Detail Information for IndEnz0002002437
IED ID IndEnz0002002437
Enzyme Type ID protease002437
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 Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MFVRMLVFRVLLLIALVGKSVIGLSLMSFIAPPDPDWTPDDYYYSYEQSSPDEDPSVTQTTPENPDWYYEDDDPCQSNPCEHGGDCIIRGDTFSCSCPAPFSGSRCQTAQNKCKDNPCVHGDCLITQKHPYYRCACKYPYTGPDCSKVLPACRPNPCQNGGVCSRHRRRSRFTCACPDQYKGKFCEIGPDDCYVGDGYSYRGKVSKTVNQNPCLYWNSHLLLQETYNMFMEDAETHGIAEHNFCRNPDGDHKPWCFVKVNSEKVKWEYCDVTVCPVPDTPNPVESLLEPVMELPGFESCGKTEVAEHAVKRIYGGFKSTAGKHPWQVSLQTSLPLTTSMPQGHFCGGALIHPCWVLTAAHCTDINTKHLKVVLGDQDLKKTESHEQTFRVEKILKYSQYNERDEIPHNDIALLKLKPVGGHCALESRYVKTVCLPSDPFPSGTECHISGWGVTETGEGSRQLLDAKVKLIANPLCNSRQLYDHTIDDSMICAGNLQKPGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGKKPGVYTQVTKFLNWIKTTMHREAGL
Enzyme Length 558
Uniprot Accession Number Q8K0D2
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); Alternative sequence (1); Chain (4); Disulfide bond (17); Domain (5); Erroneous initiation (1); Signal peptide (1); Site (3)
Keywords Alternative splicing;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;EGF-like domain;Hydrolase;Kringle;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted. 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-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 2 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.
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000269|PubMed:11379758
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12477932; 16141072; 17145954; 17683524; 18554416; 20042707; 21267068; 21780244; 22989567; 23341458; 25300579; 25427855; 25615590; 26027930; 26258302; 27431088; 27462075; 28081210; 30814516; 31319059; 33454424; 34292881;
Motif
Gene Encoded By
Mass 62,357
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda