Prf1
entrez
18646
canonical
uniprot
P10820
canonical
ensembl
ENSMUSG00000037202
resolver
ensp
ENSMUSP00000041483
resolver
ensp
ENSMUSP00000151354
resolver
ensp
ENSMUSP00000234176
resolver
enst
ENSMUST00000035419
resolver
enst
ENSMUST00000219375
resolver
genesymbol
Prf1
resolver
genesymbol_syn
Pfp
resolver
uniprot
A2RSY7
resolver
uniprot_entry
A2RSY7_MOUSE
resolver
uniprot_entry
PERF_MOUSE
resolver
amino_acid_sequence
MATCLFLLGLFLLLPRPVPAPCYTATRSECKQKHKFVPGVWMAGEGMDVTTLRRSGSFPVNTQRFLRPDRTCTLCKNSLMRDATQRLPVAITHWRPHSSHCQRNVAAAKVHSTEGVAREAAANINNDWRVGLDVNPRPEANMRASVAGSHSKVANFAAEKTYQDQYNFNSDTVECRMYSFRLVQKPPLHLDFKKALRALPRNFNSSTEHAYHRLISSYGTHFITAVDLGGRISVLTALRTCQLTLNGLTADEVGDCLNVEAQVSIGAQASVSSEYKACEEKKKQHKMATSFHQTYRERHVEVLGGPLDSTHDLLFGNQATPEQFSTWTASLPSNPGLVDYSLEPLHTLLEEQNPKREALRQAISHYIMSRARWQNCSRPCRSGQHKSSHDSCQCECQDSKVTNQDCCPRQRGLAHLVVSNFRAEHLWGDYTTATDAYLKVFFGGQEFRTGVVWNNNNPRWTDKMDFENVLLSTGGPLRVQVWDADYGWDDDLLGSCDRSPHSGFHEVTCELNHGRVKFSYHAKCLPHLTGGTCLEYAPQGLLGDPPGNRSGAVW
uniprot
proteins
function
FUNCTION: Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells (PubMed:19446473, PubMed:21037563, PubMed:26306037, PubMed:2783478, PubMed:3261391, PubMed:35148176, PubMed:35705808, PubMed:7520535, PubMed:7526382, PubMed:7972104, PubMed:8164737). Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores (PubMed:19446473, PubMed:21037563, PubMed:26306037, PubMed:3261391, PubMed:35148176, PubMed:35705808, PubMed:7526382, PubMed:8164737). Promotes cytolysis and apoptosis of target cells by mediating the passage and uptake of cytotoxic granzymes (PubMed:19446473, PubMed:21037563, PubMed:26306037, PubMed:3261391, PubMed:35148176, PubMed:7526382, PubMed:8164737). Facilitates the delivery of cationic cargo protein, while anionic or neural proteins are not delivered efficiently (By similarity). Perforin pores allow the release of mature caspase-7 (CASP7) into the extracellular milieu (PubMed:35705808). {ECO:0000250|UniProtKB:P14222, ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:26306037, ECO:0000269|PubMed:3261391, ECO:0000269|PubMed:35148176, ECO:0000269|PubMed:35705808, ECO:0000269|PubMed:7520535, ECO:0000269|PubMed:7526382, ECO:0000269|PubMed:7972104, ECO:0000269|PubMed:8164737}.
uniprot
proteins
mass_dalton
62081
uniprot
proteins
mutagenesis
MUTAGEN 191; /note="D->K,V: Loss of cytotoxicity."; /evidence="ECO:0000269|PubMed:19446473"; MUTAGEN 191; /note="D->S: Strongly decreased cytotoxicity."; /evidence="ECO:0000269|PubMed:19446473"; MUTAGEN 213; /note="R->E,L: Strongly decreased cytotoxicity."; /evidence="ECO:0000269|PubMed:19446473"; MUTAGEN 343; /note="E->R: Strongly decreased cytotoxicity."; /evidence="ECO:0000269|PubMed:19446473"; MUTAGEN 427..430; /note="WGDY->AGDA: Abolished lipid-binding and pore formation; when associated with 486-A--A-488."; /evidence="ECO:0000269|PubMed:26306037"; MUTAGEN 429; /note="D->N: Abolished binding of the weakest calcium-binding site, leading to impaired interaction with lipid membranes."; /evidence="ECO:0000269|PubMed:26306037"; MUTAGEN 435; /note="D->N: Abolished binding of the weakest calcium-binding site, leading to impaired interaction with lipid membranes."; /evidence="ECO:0000269|PubMed:26306037"; MUTAGEN 483; /note="D->N: Abolished binding of the weakest calcium-binding site, leading to impaired interaction with lipid membranes."; /evidence="ECO:0000269|PubMed:26306037"; MUTAGEN 486..488; /note="YGW->AGA: Abolished lipid-binding and pore formation; when associated with 427-A--A-430."; /evidence="ECO:0000269|PubMed:26306037"; MUTAGEN 490; /note="D->N: Does not affect interaction with lipid membranes."; /evidence="ECO:0000269|PubMed:26306037"; MUTAGEN 491; /note="D->N: Decreased calcium-binding."; /evidence="ECO:0000269|PubMed:26306037
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. The glycosylation sites are facing the interior of the pore. {ECO:0000269|PubMed:21037563}.
uniprot
proteins
protein_family
Complement C6/C7/C8/C9 family
uniprot
proteins
pubmed
1401900
uniprot
proteins
pubmed
19446473
uniprot
proteins
pubmed
2040805
uniprot
proteins
pubmed
21037563
uniprot
proteins
pubmed
2303785
uniprot
proteins
pubmed
26306037
uniprot
proteins
pubmed
2783478
uniprot
proteins
pubmed
2783486
uniprot
proteins
pubmed
2783549
uniprot
proteins
pubmed
3190678
uniprot
proteins
pubmed
3261391
uniprot
proteins
pubmed
35148176
uniprot
proteins
pubmed
35705808
uniprot
proteins
pubmed
7520535
uniprot
proteins
pubmed
7526382
uniprot
proteins
pubmed
7972104
uniprot
proteins
pubmed
8164737
uniprot
proteins
sequence_length
554
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytolytic granule {ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:8164737}. Secreted {ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:3261391}. Cell membrane {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:35148176}; Multi-pass membrane protein {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:35148176}. Endosome lumen {ECO:0000250|UniProtKB:P14222}. Note=Released from cytotoxic lymphocytes, together with proapoptotic granzymes: stored in cytolytic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell (PubMed:2040805, PubMed:8164737). May be taken up via endocytosis involving clathrin-coated vesicles and accumulate in a first time in large early endosomes (By similarity). Inserts into the cell membrane of target cells and forms pores (PubMed:19446473, PubMed:21037563). Membrane insertion and pore formation requires a major conformation change (PubMed:19446473, PubMed:21037563). {ECO:0000250|UniProtKB:P14222, ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:8164737}.
uniprot
proteins
transmembrane_region
TRANSMEM 128..148; /note="Beta stranded; Name=CH1"; /evidence="ECO:0000305|PubMed:21037563"; TRANSMEM 256..278; /note="Beta stranded; Name=CH2"; /evidence="ECO:0000305|PubMed:21037563
uniprot
proteins