IED ID | IndEnz0002015619 |
Enzyme Type ID | protease015619 |
Protein Name |
Inter-alpha-trypsin inhibitor heavy chain H1 ITI heavy chain H1 ITI-HC1 Inter-alpha-inhibitor heavy chain 1 |
Gene Name | ITIH1 |
Organism | Bos taurus (Bovine) |
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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
Enzyme Sequence | MGLRGLLCVCLVSLLALQAVAAQGSPTRNPKGGKKRMAVDAAVDGVVIRSLKVNCKVTSRFAHYIITSQVVNSADTAKEVSFNVEIPKTAFISDFAITADENAFTGDIKDKVTAWKQYRKAAISGENAGLVRASGRTMEQFSIHIIVGPRSKATFRLTYEEVLRRKLMQYDIVIKVKPQQLVQHFEIDVDIFEPQGIRKLDVEASFLPKELAAQLIKKSFSGKKGHVLFRPTVSQQQTCPTCSTTLLNGDFKVTYDVNRDDACDLLVANNYFAHFFAPQNLKKLNKNVVFVIDISSSMEGQKLKQTKEALHKILGDMRPGDYFDLVLFGSAVQSWKGSLVQASPANLEAARNFVQQFSLAGATNLNGGLLRGIEILNKAQQSLPELSNHASILIMLTDGEPTEGVMDRTQILKNVRDGIKGRFPLYNLGFGHDVDLNFLEVMSLENNGRVQRIYEDHDATQQLQGFYEQVANPLLRDVELLYPREAVSDLTQHRHKQYYEGSEIMVAGRIADHKLSSFKADVRAHGEGQEFMTTCLVDKEEMKKLLRERGHMLENHVERLWAYLTIQELLAKRMKLEGQEKANVSAKALQMSLAYQFVTPLTSMTVRGMTDQDGLEPIIDKPLDDYLPLEMVGPRKTFMLQASQPAPTHSSLDIKKLPDQVTGVDTDPHFLIHVPQKEDTLCFNINEEPGVVLSLVQDPDTGFSVNGQLIGNEAGSPGKHEGTYFGRLGIANPATDFQLEVTPQNITLNPGSGGPVFSWRDQAFLRQNEVLVTINRKRNLVVSVEDGGTFEVVLHRVWRGSAVRQDFLGFYVLDSHRMSARTHGLLGQFFHPFDYKVSNLHPGSDPTKTDATMVVKNRRLTVTRGLQKDYRKDPRHGAEVTCWFIHNNGDGLIDGIHTDYIVPDIF |
Enzyme Length | 906 |
Uniprot Accession Number | Q0VCM5 |
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); Glycosylation (5); Modified residue (4); Propeptide (2); Signal peptide (1) |
Keywords | Glycoprotein;Phosphoprotein;Protease inhibitor;Proteoglycan;Reference proteome;Secreted;Serine protease inhibitor;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | MOD_RES 124; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P19827; MOD_RES 397; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P19827; MOD_RES 402; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P19827; MOD_RES 667; /note=Aspartate 1-(chondroitin 4-sulfate)-ester; /evidence=ECO:0000250 |
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: The S-linked glycan is composed of two 6-carbon sugars, possibly Glc or Gal. {ECO:0000250}. |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 101,237 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |