Descriptions

Gasdermin proteins are a pore-forming protein causing membrane permeabilization and pyroptosis, and functions downstream of the inflammatory caspases. The C-terminal gasdermin domain may adopt an intramolecular complex with the N-terminal domain, which may inhibit the activation of the N-terminal gasdermin domain as observed in GSDMD.

Autoinhibitory domains (AIDs)

Target domain

3-233 (N-terminal gasdermin domain)

Relief mechanism

Cleavage

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q32M21

Entry ID Method Resolution Chain Position Source
AF-Q32M21-F1 Predicted AlphaFoldDB

48 variants for Q32M21

Variant ID(s) Position Change Description Diseaes Association Provenance
rs244620717 2 S>P No Ensembl
rs244620717 2 S>T No Ensembl
rs580388776 6 D>N No Ensembl
rs264762506 12 A>V No Ensembl
rs229266266 14 Q>E No Ensembl
rs259542803 18 R>Q No Ensembl
rs582900366 28 I>M No Ensembl
rs27059399 55 R>H No Ensembl
rs246204601 123 T>M No Ensembl
rs27059396 147 Y>H No Ensembl
rs217322197 167 K>T No Ensembl
rs239673342 199 K>M No Ensembl
rs247077233 211 I>M No Ensembl
rs257156978 212 I>V No Ensembl
rs582088992 217 E>K No Ensembl
rs261745273 221 P>S No Ensembl
rs218555340 222 Y>H No Ensembl
rs235464998 227 N>S No Ensembl
rs251461635 233 P>H No Ensembl
rs220582463 236 V>M No Ensembl
rs27059387 237 L>P No Ensembl
rs27059386 241 G>A No Ensembl
rs222694239 244 V>A No Ensembl
rs240799727 246 M>K No Ensembl
rs264867708 247 I>L No Ensembl
rs581724432 258 L>I No Ensembl
rs582645519 260 K>E No Ensembl
rs578382460 262 V>I No Ensembl
rs211960638 264 Q>R No Ensembl
rs252528260 300 M>T No Ensembl
rs579847012 309 H>Q No Ensembl
rs583582660 312 T>I No Ensembl
rs261457578 323 L>S No Ensembl
rs587346533 326 A>P No Ensembl
rs222363488 349 V>I No Ensembl
rs579182722 358 P>L No Ensembl
rs246546055 358 P>S No Ensembl
rs255158090 378 D>G No Ensembl
rs240549416 383 R>Q No Ensembl
rs259500555 392 E>K No Ensembl
rs231650341 394 D>E No Ensembl
rs248853320 395 Q>L No Ensembl
rs582636828 403 G>E No Ensembl
rs231066910 419 N>D No Ensembl
rs216479573 423 C>R No Ensembl
rs228626841 426 L>V No Ensembl
rs585312092 440 S>G No Ensembl
rs27059365 441 R>K No Ensembl

1 associated diseases with Q32M21

Without disease ID

8 regional properties for Q32M21

Type Name Position InterPro Accession
domain AGC-kinase, C-terminal 357 - 425 IPR000961
domain Pleckstrin homology domain 1150 - 1351 IPR001849
active_site Serine/threonine-protein kinase, active site 210 - 222 IPR008271
domain HR1 rho-binding domain 497 - 573 IPR011072
domain ROCK, Rho binding domain 978 - 1047 IPR015008
binding_site Protein kinase, ATP binding site 98 - 121 IPR017441
domain Rho-associated protein kinase 2, catalytic domain 39 - 417 IPR029878
domain Rho-associated protein kinase 2, HR1 domain 505 - 571 IPR037311

Functions

Description
EC Number
Subcellular Localization
  • [Gasdermin-A2]: Cytoplasm, perinuclear region
  • Cytoplasm, cytosol
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
phosphatidylinositol-4,5-bisphosphate binding Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
phosphatidylinositol-4-phosphate binding Binding to phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position.
phosphatidylserine binding Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine.

3 GO annotations of biological process

Name Definition
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
defense response to bacterium Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
pyroptosis A caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P57764 GSDMD Gasdermin-D Homo sapiens (Human) EV
Q9BYG8 GSDMC Gasdermin-C Homo sapiens (Human) SS
Q96QA5 GSDMA Gasdermin-A Homo sapiens (Human) SS
Q8TAX9 GSDMB Gasdermin-B Homo sapiens (Human) EV
Q8CB12 Gsdmc3 Gasdermin-C3 Mus musculus (Mouse) SS
Q2KHK6 Gsdmc2 Gasdermin-C2 Mus musculus (Mouse) SS
Q3TR54 Gsdmc4 Gasdermin-C4 Mus musculus (Mouse) SS
Q99NB5 Gsdmc Gasdermin-C Mus musculus (Mouse) SS
Q9D8T2 Gsdmd Gasdermin-D Mus musculus (Mouse) SS
Q5Y4Y6 Gsdma3 Gasdermin-A3 Mus musculus (Mouse) EV
Q9EST1 Gsdma Gasdermin-A Mus musculus (Mouse) SS
P85967 Gsdmc Gasdermin-C Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MSMFEDVTRA LARQLNPRGD LTPLDSLIDF KRFHPFCLVL RKRKSTLFWG ARYVRTDYTL
70 80 90 100 110 120
LDVLEPGSSP SDPTLLGNFS FKNMLDVRVE GDVEVPTMMK VKGTVGLSQS STLEVQMLSV
130 140 150 160 170 180
APTALENLHM ERKLSADHPF LKEMREYKQN LYVVMEVVKA KQEVTLKRAS NAISKFSLNL
190 200 210 220 230 240
PSLGLQGSVN HKEAVTIPKG CVLAYRVRQL IIYGKDEWGI PYICTDNMPT FNPLCVLQRQ
250 260 270 280 290 300
GSTVQMISGE MHEDFKTLKK EVQQETQEVE KLSPVGRSSL LTSLSHLLGK KKELQDLEQM
310 320 330 340 350 360
LEGALDKGHE VTLEALPKDV LLLKDAMDAI LYFLGALTEL SEEQLKILVK SLENKVLPVQ
370 380 390 400 410 420
LKLVESILEQ NFLQDKEDVF PLRPDLLSSL GEEDQILTEA LVGLSGLEVQ RSGPQYTWNP
430 440
DTCHNLCALY AGLSLLHLLS RDS