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

4-243 (N-terminal gasdermin domain)

Relief mechanism

Cleavage

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P85967

Entry ID Method Resolution Chain Position Source
AF-P85967-F1 Predicted AlphaFoldDB

No variants for P85967

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P85967

No associated diseases with P85967

2 regional properties for P85967

Type Name Position InterPro Accession
domain Gasdermin, pore forming domain 4 - 243 IPR040460
domain Gasdermin, PUB domain 279 - 447 IPR041263

Functions

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

4 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
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.

2 GO annotations of biological process

Name Definition
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
Q96QA5 GSDMA Gasdermin-A Homo sapiens (Human) SS
Q8TAX9 GSDMB Gasdermin-B Homo sapiens (Human) EV
Q9BYG8 GSDMC Gasdermin-C Homo sapiens (Human) SS
Q32M21 Gsdma2 Gasdermin-A2 Mus musculus (Mouse) SS
Q5Y4Y6 Gsdma3 Gasdermin-A3 Mus musculus (Mouse) EV
Q8CB12 Gsdmc3 Gasdermin-C3 Mus musculus (Mouse) SS
Q9D8T2 Gsdmd Gasdermin-D Mus musculus (Mouse) SS
Q9EST1 Gsdma Gasdermin-A Mus musculus (Mouse) SS
Q3TR54 Gsdmc4 Gasdermin-C4 Mus musculus (Mouse) SS
Q99NB5 Gsdmc Gasdermin-C Mus musculus (Mouse) SS
Q2KHK6 Gsdmc2 Gasdermin-C2 Mus musculus (Mouse) SS
10 20 30 40 50 60
MLYTFDQVSK DVVKKLQGKD LRPVRCLSDA TKFRQFDILQ KTPQSLFFKS EDTPVGYSLL
70 80 90 100 110 120
QILEPNFPVP ETEVSAPMPL KHITSQKWKA DVDVKATIAD GGASAEFVQS CGYDIEVQSR
130 140 150 160 170 180
SIPDSKLESL QNRQGPWGKL LDKKLSFVTD CQMGRNNLYV VTEVFEVTKD TVVQGSSSID
190 200 210 220 230 240
LSGKALVSQL VKGEAQGQWQ RETTDLVPIP KGAVLAYKKK QLVIENNTCA ILLSANAKKK
250 260 270 280 290 300
TFPGIFNFGM SSRSQTMEIV NSSWIDYIPP IGRIEEPVHL DFKYLEKEVF LRKEQLAMLS
310 320 330 340 350 360
KDVQDVVFSN LLPMLSDSDV LFDLINMLEL DQLGHMDGPA GLILDELRKN SSTPWIDLKG
370 380 390 400 410 420
LILYLLQALM VLSDTQLDLL AQSMEMRILL QQRELVRSIL EPNFKYPWNI PFTLQPQLLA
430 440 450 460 470
PLQGEGLAIT YELLKGCGLK MEPNSPRSTW DLEAKMPLSA LYGILSCLQQ LVEA