Detail Information for IndEnz0002004131
IED ID IndEnz0002004131
Enzyme Type ID protease004131
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 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 MEGATGLRVLLCLLPLLTLQARPALGLATGRPRGSEKRHAVDTSVNGVSIKSLKVNCKVTSRFAHYVITSQVVNNADKAREVAFDVEIPKTAFISDFAITSDGKAFIGDIKDKVTAWKQYRKAAVLGESAGLVRASGRNMEQFTIHITVGAQSKATFRLTYEEVLKRRLMQYDITIKVRPKQLVQHFEIDVDIFEPQGISKLDAQASFLSEELAAQTIKKSFSGKKGHVLFRPTVSQQQSCPTCSTSLLNGEFKVTYDVNRDKLCDLLVANNYFTHFFAPKNLTNMSKNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFSLAGATNLNGGLLRGIEILNKAQGSHPELSSPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMSTENNGWAQRIYEDHDATQQLQGFYNQVANPLLTDVELQYPQDAVLALTQHRHKQYYDGSEIVVAGRIANHKLNTFKADVRARGEKQEFRATCLVDEEEMKKLLRERGHVLENHVERLWAYLTIQELLAKRMKTEGEERANLSSQVLKMSLDYHFVTPLTSLTIRGLTDEDGLEPTIDKPLEDSQPLEMVGPRRTFVLSAIQPSPTAHPIDSKLPLRVTGVDTDPHFIIYVPSKEDSLCFNINEEPGVILNLVQDPDTGFTVNGQLIGNKASSPGQHESTYFGRLGISSPTSDFQLEVTPQNITLNPSSSGSMFSWRDQAVLQKDGVVVTINKKRNLVVSVDDGATFEIVLHRTWKGSAVHQDFLGFYVLDSFRMSARTKGLLGQFFSPLDFEVFDLHPGSDPTKTDATMVVKNRQLTVTRGLQKDYSKDPRHGAEVPCWFVHDNGAGLIDGVHTDYVVSDIF
Enzyme Length 907
Uniprot Accession Number Q61702
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 (3); Propeptide (2); Sequence conflict (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.
Modified Residue MOD_RES 399; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P19827; MOD_RES 404; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P19827; MOD_RES 668; /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..26; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10446282; 11130978; 1371941; 1385302; 17675295; 17785858; 21267068; 21677750; 22159717; 28071719; 7504460; 7522574; 9126497;
Motif
Gene Encoded By
Mass 101,067
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda