IED ID | IndEnz0002009218 |
Enzyme Type ID | protease009218 |
Protein Name |
Murinoglobulin-1 Alpha-1 inhibitor 3 variant I Alpha-X protein |
Gene Name | Mug1 A1i3 |
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 | MKKNREAQLCLFSALLAFLPFASLLNGNSKYMVLVPSQLYTETPEKICLHLYHLNETVTVTASLISQRGTRKLFDELVVDKDLFHCLSFTIPRLPSSEEEESLDINIEGAKHKFSERRVVLVKNKESVVFVQTDKPVYKPGQSVKFRVVSMDKNLHPLNELFPLAYIEDPKMNRIMQWQDIKTENGLKQLSFSLSAEPIQGPYKIVILKQSGVKEEHSFTVMEFVLPRFGVDVKVPNAISVYDEIINVTACAIYTYGKPVPGHVKISLCHGNPSFSSETKSACKEEDSELDNNGCSTQEVNITEFQLKENYLKMHQAFHVNATVTEEGTGSEFSGSGRIEVERTRNKFLFLKADSHFRHGIPFFVKIRLVDIKGDPIPNEQVFIKAQEAGYTNATTTDQHGLAKFSIDTSSISGYSLNIKVYHKEESSCIHSSCTAERHAEEHHTAYAVYSLSKSYIYLDTEAGVLPCNQIHTVQAHFILKGQVLGVLPQIVFHYLVMAQGSILQTGNHTHQVEPGVSQVQGNFALEIPVEFSMVPVAKMLIYTILPDGEVIADSVTFQVEKCLRNKVHLSFSPSQSLPASQTHMRVTASPQSLCGLRAVDQSVLLLKPEAELSPSLIYDLPGMQDSNFIPSSYHPFEDEYDCLMYQPRDTEELTYSVPYGREKDVYRYVRDMGLTAFTNLKIKHPTYCYEMNMVVLSAPAVESELSPRGGEFEMMPLGVNKSPLPKEPPRKDPPPKDPVIETIRNYFPETWIWDLVTVNSSGVTEVEMTVPDTITEWKAGALCLSNDTGLGLSSVATLQAFQPFFVELTMPYSVIRGEAFMLKATVMNYLPTSLPMAVQLEASPDFTAVPVGNDQDSYCLGANGRHTSSWLVTPKSLGNVNFSVSVEAQQSPELCGSQVATVPETGRKDTVVKVLIVEPEGIKKEHTFSSLLCASDAELSETLSLLLPPTVVKDSARAHFSVMGDILSSAIKNTQNLIQMPYGCGEQNMVLFAPNIYVLKYLNETQQLTEKIKSKALGYLRAGYQRELNYKHKDGSYSAFGDHNGQGQGNTWLTAFVLKSFAQARAFIFIDESHITDAFTWLSKQQKDSGCFRSSGSLFNNAMKGGVDDEITLSAYITMALLESSLPDTDPVVSKALGCLEASWETIEQGRNGSFVYTKTLMAYAFALAGNQEKRNEILKSLDKEAIREDNSIHWERPQKPTKSEGYLYTPQASSAEVEMSAYVVLARLTAQPAPSPEDLALSMGTIKWLTKQQNSHGGFSSTQDTVVALDALSKYGAATFSKSQKTPLVTIQSSGSFSQKFQVDNSNRLLLQQVSLPDIPGNYTVSVSGEGCVYAQTTLRYNMPLEKQQPAFALKVQTVPLTCNNPKGQNSFQISLEISYTGSRPASNMVIADVKMLSGFIPLKPTVKKLERLEHVSRTEVTTNNVLLYLDQVTNQTLSFSFIIQQDIPVKNLQPAIVKVYDYYETDEVAFAEYSSPCSSDKQNV |
Enzyme Length | 1487 |
Uniprot Accession Number | Q03626 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective. {ECO:0000305}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (1); Chain (1); Cross-link (1); Disulfide bond (10); Glycosylation (13); Region (1); Sequence conflict (2); Signal peptide (1) |
Keywords | Acute phase;Alternative splicing;Bait region;Disulfide bond;Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal;Thioester bond |
Interact With | |
Induction | INDUCTION: Expression level in the liver as well as protein level in plasma down-regulated by up to 70% during acute inflammation or tumor development. {ECO:0000269|PubMed:1709877, ECO:0000269|PubMed:2511184}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2511184}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 22206666; |
Motif | |
Gene Encoded By | |
Mass | 165,326 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |