GSDMD
entrez
79792
canonical
uniprot
P57764
canonical
ensembl
ENSG00000104518
resolver
ensembl
ENSG00000278718
resolver
ensp
ENSP00000262580
resolver
ensp
ENSP00000433209
resolver
ensp
ENSP00000482096
resolver
ensp
ENSP00000488012
resolver
ensp
ENSP00000536688
resolver
ensp
ENSP00000536689
resolver
ensp
ENSP00000536690
resolver
ensp
ENSP00000536691
resolver
ensp
ENSP00000536692
resolver
ensp
ENSP00000587360
resolver
ensp
ENSP00000587361
resolver
ensp
ENSP00000637767
resolver
ensp
ENSP00000637768
resolver
ensp
ENSP00000637769
resolver
ensp
ENSP00000637770
resolver
enst
ENST00000262580
resolver
enst
ENST00000526406
resolver
enst
ENST00000615119
resolver
enst
ENST00000631751
resolver
enst
ENST00000866629
resolver
enst
ENST00000866630
resolver
enst
ENST00000866631
resolver
enst
ENST00000866632
resolver
enst
ENST00000866633
resolver
enst
ENST00000917301
resolver
enst
ENST00000917302
resolver
enst
ENST00000967708
resolver
enst
ENST00000967709
resolver
enst
ENST00000967710
resolver
enst
ENST00000967711
resolver
genesymbol
GSDMD
resolver
genesymbol_syn
DFNA5L
resolver
genesymbol_syn
GSDMDC1
resolver
hgnc
HGNC:25697
resolver
uniprot
A8K702
resolver
uniprot
D3DWJ9
resolver
uniprot
Q96Q98
resolver
uniprot_entry
GSDMD_HUMAN
resolver
uniprot_sec
A8K702
resolver
uniprot_sec
D3DWJ9
resolver
uniprot_sec
Q96Q98
resolver
activity_regulation
ACTIVITY REGULATION: [Gasdermin-D]: The full-length protein before cleavage is inactive: intramolecular interactions between N- and C-terminal domains mediate autoinhibition in the absence of activation signal (PubMed:26375003, PubMed:28928145, PubMed:29576317, PubMed:32109412). The intrinsic pyroptosis-inducing activity is carried by the released N-terminal moiety (Gasdermin-D, N-terminal) following cleavage by caspases CASP1, CASP4, CASP5 or CASP8 (PubMed:26375003, PubMed:26375259, PubMed:27418190, PubMed:29898893, PubMed:32109412). Cleavage at Asp-87 by CASP3 or CASP7 inactivates the ability to mediate pyroptosis (PubMed:28392147). Homooligomerization and pore formation is specifically inhibited by VHH(GSDMD-1) and, to a lesser extent, VHH(GSDMD-2) nanobodies, protecting against excessive pyroptosis (PubMed:38040708). Inhibited by small molecule NU6300, which covalently reacts with Cys-191, thereby preventing palmitoylation and pyroptosis (PubMed:38324683). {ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:27418190, ECO:0000269|PubMed:28392147, ECO:0000269|PubMed:28928145, ECO:0000269|PubMed:29576317, ECO:0000269|PubMed:29898893, ECO:0000269|PubMed:32109412, ECO:0000269|PubMed:38040708, ECO:0000269|PubMed:38324683}.
uniprot
proteins
amino_acid_sequence
MGSAFERVVRRVVQELDHGGEFIPVTSLQSSTGFQPYCLVVRKPSSSWFWKPRYKCVNLSIKDILEPDAAEPDVQRGRSFHFYDAMDGQIQGSVELAAPGQAKIAGGAAVSDSSSTSMNVYSLSVDPNTWQTLLHERHLRQPEHKVLQQLRSRGDNVYVVTEVLQTQKEVEVTRTHKREGSGRFSLPGATCLQGEGQGHLSQKKTVTIPSGSTLAFRVAQLVIDSDLDVLLFPDKKQRTFQPPATGHKRSTSEGAWPQLPSGLSMMRCLHNFLTDGVPAEGAFTEDFQGLRAEVETISKELELLDRELCQLLLEGLEGVLRDQLALRALEEALEQGQSLGPVEPLDGPAGAVLECLVLSSGMLVPELAIPVVYLLGALTMLSETQHKLLAEALESQTLLGPLELVGSLLEQSAPWQERSTMSLPPGLLGNSWGEGAPAWVLLDECGLELGEDTPHVCWEPQAQGRMCALYASLALLSGLSQEPH
uniprot
proteins
function
FUNCTION: [Gasdermin-D]: Precursor of a pore-forming protein that plays a key role in host defense against pathogen infection and danger signals (PubMed:26375003, PubMed:26375259, PubMed:27281216). This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-D, N-terminal) binds to membranes and forms pores, triggering pyroptosis (PubMed:26375003, PubMed:26375259, PubMed:27281216, PubMed:39673710, PubMed:40118151). {ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:39673710, ECO:0000269|PubMed:40118151}.; FUNCTION: [Gasdermin-D, N-terminal]: Promotes pyroptosis in response to microbial infection and danger signals (PubMed:26375003, PubMed:26375259, PubMed:27418190, PubMed:28392147, PubMed:32820063, PubMed:34289345, PubMed:38040708, PubMed:38530158, PubMed:38599239). Produced by the cleavage of gasdermin-D by inflammatory caspases CASP1, CASP4 or CASP5 in response to canonical, as well as non-canonical (such as cytosolic LPS) inflammasome activators (PubMed:26375003, PubMed:26375259, PubMed:27418190). After cleavage, moves to the plasma membrane where it strongly binds to inner leaflet lipids, including monophosphorylated phosphatidylinositols, such as phosphatidylinositol 4-phosphate, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-bisphosphate, and more weakly to phosphatidic acid and phosphatidylserine (PubMed:27281216, PubMed:29898893, PubMed:36227980). Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature interleukin-1 (IL1B and IL18) and triggering pyroptosis (PubMed:27281216, PubMed:27418190, PubMed:29898893, PubMed:33883744, PubMed:38040708, PubMed:38530158, PubMed:38599239). Gasdermin pores also allow the release of mature caspase-7 (CASP7) (By similarity). In some, but not all, cells types, pyroptosis is followed by pyroptotic cell death, which is caused by downstream activation of ninjurin-1 (NINJ1), which mediates membrane rupture (cytolysis) (PubMed:33472215, PubMed:37198476). Also forms pores in the mitochondrial membrane, resulting in release of mitochondrial DNA (mtDNA) into the cytosol (By similarity). Gasdermin-D, N-terminal released from pyroptotic cells into the extracellular milieu rapidly binds to and kills both Gram-negative and Gram-positive bacteria, without harming neighboring mammalian cells, as it does not disrupt the plasma membrane from the outside due to lipid-binding specificity (PubMed:27281216). Under cell culture conditions, also active against intracellular bacteria, such as Listeria monocytogenes (By similarity). Also active in response to MAP3K7/TAK1 inactivation by Yersinia toxin YopJ, which triggers cleavage by CASP8 and subsequent activation (By similarity). Required for mucosal tissue defense against enteric pathogens (By similarity). Activation of the non-canonical inflammasome in brain endothelial cells can lead to excessive pyroptosis, leading to blood-brain barrier breakdown (By similarity). Strongly binds to bacterial and mitochondrial lipids, including cardiolipin (PubMed:27281216). Does not bind to unphosphorylated phosphatidylinositol, phosphatidylethanolamine nor phosphatidylcholine (PubMed:27281216). {ECO:0000250|UniProtKB:Q9D8T2, ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:27418190, ECO:0000269|PubMed:28392147, ECO:0000269|PubMed:29898893, ECO:0000269|PubMed:32820063, ECO:0000269|PubMed:33472215, ECO:0000269|PubMed:33883744, ECO:0000269|PubMed:34289345, ECO:0000269|PubMed:36227980, ECO:0000269|PubMed:37198476, ECO:0000269|PubMed:38040708, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38599239, ECO:0000269|PubMed:40097387}.; FUNCTION: [Gasdermin-D, p13]: Transcription coactivator produced by the cleavage by CASP3 or CASP7 in the upper small intestine in response to dietary antigens (By similarity). Required to maintain food tolerance in small intestine: translocates to the nucleus and acts as a coactivator for STAT1 to induce the transcription of CIITA and MHC class II molecules, which in turn induce type 1 regulatory T (Tr1) cells in upper small intestine (By similarity). {ECO:0000250|UniProtKB:Q9D8T2}.; FUNCTION: [Gasdermin-D, p40]: Produced by the cleavage by papain allergen (PubMed:35794369). After cleavage, moves to the plasma membrane and homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the specific release of mature interleukin-33 (IL33), promoting type 2 inflammatory immune response (PubMed:35794369). {ECO:0000269|PubMed:35794369}.
uniprot
proteins
mass_dalton
52801
uniprot
proteins
mutagenesis
MUTAGEN 7..11; /note="RVVRR->AVVAA: Impaired pore-formation."; /evidence="ECO:0000269|PubMed:29695864"; MUTAGEN 15; /note="E->K: No spontaneous pyroptosis-inducing activity; when associated with D-192."; /evidence="ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:28928145"; MUTAGEN 16..22; /note="LDHGGEF->VSGSRGD: Abolished ubiquitination by S.flexneri IpaH7.8."; /evidence="ECO:0000269|PubMed:36991125"; MUTAGEN 42..53; /note="RKPSSSWFWKPR->EEPSSSWFWEPE: Abolished ability to form a pore."; /evidence="ECO:0000269|PubMed:33883744"; MUTAGEN 48..50; /note="WFW->GFG: Abolished ability to form a pore."; /evidence="ECO:0000269|PubMed:33883744"; MUTAGEN 63..73; /note="DILEPDAAEPD->AILAPDAAAPA: In AP1; promotes ability to release of interleukin-1 (IL1B and IL18) precursors."; /evidence="ECO:0000269|PubMed:33883744"; MUTAGEN 87..95; /note="DGQIQGSVE->AGQIQGSVA: In AP2; promotes ability to release of interleukin-1 (IL1B and IL18) precursors."; /evidence="ECO:0000269|PubMed:33883744"; MUTAGEN 104; /note="I->N: Decreased effectiveness in pore formation and pyroptosis induction. No effect on cleavage by CASP1."; /evidence="ECO:0000269|PubMed:27418190"; MUTAGEN 174; /note="R->E: Reduced ability to form a pore."; /evidence="ECO:0000269|PubMed:33883744"; MUTAGEN 191; /note="C->A: Abolished palmitoylation and ability to form a pore and mediate pyroptosis. Prevents binding to small molecule NU6300."; /evidence="ECO:0000269|PubMed:38324683, ECO:0000269|PubMed:38599239"; MUTAGEN 192; /note="L->D: Decreased induction of pyroptosis and defects in liposome-binding. No spontaneous pyroptosis-inducing activity; when associated with K-15."; /evidence="ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:28928145, ECO:0000269|PubMed:36227980"; MUTAGEN 193; /note="Q->A: Abolished cleavage by enterovirus 71 (EV71) Protease 3C and human coronavirus SARS-CoV-2 3C-like proteinase nsp5."; /evidence="ECO:0000269|PubMed:28679757, ECO:0000269|PubMed:35594856"; MUTAGEN 204; /note="K->E: Reduced ability to form a pore."; /evidence="ECO:0000269|PubMed:33883744"; MUTAGEN 234; /note="D->K: Does not affect ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 235; /note="K->D: Does not affect ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 236; /note="K->D: Does not affect ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 236; /note="K->R: Fails to mediate pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 237; /note="Q->D: Does not affect ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 238; /note="R->D: Does not affect ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 239; /note="T->D: Abolished ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 240; /note="F->D: Abolished ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 241; /note="Q->D: Does not affect ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 242; /note="P->D: Does not affect ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 243; /note="P->D: Does not affect ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 272..274; /note="FLT->AAA: Does not affect interaction with CASP4."; /evidence="ECO:0000269|PubMed:32109412"; MUTAGEN 275; /note="D->A: Loss of cleavage by CASP1 and CASP4 and of LPS-induced pyroptosis. Does not affect interaction with CASP1 and CASP4."; /evidence="ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:32109412, ECO:0000269|PubMed:38599239"; MUTAGEN 277..296; /note="VPAEGAFTEDFQGLRAEVET->SGGGS: Constitutively active mutant; promotes activation of pyroptosis."; /evidence="ECO:0000269|PubMed:28928145"; MUTAGEN 283; /note="F->A,R: Constitutively active mutant; promotes activation of pyroptosis."; /evidence="ECO:0000269|PubMed:28928145"; MUTAGEN 283; /note="F->Y: No effect."; /evidence="ECO:0000269|PubMed:28928145"; MUTAGEN 288..291; /note="QGLR->AAA: Abolished generation of the Gasdermin-D, p40 chain and ability to promote secretion of IL33."; /evidence="ECO:0000269|PubMed:35794369"; MUTAGEN 290; /note="L->D: Spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:27281216"; MUTAGEN 304..308; /note="LDREL->ADREA: Impairs interaction with CASP1 and CASP4 and subsequent cleavage."; /evidence="ECO:0000269|PubMed:32109412"; MUTAGEN 335; /note="Q->A: Does not affect cleavage by enterovirus 71 (EV71) Protease 3C."; /evidence="ECO:0000269|PubMed:28679757"; MUTAGEN 338; /note="S->A: Abolished O-GlcNAcylation, leading to increased association with CASP4."; /evidence="ECO:0000269|PubMed:37962578"; MUTAGEN 364..367; /note="VPEL->APEA: Impairs interaction with CASP1 and CASP4 and subsequent cleavage."; /evidence="ECO:0000269|PubMed:32109412"; MUTAGEN 373; /note="Y->D: Spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:27281216"; MUTAGEN 377; /note="A->D: Spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:27281216
uniprot
proteins
post_translational_modification
PTM: Cleavage at Asp-275 by CASP1 (mature and uncleaved precursor forms), CASP4, CASP5 or CASP8 relieves autoinhibition and is sufficient to initiate pyroptosis (PubMed:26375003, PubMed:29898893, PubMed:32109412). Cleavage by CASP1 and CASP4 is not strictly dependent on the consensus cleavage site on GSDMD but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (PubMed:32109412). Cleavage by CASP8 takes place following inactivation of MAP3K7/TAK1 by Yersinia toxin YopJ (By similarity). Cleavage at Asp-87 by CASP3 or CASP7 inactivates the ability to mediate pyroptosis, but generates the Gasdermin-D, p13 chain, which translocates to the nucleus and acts as a transcription regulator (PubMed:28045099, PubMed:28392147, PubMed:37327784). Cleavage by papain allergen generates the Gasdermin-D, p40 chain (PubMed:35794369). {ECO:0000250|UniProtKB:Q9D8T2, ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:28045099, ECO:0000269|PubMed:28392147, ECO:0000269|PubMed:29898893, ECO:0000269|PubMed:32109412, ECO:0000269|PubMed:35794369, ECO:0000269|PubMed:37327784}.; PTM: [Gasdermin-D, N-terminal]: Ubiquitinated by TRAF1/TRAF2 complex at Lys-236 via 'Lys-63'-linked polyubiquitin chains; leading to pyroptosis activity. {ECO:0000269|PubMed:40097387}.; PTM: [Gasdermin-D]: Palmitoylated at Cys-191 by ZDHHC5 and ZDHHC9 in response to microbial infection and danger signals (PubMed:38324683, PubMed:38530158, PubMed:38599239). Palmitoylation takes place before cleavage by caspases (CASP1, CASP4, CASP5 or CASP8) and is required for membrane translocation and pore formation (PubMed:38324683, PubMed:38530158, PubMed:38599239). Depalmitoylated by LYPLA2 (By similarity). {ECO:0000250|UniProtKB:Q9D8T2, ECO:0000269|PubMed:38324683, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38599239}.; PTM: [Gasdermin-D]: Succination of Cys-191 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits processing by caspases, and ability to initiate pyroptosis (PubMed:32820063). Succination modification is catalyzed by a non-enzymatic reaction caused by an accumulation of fumarate (PubMed:32820063). {ECO:0000269|PubMed:32820063}.; PTM: Glycosylated: O-GlcNAcylation by OGT leads to reduced cleavage by CASP4 and decreased LPS-induced endothelial cell pyroptosis. {ECO:0000269|PubMed:37962578}.; PTM: (Microbial infection) Cleaved and inactivated by Protease 3C from Human enterovirus 71 (EV71), preventing GSDMD-mediated pyroptosis. {ECO:0000269|PubMed:28679757}.; PTM: (Microbial infection) Cleaved and inactivated at Leu-28 by the 3C-like proteinase nsp5 from human coronavirus SARS-CoV-2, preventing GSDMD-mediated pyroptosis (PubMed:35594856, PubMed:39673710, PubMed:40118151). The 3C-like proteinase nsp5 from human coronavirus SARS-CoV-2 also cleaves and activates GSDMD at His-270 and Asp-275, thereby promoting unconventional secretion of the viral nucleocapsid through gasdermin pores into the host extracellular space (PubMed:39673710). {ECO:0000269|PubMed:35594856, ECO:0000269|PubMed:39673710, ECO:0000269|PubMed:40118151}.; PTM: (Microbial infection) Ubiquitinated by S.flexneri IpaH7.8, leading to its degradation by the proteasome. {ECO:0000269|PubMed:34492225, ECO:0000269|PubMed:36599845, ECO:0000269|PubMed:36991122, ECO:0000269|PubMed:36991125}.
uniprot
proteins
protein_family
Gasdermin family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15289881
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19051310
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26375003
uniprot
proteins
pubmed
26375259
uniprot
proteins
pubmed
27281216
uniprot
proteins
pubmed
27418190
uniprot
proteins
pubmed
28045099
uniprot
proteins
pubmed
28392147
uniprot
proteins
pubmed
28679757
uniprot
proteins
pubmed
28928145
uniprot
proteins
pubmed
29576317
uniprot
proteins
pubmed
29695864
uniprot
proteins
pubmed
29898893
uniprot
proteins
pubmed
31097341
uniprot
proteins
pubmed
32109412
uniprot
proteins
pubmed
32820063
uniprot
proteins
pubmed
33472215
uniprot
proteins
pubmed
33883744
uniprot
proteins
pubmed
34289345
uniprot
proteins
pubmed
34492225
uniprot
proteins
pubmed
35594856
uniprot
proteins
pubmed
35794369
uniprot
proteins
pubmed
36227980
uniprot
proteins
pubmed
36599845
uniprot
proteins
pubmed
36991122
uniprot
proteins
pubmed
36991125
uniprot
proteins
pubmed
37198476
uniprot
proteins
pubmed
37327784
uniprot
proteins
pubmed
37962578
uniprot
proteins
pubmed
38040708
uniprot
proteins
pubmed
38324683
uniprot
proteins
pubmed
38530158
uniprot
proteins
pubmed
38599239
uniprot
proteins
pubmed
39673710
uniprot
proteins
pubmed
40097387
uniprot
proteins
pubmed
40118151
uniprot
proteins
sequence_length
484
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Gasdermin-D]: Cytoplasm, cytosol {ECO:0000269|PubMed:27281216}. Inflammasome {ECO:0000250|UniProtKB:Q9D8T2}. Note=In response to a canonical inflammasome stimulus, such as nigericin, recruited to NLRP3 inflammasone with similar kinetics to that of uncleaved CASP1 precursor. {ECO:0000250|UniProtKB:Q9D8T2}.; SUBCELLULAR LOCATION: [Gasdermin-D, N-terminal]: Cell membrane {ECO:0000269|PubMed:27281216, ECO:0000269|PubMed:32109412, ECO:0000269|PubMed:33883744, ECO:0000269|PubMed:36227980, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38599239}; Multi-pass membrane protein {ECO:0000269|PubMed:33883744, ECO:0000305|PubMed:29898893}. Secreted {ECO:0000250|UniProtKB:Q9D8T2}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9D8T2}. Note=Released in the extracellular milieu following pyroptosis. {ECO:0000250|UniProtKB:Q9D8T2}.; SUBCELLULAR LOCATION: [Gasdermin-D, N-terminal]: Cytoplasm, cytosol {ECO:0000269|PubMed:36227980}. Note=(Microbial infection) Upon infection by M.tuberculosis, localization to cell membrane is prevented by M.tuberculosis phosphatase PtpB that catalyzes dephosphorylation of phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol 4-phosphate, thereby inhibiting the membrane targeting of Gasdermin-D, N-terminal and subsequent cytokine release and pyroptosis. {ECO:0000269|PubMed:36227980}.; SUBCELLULAR LOCATION: [Gasdermin-D, p13]: Nucleus {ECO:0000250|UniProtKB:Q9D8T2}.; SUBCELLULAR LOCATION: [Gasdermin-D, C-terminal]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9D8T2}.
uniprot
proteins
transmembrane_region
TRANSMEM 91..97; /note="Beta stranded"; /evidence="ECO:0000269|PubMed:33883744, ECO:0007744|PDB:6VFE"; TRANSMEM 103..108; /note="Beta stranded"; /evidence="ECO:0000269|PubMed:33883744, ECO:0007744|PDB:6VFE"; TRANSMEM 180..186; /note="Beta stranded"; /evidence="ECO:0000269|PubMed:33883744, ECO:0007744|PDB:6VFE"; TRANSMEM 191..197; /note="Beta stranded"; /evidence="ECO:0000269|PubMed:33883744, ECO:0007744|PDB:6VFE
uniprot
proteins