| IED ID | IndEnz0002002836 |
| Enzyme Type ID | protease002836 |
| Protein Name |
T-kininogen 1 Alpha-1-MAP Major acute phase protein T-kininogen I Thiostatin Cleaved into: T-kininogen 1 heavy chain T-kininogen I heavy chain ; T-kinin; T-kininogen 1 light chain T-kininogen I light chain |
| Gene Name | Map1 |
| 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 | MKLITILLLCSRLLPSLAQEEGAQELNCNDETVFQAVDTALKKYNAELESGNQFVLYRVTEGTKKDGAETLYSFKYQIKEGNCSVQSGLTWQDCDFKDAEEAATGECTTTLGKKENKFSVATQICNITPGKGPKKTEEDLCVGCFQPIPMDSSDLKPVLKHAVEHFNNNTKHTHLFALREVKSAHSQVVAGMNYKIIYSIVQTNCSKEDFPSLREDCVPLPYGDHGECTGHTHVDIHNTIAGFSQSCDLYPGDDLFELLPKNCRGCPREIPVDSPELKEALGHSIAQLNAQHNHIFYFKIDTVKKATSQVVAGVIYVIEFIARETNCSKQSKTELTADCETKHLGQSLNCNANVYMRPWENKVVPTVRCQALDMMISRPPGFSPFRLVRVQETKEGTTRLLNSCEYKGRLSKARAGPAPDHQAEASTVTP |
| Enzyme Length | 430 |
| Uniprot Accession Number | P01048 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Kininogens are plasma glycoproteins with a number of functions: (1) as precursor of the active peptide bradykinin they effect smooth muscle contraction, induction of hypotension and increase of vascular permeability. (2) They play a role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII. (3) They are inhibitor of thiol proteases. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Disulfide bond (9); Domain (3); Glycosylation (4); Modified residue (1); Peptide (1); Region (1); Sequence conflict (21); Signal peptide (1) |
| Keywords | Acute phase;Direct protein sequencing;Disulfide bond;Glycoprotein;Protease inhibitor;Pyrrolidone carboxylic acid;Reference proteome;Repeat;Secreted;Signal;Thiol protease inhibitor;Vasoactive;Vasodilator |
| Interact With | |
| Induction | INDUCTION: In response to an inflammatory stimulant. T-kininogen II synthesis is induced and the plasma concentration of T-kininogen I is raised. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | MOD_RES 19; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:3121623 |
| Post Translational Modification | PTM: As T-kinin is preceded by a Met instead of an Arg or Lys, it is not released from its precursor by either tissue or plasma kallikrein. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:3121623 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,775 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |