| IED ID | IndEnz0002002861 |
| Enzyme Type ID | protease002861 |
| Protein Name |
Hyaluronan-binding protein 2 EC 3.4.21.- 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 Phbp |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSVVMLVFRVLLLIALVGNSAIGLSLMPFIAPPDPDWTPDDYYYSYEQSSPDKDASVTQTSPENPDWYYEDDDPCQSNPCEHGGDCIIRGNTFSCSCPAPFSGSRCQTVQNKCKDNPCVQGDCLITQTPPYYRCACKYPYTGPDCSKVLPVCRPNPCQNGGVCSRHRRRSRFSCACPDQYKGRFCEIGPDDCYVGDGYSYRGKVSRTVNQNPCLYWNSHLLLQENYNMFMEDAETHGIADHNFCRNPDGDHKPWCFVKVNSEKVKWEYCNVEVCPESDAANPVGSLQEPVMELPGFDSCGKTEMTEHAVKRIYGGFKSTAGKHPWQVSLQTSLPLTTSMPQGHFCGGSLIHPCWVLTAAHCTDMSTKHLKVVLGDQDLKKTESHEQTFRVEKILKYSQYNERDEIPHNDIALLKLKPVGGHCALESKYVKTVCLPSDPFPSGTECHISGWGVTETGEGSRQLLDAKVKLIANALCNSRQLYDHTIDDSMICAGNLQKPGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGKKPGVYTQVTKFLNWIKTTMHKEAGL |
| Enzyme Length | 558 |
| Uniprot Accession Number | Q6L711 |
| Absorption | |
| Active Site | ACT_SITE 360; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 409; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 507; /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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (4); Disulfide bond (17); Domain (5); Signal peptide (1); Site (3) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Hydrolase;Kringle;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form. {ECO:0000250}. |
| 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-311 or Lys-317 can give rise to the 27 kDa light chain. The heavy chain can undergo further proteolytic cleavage at Arg-168 or Arg-169 to give rise to two inactive 26 kDa fragments and the light chain can undergo further proteolytic cleavage at Arg-478 to give rise to inactive 17 kDa and 8 kDa fragments (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20818495; 22715430; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,093 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |