Gzmb
entrez
171528
canonical
uniprot
P18291
canonical
ensembl
ENSRNOG00000049976
resolver
ensembl
ENSRNOG00055012185
resolver
ensembl
ENSRNOG00060017012
resolver
ensembl
ENSRNOG00065031090
resolver
ensp
ENSRNOP00000075556
resolver
ensp
ENSRNOP00055016714
resolver
ensp
ENSRNOP00060023430
resolver
ensp
ENSRNOP00065044053
resolver
enst
ENSRNOT00000083961
resolver
enst
ENSRNOT00055020726
resolver
enst
ENSRNOT00060029104
resolver
enst
ENSRNOT00065053603
resolver
genesymbol
Gzmb
resolver
uniprot_entry
GRAB_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inactivated by the serine protease inhibitor diisopropylfluorophosphate. {ECO:0000250|UniProtKB:P10144}.
uniprot
proteins
amino_acid_sequence
MKLLLLLLSFSLAPKTEAGEIIGGHEAKPHSRPYMAYLQIMDEYSGSKKCGGFLIREDFVLTAAHCSGSKINVTLGAHNIKEQEKMQQIIPVVKIIPHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKCESYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKKVAAGIVSYGQNDGSTPRAFTKVSTFLSWIKKTMKKS
uniprot
proteins
ec_number
3.4.21.79
uniprot
proteins
function
FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (By similarity). It cleaves after Asp (PubMed:9765264). Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death (By similarity). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution (By similarity). Cleaves caspase-3 and -9 (CASP3 and CASP9, respectively) to give rise to active enzymes mediating apoptosis (PubMed:9765264). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity). {ECO:0000250|UniProtKB:P04187, ECO:0000250|UniProtKB:P10144, ECO:0000269|PubMed:9765264}.
uniprot
proteins
mass_dalton
27326
uniprot
proteins
mutagenesis
MUTAGEN 102; /note="N->Q: Decreased secretion without affecting the protease activity."; /evidence="ECO:0000269|PubMed:9765264"; MUTAGEN 229; /note="R->A: Does not affect the protease activity."; /evidence="ECO:0000269|PubMed:9765264"; MUTAGEN 229; /note="R->E: Decreased activity for acidic amino acids at position P3, whereas the activity against basic amino is increased."; /evidence="ECO:0000269|PubMed:9765264
uniprot
proteins
protein_family
Granzyme subfamily
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10966646
uniprot
proteins
pubmed
1727874
uniprot
proteins
pubmed
1732416
uniprot
proteins
pubmed
2307850
uniprot
proteins
pubmed
9765264
uniprot
proteins
sequence_length
248
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9765264}. Cytolytic granule {ECO:0000250|UniProtKB:P10144}. Note=Delivered into the target cell by perforin. {ECO:0000250|UniProtKB:P10144}.
uniprot
proteins