Gsdmd
entrez
69146
canonical
uniprot
Q9D8T2
canonical
ensembl
ENSMUSG00000022575
resolver
ensp
ENSMUSP00000023238
resolver
enst
ENSMUST00000023238
resolver
genesymbol
Gsdmd
resolver
genesymbol_syn
GsdmD-1
resolver
genesymbol_syn
Gsdmdc1
resolver
uniprot
A0A679AXP3
resolver
uniprot
Q3TBD9
resolver
uniprot_entry
A0A679AXP3_MOUSE
resolver
uniprot_entry
GSDMD_MOUSE
resolver
uniprot_sec
Q3TBD9
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:26375259, PubMed:26611636, PubMed:29576317, PubMed:31097341). The intrinsic pyroptosis-inducing activity is carried by the released N-terminal moiety (Gasdermin-D, N-terminal) following cleavage by inflammatory caspases CASP1, CASP4/CASP11 or CASP8 (PubMed:26375003, PubMed:26375259, PubMed:26611636, PubMed:30361383, PubMed:30381458, PubMed:32553275, PubMed:32554464). Cleavage at Asp-88 by CASP3 or CASP7 inactivates the ability to mediate pyroptosis (By similarity). Pore formation is specifically inhibited by VHH(GSDMD-1) nanobody, protecting against excessive pyroptosis (PubMed:38632402). Inhibited by small molecule NU6300, which covalently reacts with Cys-191, thereby preventing palmitoylation and pyroptosis (PubMed:38324683). {ECO:0000250|UniProtKB:P57764, ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636, ECO:0000269|PubMed:29576317, ECO:0000269|PubMed:30361383, ECO:0000269|PubMed:30381458, ECO:0000269|PubMed:31097341, ECO:0000269|PubMed:32553275, ECO:0000269|PubMed:32554464, ECO:0000269|PubMed:38324683, ECO:0000269|PubMed:38632402}.
uniprot
proteins
amino_acid_sequence
MPSAFEKVVKNVIKEVSGSRGDLIPVDSLRNSTSFRPYCLLNRKFSSSRFWKPRYSCVNLSIKDILEPSAPEPEPECFGSFKVSDVVDGNIQGRVMLSGMGEGKISGGAAVSDSSSASMNVCILRVTQKTWETMQHERHLQQPENKILQQLRSRGDDLFVVTEVLQTKEEVQITEVHSQEGSGQFTLPGALCLKGEGKGHQSRKKMVTIPAGSILAFRVAQLLIGSKWDILLVSDEKQRTFEPSSGDRKAVGQRHHGLNVLAALCSIGKQLSLLSDGIDEEELIEAADFQGLYAEVKACSSELESLEMELRQQILVNIGKILQDQPSMEALEASLGQGLCSGGQVEPLDGPAGCILECLVLDSGELVPELAAPIFYLLGALAVLSETQQQLLAKALETTVLSKQLELVKHVLEQSTPWQEQSSVSLPTVLLGDCWDEKNPTWVLLEECGLRLQVESPQVHWEPTSLIPTSALYASLFLLSSLGQKPC
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:26611636, PubMed:27383986, PubMed:27385778, PubMed:27418190). 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:26611636, PubMed:27383986, PubMed:27385778, PubMed:27418190). {ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636, ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27385778, ECO:0000269|PubMed:27418190}.; FUNCTION: [Gasdermin-D, N-terminal]: Promotes pyroptosis in response to microbial infection and danger signals (PubMed:26375003, PubMed:26375259, PubMed:26611636, PubMed:27383986, PubMed:27385778, PubMed:27418190, PubMed:32820063, PubMed:34289345, PubMed:35705808, PubMed:37988464, PubMed:38530158, PubMed:38538834, PubMed:38632402). Produced by the cleavage of gasdermin-D by inflammatory caspases CASP1 or CASP4/CASP11 in response to canonical, as well as non-canonical (such as cytosolic LPS) inflammasome activators (PubMed:26375003, PubMed:26375259, PubMed:26611636, PubMed:27383986, PubMed:27385778, PubMed:27418190, PubMed:35705808, PubMed:38632402). 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:27339137, PubMed:27383986). 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:27383986, PubMed:29195811, PubMed:29274245, PubMed:33883744, PubMed:38530158, PubMed:38538834). Gasdermin pores also allow the release of mature caspase-7 (CASP7) (PubMed:35705808). 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:38632402). Also forms pores in the mitochondrial membrane, resulting in release of mitochondrial DNA (mtDNA) into the cytosol (PubMed:37001519). 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:27383986). Under cell culture conditions, also active against intracellular bacteria, such as Listeria monocytogenes (PubMed:27383986). Also active in response to MAP3K7/TAK1 inactivation by Yersinia toxin YopJ, which triggers cleavage by CASP8 and subsequent activation (PubMed:30361383, PubMed:30381458). Required for mucosal tissue defense against enteric pathogens (PubMed:37988464). Activation of the non-canonical inflammasome in brain endothelial cells can lead to excessive pyroptosis, leading to blood-brain barrier breakdown (PubMed:38632402). Strongly binds to bacterial and mitochondrial lipids, including cardiolipin. Does not bind to unphosphorylated phosphatidylinositol, phosphatidylethanolamine nor phosphatidylcholine (PubMed:27383986). {ECO:0000250|UniProtKB:P57764, ECO:0000269|PubMed:26375003, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636, ECO:0000269|PubMed:27339137, ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27385778, ECO:0000269|PubMed:27418190, ECO:0000269|PubMed:29195811, ECO:0000269|PubMed:29274245, ECO:0000269|PubMed:30361383, ECO:0000269|PubMed:30381458, ECO:0000269|PubMed:32820063, ECO:0000269|PubMed:33883744, ECO:0000269|PubMed:34289345, ECO:0000269|PubMed:35705808, ECO:0000269|PubMed:37001519, ECO:0000269|PubMed:37988464, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38538834, ECO:0000269|PubMed:38632402}.; FUNCTION: [Gasdermin-D, p13]: Transcription coactivator produced by the cleavage by CASP3 or CASP7 in the upper small intestine in response to dietary antigens (PubMed:37327784). 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 (PubMed:37327784). {ECO:0000269|PubMed:37327784}.; 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:35749514, PubMed:35794369). {ECO:0000269|PubMed:35749514, ECO:0000269|PubMed:35794369}.
uniprot
proteins
mass_dalton
53238
uniprot
proteins
mutagenesis
MUTAGEN 7..14; /note="KVVKNVIK->AVVANVIA: Reduced ability to induct pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 17..20; /note="SGSR->DGS: Renders Gsdmd susceptible to ubiquitination by S.flexneri IpaH7.8."; /evidence="ECO:0000269|PubMed:36599845"; MUTAGEN 29; /note="L->A: Reduced homoolimerization, leading to reduced ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 39; /note="C->A: Loss of oligomerization of Gasdermin-D, N-terminal."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 43..54; /note="RKFSSSRFWKPR->AAFSSSRFWAPA: Reduced ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 50..51; /note="FW->GG: Abolished ability to form a pore, leading to educed ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341, ECO:0000269|PubMed:33883744"; MUTAGEN 57; /note="C->A: No effect on oligomerization."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 60; /note="L->G: Reduced homoolimerization, leading to reduced ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 77; /note="C->A: No effect on oligomerization."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 81; /note="F->D: Reduced homoolimerization, leading to reduced ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 85..88; /note="DVVD->AAAA: Abolished cleavage by CASP3 and CASP7."; /evidence="ECO:0000269|PubMed:37327784"; MUTAGEN 91; /note="I->D: Reduced homoolimerization, leading to reduced ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 95; /note="V->D: Reduced homoolimerization, leading to reduced ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 105; /note="I->N: Reduced ability to induce pyroptosis. No effect on protein expression. No effect on cleavage by CASP4."; /evidence="ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:29576317"; MUTAGEN 122; /note="C->A: No effect on oligomerization."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 138; /note="R->A,S: Complete loss of homooligomerization, lipid-binding, relocalization of Gasdermin-D, N-terminal to the plasma membrane and pyroptosis, as well as loss of bactericidal activity; when associated with A-146; A-152 and A-154. Partial loss of homooligomerization and pyroptosis; when associated with A-146."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 146; /note="K->A: Complete loss of homooligomerization, lipid-binding, relocalization of Gasdermin-D, N-terminal to the plasma membrane and pyroptosis, as well as loss of bactericidal activity; when associated with A-138 or with S-138; A-152 and A-154. Partial loss of homooligomerization and pyroptosis; when associated with A-138, with A-152 or with A-152 and A-154."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 152; /note="R->A: Complete loss of homooligomerization, lipid-binding, relocalization of Gasdermin-D, N-terminal to the plasma membrane and pyroptosis, as well as loss of bactericidal activity; when associated with A-138 or with S-138; A-146 and A-154. Partial loss of homooligomerization and pyroptosis; when associated with A-146 or with A-154, or with A-146 and A-154."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 154; /note="R->A: Complete loss of homooligomerization, lipid-binding, relocalization of Gasdermin-D, N-terminal to the plasma membrane and pyroptosis, as well as loss of bactericidal activity; when associated with A-138 or with S-138; A-146 and A-152. Partial loss of homooligomerization and pyroptosis; when associated with A-152 or with A-146 and A-152."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 192; /note="C->A: Loss of oligomerization of Gasdermin-D, N-terminal. Abolished palmitoylation and ability to form a pore and mediate pyroptosis."; /evidence="ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:32820063, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38538834"; MUTAGEN 193; /note="L->D: Reduced homoolimerization, leading to reduced ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 230..233; /note="ILLV->ALLA: Reduced homoolimerization, leading to reduced ability to induce pyroptosis."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 237; /note="K->A: No effect on pyroptosis; when associated with A-239 or with A-239; A-248 and A-249."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 239; /note="R->A: No effect on pyroptosis; when associated with A-237 or with A-237; A-248 and A-249."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 248; /note="R->A: No effect on pyroptosis; when associated with A-237; A-239 and A-249."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 249; /note="K->A: No effect on pyroptosis; when associated with A-237; A-239 and A-248."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 265; /note="C->A: No effect on oligomerization."; /evidence="ECO:0000269|PubMed:27383986"; MUTAGEN 273; /note="L->A: Impaired interaction and cleavage by CASP1."; /evidence="ECO:0000269|PubMed:32553275"; MUTAGEN 276; /note="D->A,N: Loss of CASP1-induced cleavage, pyroptosis and IL1B release. Does not impair interaction with CASP1. Loss of CASP4/CASP11-induced cleavage. Abolished ability to induce pyroptosis following inactivation of MAP3K7/TAK1 by Yersinia toxin YopJ."; /evidence="ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636, ECO:0000269|PubMed:30135078, ECO:0000269|PubMed:30361383, ECO:0000269|PubMed:32553275, ECO:0000269|PubMed:38538834"; MUTAGEN 292; /note="L->D: Disrupts intramolecular interactions and autoinhibition, leading to spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 295; /note="E->R: Disrupts intramolecular interactions and autoinhibition, leading to spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 306..310; /note="LEMEL->AEMEA: In 5A mutant; abolished interaction with CASP1; when associated with 361-L--L370."; /evidence="ECO:0000269|PubMed:32553275"; MUTAGEN 309..313; /note="ELRQQ->AAAAA: Abolished generation of the Gasdermin-D, p40 chain and ability to promote secretion of IL33."; /evidence="ECO:0000269|PubMed:35794369"; MUTAGEN 309..313; /note="Missing: Abolished generation of the Gasdermin-D, p40 chain and ability to promote secretion of IL33."; /evidence="ECO:0000269|PubMed:35794369"; MUTAGEN 361..370; /note="LDSGELVPEL->ADSGELAPEA: In 5A mutant; abolished interaction with CASP1; when associated with 306-L--L310."; /evidence="ECO:0000269|PubMed:32553275"; MUTAGEN 369; /note="E->K: Impaired interaction and cleavage by CASP1."; /evidence="ECO:0000269|PubMed:32553275"; MUTAGEN 376; /note="Y->D: Spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:29576317"; MUTAGEN 380; /note="A->D: Disrupts intramolecular interactions and autoinhibition, leading to spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 470; /note="S->R: Disrupts intramolecular interactions and autoinhibition, leading to spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:31097341"; MUTAGEN 474; /note="A->D: Disrupts intramolecular interactions and autoinhibition, leading to spontaneous pyroptosis-inducing activity."; /evidence="ECO:0000269|PubMed:31097341
uniprot
proteins
post_translational_modification
PTM: Cleavage at Asp-276 by CASP1 (mature and uncleaved precursor forms), CASP4/CASP11 or CASP8 relieves autoinhibition and is sufficient to initiate pyroptosis (PubMed:26375259, PubMed:26611636, PubMed:32553275, PubMed:32554464). Cleavage by CASP1 and CASP4/CASP11 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:32553275, PubMed:32554464). Cleavage by CASP8 takes place following inactivation of MAP3K7/TAK1 by Yersinia toxin YopJ (PubMed:30361383, PubMed:30381458). Cleavage at Asp-88 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:37327784). Cleavage by papain allergen generates the Gasdermin-D, p40 chain (PubMed:35794369). {ECO:0000250|UniProtKB:P57764, ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:26611636, ECO:0000269|PubMed:30361383, ECO:0000269|PubMed:30381458, ECO:0000269|PubMed:32553275, ECO:0000269|PubMed:32554464, ECO:0000269|PubMed:35794369, ECO:0000269|PubMed:37327784}.; PTM: [Gasdermin-D]: Palmitoylated at Cys-192 by ZDHHC5 and ZDHHC9 in response to microbial infection and danger signals (PubMed:38324683, PubMed:38530158, PubMed:38599239). May also be palmitoylated by ZDHHC7 (PubMed:38538834). 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:38538834, PubMed:38599239). Depalmitoylated by LYPLA2 (PubMed:38538834). {ECO:0000269|PubMed:38324683, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38538834, ECO:0000269|PubMed:38599239}.; PTM: [Gasdermin-D]: Succination of Cys-192 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: [Gasdermin-D, N-terminal]: Ubiquitinated by TRAF1/TRAF2 complex at Lys-237 via 'Lys-63'-linked polyubiquitin chains; leading to pyroptosis activity. {ECO:0000250|UniProtKB:P57764}.; PTM: Glycosylated: O-GlcNAcylation by OGT leads to reduced cleavage by CASP4 and decreased LPS-induced endothelial cell pyroptosis. {ECO:0000250|UniProtKB:P57764}.
uniprot
proteins
protein_family
Gasdermin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18693275
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26375003
uniprot
proteins
pubmed
26375259
uniprot
proteins
pubmed
26611636
uniprot
proteins
pubmed
27339137
uniprot
proteins
pubmed
27383986
uniprot
proteins
pubmed
27385778
uniprot
proteins
pubmed
27418190
uniprot
proteins
pubmed
29195811
uniprot
proteins
pubmed
29274245
uniprot
proteins
pubmed
29576317
uniprot
proteins
pubmed
30135078
uniprot
proteins
pubmed
30361383
uniprot
proteins
pubmed
30381458
uniprot
proteins
pubmed
31097341
uniprot
proteins
pubmed
32109412
uniprot
proteins
pubmed
32553275
uniprot
proteins
pubmed
32554464
uniprot
proteins
pubmed
32820063
uniprot
proteins
pubmed
33883744
uniprot
proteins
pubmed
34289345
uniprot
proteins
pubmed
35705808
uniprot
proteins
pubmed
35749514
uniprot
proteins
pubmed
35794369
uniprot
proteins
pubmed
36227980
uniprot
proteins
pubmed
36599845
uniprot
proteins
pubmed
37001519
uniprot
proteins
pubmed
37327784
uniprot
proteins
pubmed
37988464
uniprot
proteins
pubmed
38324683
uniprot
proteins
pubmed
38530158
uniprot
proteins
pubmed
38538834
uniprot
proteins
pubmed
38599239
uniprot
proteins
pubmed
38632402
uniprot
proteins
sequence_length
487
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Gasdermin-D]: Cytoplasm, cytosol {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190}. Inflammasome {ECO:0000269|PubMed:26611636}. 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:0000269|PubMed:26611636}.; SUBCELLULAR LOCATION: [Gasdermin-D, N-terminal]: Cell membrane {ECO:0000269|PubMed:27339137, ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:27418190, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38538834}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P57764}. Secreted {ECO:0000269|PubMed:27383986}. Mitochondrion membrane {ECO:0000269|PubMed:37001519}. Note=Released in the extracellular milieu following pyroptosis (PubMed:27383986). Mitochondrial localization results in release of mitochondrial DNA into the cytosol (PubMed:37001519). {ECO:0000269|PubMed:27383986, ECO:0000269|PubMed:37001519}.; 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:0000269|PubMed:37327784}.; SUBCELLULAR LOCATION: [Gasdermin-D, C-terminal]: Cytoplasm, cytosol {ECO:0000305|PubMed:27339137}.
uniprot
proteins
transmembrane_region
TRANSMEM 92..98; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P57764"; TRANSMEM 104..109; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P57764"; TRANSMEM 181..187; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P57764"; TRANSMEM 192..198; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P57764
uniprot
proteins