Detail Information for IndEnz0002004661
IED ID IndEnz0002004661
Enzyme Type ID protease004661
Protein Name Inter-alpha-trypsin inhibitor heavy chain H2
ITI heavy chain H2
ITI-HC2
Inter-alpha-inhibitor heavy chain 2
Inter-alpha-trypsin inhibitor complex component II
Serum-derived hyaluronan-associated protein
SHAP
Gene Name ITIH2 IGHEP2
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MKRLTCFFICFFLSEVSGFEIPINGLSEFVDYEDLVELAPGKFQLVAENRRYQRSLPGESEEMMEEVDQVTLYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEKTVGRALYAQARAKGKTAGLVRSSALDMENFRTEVNVLPGAKVQFELHYQEVKWRKLGSYEHRIYLQPGRLAKHLEVDVWVIEPQGLRFLHVPDTFEGHFDGVPVISKGQQKAHVSFKPTVAQQRICPNCRETAVDGELVVLYDVKREEKAGELEVFNGYFVHFFAPDNLDPIPKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQPSGGTNINEALLRAIFILNEANNLGLLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLSNENHGIAQRIYGNQDTSSQLKKFYNQVSTPLLRNVQFNYPHTSVTDVTQNNFHNYFGGSEIVVAGKFDPAKLDQIESVITATSANTQLVLETLAQMDDLQDFLSKDKHADPDFTRKLWAYLTINQLLAERSLAPTAAAKRRITRSILQMSLDHHIVTPLTSLVIENEAGDERMLADAPPQDPSCCSGALYYGSKVVPDSTPSWANPSPTPVISMLAQGSQVLESTPPPHVMRVENDPHFIIYLPKSQKNICFNIDSEPGKILNLVSDPESGIVVNGQLVGAKKPNNGKLSTYFGKLGFYFQSEDIKIEISTETITLSHGSSTFSLSWSDTAQVTNQRVQISVKKEKVVTITLDKEMSFSVLLHRVWKKHPVNVDFLGIYIPPTNKFSPKAHGLIGQFMQEPKIHIFNERPGKDPEKPEASMEVKGQKLIITRGLQKDYRTDLVFGTDVTCWFVHNSGKGFIDGHYKDYFVPQLYSFLKRP
Enzyme Length 946
Uniprot Accession Number P19823
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.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (2); Domain (2); Frameshift (1); Glycosylation (6); Modified residue (6); Natural variant (3); Propeptide (2); Region (1); Sequence conflict (7); Signal peptide (1)
Keywords Direct protein sequencing;Disulfide bond;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; by FAM20C"; /evidence="ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569"; MOD_RES 282; /note="4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:2450046"; MOD_RES 283; /note="4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:2450046"; MOD_RES 466; /note="Phosphoserine; by FAM20C"; /evidence="ECO:0000269|PubMed:26091039"; MOD_RES 702; /note="Aspartate 1-(chondroitin 4-sulfate)-ester"; MOD_RES 886; /note="Phosphoserine; by FAM20C"; /evidence="ECO:0000269|PubMed:26091039"
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: N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:7682553, ECO:0000269|PubMed:9425062, ECO:0000269|PubMed:9677337}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 15840581; 16169070; 16385451; 16702221; 18382897; 18425383; 20297716; 21939789; 23300094; 26728454; 31484722;
Motif
Gene Encoded By
Mass 106,463
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda