| IED ID | IndEnz0002003433 |
| Enzyme Type ID | protease003433 |
| Protein Name |
Inter-alpha-trypsin inhibitor heavy chain H2 ITI heavy chain H2 ITI-HC2 Inter-alpha-inhibitor heavy chain 2 |
| Gene Name | Itih2 |
| 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 | MQRPVCLLIWLFLLEAQAFEIPINGNSEFAEYSDLVELAPDKLPFVQENGRHQRSLPEESGEETDTVDPVTLYSYKVQSTITSRVATTTIQSKLVNNSPLPQSVVFDVQIPKGAFISNFTMTVNGMTFTSSIKEKTVGRALYSQARAKGKTAGWVRSRTLDMENFNTEVNIPPGAKVQFELHYQEVKWRKLGSYEHKIHLQPGKLAKHLEVNVWIIEPQGMRFLHVPDTFEGHFQGVPVISKGQQKAHVSFKPTVAQQRKCPNCTETAVNGELVVMYDVNREEKAGELEVFNGYFVHFFAPENLDPIPKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIEKIQPSGGTNINEALLRAIFILNEASNMGLLNPDSVSLIILVSDGDPTVGELKLSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKRLSNENRGIAQRIYGNQDTSSQLKKFYNQVSTPLLRNVQFNYPQASVTDVTQNNFHNYFGGSEIVVAGKFDPSKLTEVQSIITATSANTELVLETLSQMDDLEEFLSKDKHADPDFTKKLWAYLTINQLLAERSLAPTAAIKRKITKTILQMSLDHHIVTPLTAMVIENDAGDERMLADSPPQDHSCCSGALYYGTKVASGPIPSWANPSPTPMSAMLAVGAKPLESTPPTHLNQVENDPHFIIYLPKSKRNICFNIDSEPGKILSLVSDPESGIVVNGQLIGAKRAENGKLSTYFGKLGFYFQKEGMKIEISTETITLSSGSSTSRLSWSDTAHLGNSRVLISVKKEKSVTLTLNKELFFSVLLHRVWRKHPVNVDFLGIYAPPIDKFSPRVHGLLGQFMQEPAIHIFNERPGKEPGKPEASMEVKGHKLTVTRGLQKDYRTDIVFGTDVPCWFVHNSGKGFIDGHYKDYFVPQLYSFLKRP |
| Enzyme Length | 946 |
| Uniprot Accession Number | Q61703 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (2); Erroneous initiation (1); Glycosylation (3); Modified residue (6); Propeptide (2); Sequence conflict (1); Signal peptide (1) |
| Keywords | Gamma-carboxyglutamic acid;Glycoprotein;Phosphoprotein;Protease inhibitor;Proteoglycan;Reference proteome;Secreted;Serine protease inhibitor;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 282; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P19823"; MOD_RES 283; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P19823"; MOD_RES 466; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P19823"; MOD_RES 702; /note="Aspartate 1-(chondroitin 4-sulfate)-ester"; /evidence="ECO:0000250"; MOD_RES 886; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P19823" |
| Post Translational Modification | PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate esterified to the alpha-carboxyl of the C-terminal aspartate after propeptide cleavage. {ECO:0000250}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P19823}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12051830; 1371941; 1385302; 16615898; 18554416; 21267068; 21510876; 22159717; 24006456; 7504460; |
| Motif | |
| Gene Encoded By | |
| Mass | 105,928 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |