF |
| Enzyme Length | 560 |
| Uniprot Accession Number | Q14520 |
| Absorption | |
| Active Site | ACT_SITE 362; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 411; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 509; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII (PubMed:8827452, PubMed:10754382, PubMed:11217080). May function as a tumor suppressor negatively regulating cell proliferation and cell migration (PubMed:26222560). {ECO:0000269|PubMed:10754382, ECO:0000269|PubMed:11217080, ECO:0000269|PubMed:26222560, ECO:0000269|PubMed:8827452}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (4); Disulfide bond (17); Domain (5); Glycosylation (2); Natural variant (3); Sequence conflict (1); Signal peptide (1); Site (3) |
| Keywords | Alternative splicing;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Kringle;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8827452}. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytic cleavage at Gly-23 or Met-27 can give rise to the 50 kDa heavy chain and cleavage at Arg-313 or Lys-319 can give rise to the 27 kDa light chain. The heavy chain can undergo further proteolytic cleavage at Lys-169 or Arg-170 to give rise to 2 inactive 26 kDa fragments and the light chain can undergo further proteolytic cleavage at Arg-480 to give rise to inactive 17 kDa and 8 kDa fragments (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:8827452 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11379758; 15486068; 15543324; 15654766; 15933067; 16153533; 16332249; 16385451; 16461761; 17003923; 17145954; 17479202; 17482622; 17540775; 18278202; 18394684; 19105210; 19446554; 19817990; 19913121; 20042707; 20045910; 20235792; 20532885; 20558613; 20628086; 20818495; 21071862; 21098215; 21600885; 21655671; 21737124; 21812934; 22116096; 22235940; 22308306; 22383781; 22409238; 22421107; 22449009; 22850287; 22906531; 22989567; 23341458; 23575879; 24075769; 24497464; 25370187; 25847894; 26732560; 26832773; 26906432; 27073188; 27245704; 27462075; 27530615; 27873212; 28089742; 28222214; 28246168; 28402931; 28418605; 28501930; 28548975; 28726978; 28881271; 29178989; 29665850; 29895015; 30070759; 30076961; 31635523; 31698750; 31831842; 31914657; 32087413; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,672 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B1; |