A2m
entrez
232345
canonical
uniprot
Q6GQT1
canonical
ensembl
ENSMUSG00000030111
resolver
ensp
ENSMUSP00000032203
resolver
enst
ENSMUST00000032203
resolver
genesymbol
A2m
resolver
genesymbol_syn
A2mp
resolver
uniprot
E9QMQ7
resolver
uniprot
Q811S0
resolver
uniprot_entry
A2MG_MOUSE
resolver
uniprot_sec
E9QMQ7
resolver
uniprot_sec
Q811S0
resolver
amino_acid_sequence
MGKRWLPSLALLPLPPPLLLLLLLLLPTNASAPQKPIYMVMVPSLLHAGTPEKGCLLFNHLNETVTVKVSMESVRGNQSLFTDLVVDKDLFHCASFIVPQSSSNEVMFLTVQVKGPTHEFRRRSTVLIKTKESLVFAQTDKPIYKPGQMVRFRVVSLDENFHPLNELIPLLYIQDSKKNRIAQWQNFRLEGGLKQLSFPLSSEPTQGSYKVVIRTESGRTVEHPFSVKEFVLPKFEVKVAVPETITILEEEMNVSVCGIYTYGKPVPGHVTVNICRKYSNPSSCFGEESLAFCEKFSQQLDGRGCFSQLVKTKSFQLKRQEYEMQLDVNAKIQEEGTGVEETGKGLTKITRTITKLSFVNVDTHFRQGIPFVGQVLLVDGRGTPIPYEMIFIGADEANQNINTTTDKNGLARFSINTDDIMGTSLTVRAKYKDSNVCYGFRWLTEENVEAWHTANAVFSPSRSFVHLESLPYKLRCEQTLAVQAHYILNDEAVLERKELVFYYLMMAKGGIVRAGTHVLPVTQGHKKGHFSILISMETDLAPVARLVLYTILPNGEVVGDTVKYEIEKCLANKVDLVFHPNIGLPATRAFLSVMASPQSLCGLRAVDQSVLLTKPEAELSASLVYDLLPVKDLTGFPKGVNQQEEDTNGCLKQNDTYINGILYSPVQNTNEEDMYGFLKDMGLKVFTNLNIRKPKVCERLGVNKIPAAYHLVSQGHMDAFLESSESPTETTRSYFPETWIWDLVIVDSTGVAEMEVTVPDTITEWKAGAFCLSNDTGLGLSPVIDFQAFQPFFVDLTMPYSVIRGEAFTLKATVLNYLQTCIRVGVQLEASPDFLATPEEKEQKSHCICMNERHTMSWAVIPKSLGNVNFTVSAEALDSKELCRNEVPVVPERGKKDTIIKSLLVEPEGLENEVTFNSLLCPTGAEVSEQISLKLPSDVVEESARASVTVLGDILGSAMQNTQDLLKMPYGCGEQNMVLFAPNIYVLDYLNETEQLTQEIKTKAITYLNTGYQRQLNYKHRDGSYSTFGDKPGRSHANTWLTAFVLKSFAQARRYIFIDESHITQALTWLSQQQKDNGCFRSSGSLLNNAMKGGVEDEVTLSAYITIALLEMSLPVTHPVVRNALFCLDTAWKSARRGASGNHVYTKALLAYAFALAGNQDTKKEILKSLDEEAVKEDNSVHWTRAQKPRVPADLWYQPQAPSAEVEMTAYVLLAYLTTELVPTREDLTAAMLIVKWLTKQQNSHGGFSSTQDTVVALHALSKYGAATFTRAKKAAHVTIQSSGAFYTKFQVNNDNQLLLQRVTLPTVPGDYTAKVAGEGCVYLQTSLKYSVLPREKEFPFALVVQTLPGTCEDLKAHTTFQISLNISYIGSRSDSNMAIADVKMVSGFIPLKPTVKMLERSVHVSRTEVSNNHVLIYLDKVSNQMLTLFFMVQQDIPVRDLKPAIVKVYDYYEKDEFAVAKYSAPCSAGYGNA
uniprot
proteins
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}.
uniprot
proteins
mass_dalton
164353
uniprot
proteins
protein_family
Protease inhibitor I39 (alpha-2-macroglobulin) family
uniprot
proteins
pubmed
15355875
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
sequence_length
1474
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
uniprot
proteins