Detail Information for IndEnz0002013955
IED ID IndEnz0002013955
Enzyme Type ID protease013955
Protein Name Alpha-1-macroglobulin
Alpha-1-M
Alpha-1-macroglobulin 165 kDa subunit

Cleaved into: Alpha-1-macroglobulin 45 kDa subunit
Gene Name A1m Pzp
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 MRRNQLPIPVFLLLLLLLPRDATAATGKPRYVVLVPSELYAGVPEKVCVHLNHLNETVTLNVTLEYGVQYSNLLIDQAVDKDSSYCSSFTISRPLSPSALIAVEIKGPTHHFIKKKSMWITKAESPVFVQTDKPIYKPGQTVKFRVVSVDISFRPVNETFPVVYIENPKRNRIFQWQNVDLPGGLHQLSFPLSVEPALGIYKVVVQKDSGKKIEHSFEVKEYVLPKFEVQVKMPKTMAFLEEELVVTACGLYTYGKPVPGLVTMKVCRKYTQSYSNCHGQHSKSICEEFSKQADEKGCFRQVVKTKVFQPRQKGYDMKIEVEAKIKEDGTGIELTGTGSCEIANTLSKLKFTKANTFYRPGLPFFGQVLLVDEKGQPIPNKNLTVQVNSVRSQFTFTTDEHGLANILIDTTNFTFSFMGIRVIYKQNNICFDNWWVDEYHTQADHSAARIFSPSRSYIQLELVLGTLACGQTQEIRIHFLLNEDALKDAKDLTFYYLIKARGSIFNSGSHVLPLEQGKVKGVVSFPIRVEPGMAPVAKLIVYTILPNEELIADVQKFDIEKCFANTVNLSFPSAQSLPASDTHLTVKATPLSLCALTAVDQSVLLLKPEAKLSPQSIYNLLPQKAEQGAYLGPLPYKGGENCIKAEDITHNGIVYTPKQDLNDNDAYSVFQSIGLKIFTNTRVHKPRYCPMYQAYPPLPYVGEPQALAMSAIPGAGYRSSNIRTSSMMMMGASEVAQEVEVRETVRKYFPETWIWDMVPLDLSGDGELPVKVPDTITEWKASAFCLSGTTGLGLSSTISHKVFQPFFLELTLPYSVVRGEAFILKATVLNYMPHCIRIHVSLEMSPDFLAVPVGSHEDSHCICGNERKTVSWAVTPKSLGEVNFTATAEALQSPELCGNKVAEVPALVQKDTVVKPVIVEPEGIEKEQTYNTLLCPQDAELQENWTLDLPANVVEGSARATQSVLGDILGSAMQNLQNLLQMPYGCGEQNMVLFVPNIYVLEYLNETQQLTEAIKSKAISYLISGYQRQLNYQHSDGSYSTFGDRGMRHSQGNTWLTAFVLKAFAQAQSYIYIEKTHITNAFNWLSMKQRENGCFQQSGSLLNNAMKGGVDDEVTLSAYITIALLEMPLPVTHSVVRNALFCLETAWASISNSQESHVYTKALLAYAFALAGNRAKRSEVLESLNKDAVNEEESVHWQRPKNVEENVREMRSFSYKPRAPSAEVEMTAYVLLAYLTSASSRPTRDLSSSDLTTASKIVKWISKQQNSHGGFSSTQDTVVALQALSKYGAATFTKSNKEVSVTIESSGTVSGTLHVNNGNRLLLQEVRLADLPGNYITKVSGSGCVYLQTSLKYNILPEAEGEAPFTLKVNTLPLNFDKAEHHRKFQIHINVSYIGERPNSNMVIVDVKMVSGFIPVKPSVKKLQDQSNIQRTEVNTNHVLIYIEKLTNQTMGFSFAVEQDIPVKNLKPAPVKVYDYYETDEFAIEEYSAPFSSDSEQGNA
Enzyme Length 1500
Uniprot Accession Number Q63041
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). {ECO:0000250|UniProtKB:P01023}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (10); Chain (2); Cross-link (1); Disulfide bond (12); Glycosylation (11); Helix (2); Region (2); Sequence conflict (3); Signal peptide (1); Turn (1)
Keywords 3D-structure;Bait region;Direct protein sequencing;Disulfide bond;Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal;Thioester bond
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1725450}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000269|PubMed:1725450
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1EDY;
Mapped Pubmed ID 11813239; 18301350; 19119138; 22206666; 2470410;
Motif
Gene Encoded By
Mass 167,125
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda