IED ID |
IndEnz0002015978 |
Enzyme Type ID |
protease015978 |
Protein Name |
Murinoglobulin-2
|
Gene Name |
Mug2 |
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 |
MWKNREAQLCLFSVLLAFLPSASLLFGNSKYMVLVPSQLYTETPEKICLHLYHLNETVTVTASLISQRGTRKLFDEPVVDKDLFHCVSFIPRLPSSEEEESLDINIEGAKHKFSKRHVVLVKNKESVVFVQTDKPMYKPGQSVKFRVVSMDKNLYPLKELVQDPKMNRIMQWQDVKTENGLKQLSFSLSAEPIQGPYKIVVLKQSGVKEEHSFTVMEFVLPRFGVDVKVPNAISVYDEIISVTACDRYTYGKPVLGRVKVRLCHGNPSFSSETKSACKEENSQLDNNGCSTQEVNITEFQLKENYLKVRQAFHVNATVTEEGTGMEFGGYGRIEVERTRNKFLFLKADSHFRHGIPFFVKVRLVDIKGDPIPNEQVFIKAQEAGYTNATTTDQHGLAKFSIDTSSISGYSLNIKVYHKEENLCIHSSCTAERHAEAHHTAYAVYSLSKSYIYLDTEAGVLPCNQIHTVQAHFILKGQVLGVLPQIVFHYLVMAQGSILQTGNHTHQVESGAPVQGNFALEIPVEFSMVPMAKMLIYTILPDGEVIADSVKFQVEKCLRNKVHLSFSPSQSLPASQTHMRVTASPQSLCGLRAVDQSVLLLRPEAELSPSLIYDLPGMQDSNFIPRSHHPFEDEDDCLMYQPRDTEELTYSVPYGREKDVYRYVDMGLTAFTNLKIKHPTYCYDLPKEPPRKDPPRKDPEPKDTVVETIRNYFPETWVWDLVTVSSSGVTEVEMTVPDTITEWKAGALCLSNDTGLGLSSVATLQAFQPFFVELTMPYSVIRGEAFTLKATVMNYLPTSLQMTVQLEASPDFTAVPVGNDQDSYCLGANGRHTSSWLVTPKSLGNVNFSVSVEAQQSPEPCGSEVATVPETGRKDTVIKVLIVEPEGIKKEHTFSSLLCASDAELSETLSLLLPPRVVKDSARAHFSVMGDILSSAIKNTQNLIQMPYGCGEQNMVLFAPNIYVLKYLNETQQLTENIKSKALGYLRAGYQRELNYKHKDGSYSAFGDHNGQGQGNTWLTAFVLKSFAQARAFIFIDESHITDAFTWLSKQQKDSGCFRSSGSLFNNAMKGGVDDEITLSAYITMALLESSLPPVVSKALGCLEASWETIEQGRNGSFVYTKALMAYAFTLAGNQEKRNEILKSLDKEAIKEDNSIHWERPQKPMKSEHYLYTPQASSVEVEMSAYVVLARLTAHPAPSPEDLALSTGTIKWLTKQQNSHGGFSSTQDTVVALDALSKYGAATFSKSQKTPSVTVQSSGSFSQKFQVDKSNRLLLQQVSLPDIPGNYTIRVSGEGCVYAQTTLRYNLPLEKQQPAFALKVKTVPLTCNNPKGQNSFQISLEISYTGSRPASNMVIADVKMLSGFIPLKPTVKKLERLEHVSRTEVTTNNVLLYLDQVTNQTLSFSFIIQQDIPVKNLQPAIVKVYDYYETDEVAFAEYSSPCSSDKQNV |
Enzyme Length |
1448 |
Uniprot Accession Number |
Q6IE52 |
Absorption |
|
Active Site |
|
Activity Regulation |
|
Binding Site |
|
Calcium Binding |
|
catalytic Activity |
|
DNA Binding |
|
EC Number |
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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 |
Chain (1); Cross-link (1); Disulfide bond (10); Glycosylation (11); Region (1); Signal peptide (1) |
Keywords |
Bait region;Direct protein sequencing;Disulfide bond;Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal;Thioester bond |
Interact With |
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Induction |
|
Subcellular Location |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue |
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Post Translational Modification |
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Signal Peptide |
SIGNAL 1..24; /evidence=ECO:0000255 |
Structure 3D |
|
Cross Reference PDB |
- |
Mapped Pubmed ID |
- |
Motif |
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Gene Encoded By |
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Mass |
161,589 |
Kinetics |
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Metal Binding |
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Rhea ID |
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Cross Reference Brenda |
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