ID   RCD12_NEUCS             Reviewed;         244 AA.
AC   P0DW10;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=Gasdermin-like protein rcd-1-2 {ECO:0000305};
DE   AltName: Full=Regulator of cell death 1-2 {ECO:0000303|PubMed:31636083};
GN   Name=rcd-1-2 {ECO:0000303|PubMed:31636083};
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=31636083; DOI=10.1534/genetics.119.302617;
RA   Daskalov A., Gladieux P., Heller J., Glass N.L.;
RT   "Programmed Cell Death in Neurospora crassa Is Controlled by the
RT   Allorecognition Determinant rcd-1.";
RL   Genetics 213:1387-1400(2019).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=32703806; DOI=10.1073/pnas.2004876117;
RA   Daskalov A., Mitchell P.S., Sandstrom A., Vance R.E., Glass N.L.;
RT   "Molecular characterization of a fungal gasdermin-like protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 117:18600-18607(2020).
CC   -!- FUNCTION: Gasdermin-like protein involved in heterokaryon
CC       incompatibility, a process that ensures that during spontaneous
CC       vegetative cell fusion, only compatible cells from the same colony
CC       survive (non-self-recognition) (PubMed:31636083, PubMed:32703806). In
CC       N.crassa, the rcd-1 locus exists as 2 incompatible alleles, rcd-1-1 (AC
CC       Q7SBA0) and rcd-1-2 (this entry) (PubMed:31636083). During the
CC       allorecognition process, forms a heterooligomer with rcd-1-1, thereby
CC       forming a functional gasdermin-like complex that binds to membranes and
CC       forms pores, triggering cell death (PubMed:32703806). Binds negatively
CC       charged phospholipids, such as cardiolipin and phosphatidylserine
CC       (PubMed:32703806). Also binds to phosphoinositides, preferentially to
CC       phosphatidylinositol-3-phosphate (PtdIns-3-P), PtdIns-5-P and PtdIns-
CC       3,5-P2 (PubMed:32703806). {ECO:0000269|PubMed:31636083,
CC       ECO:0000269|PubMed:32703806}.
CC   -!- SUBUNIT: Heterooligomer; the heterooligomer with rcd-1-1 forms a ring-
CC       shaped pore complex when inserted in the membrane.
CC       {ECO:0000269|PubMed:32703806}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32703806}. Cell
CC       membrane {ECO:0000269|PubMed:32703806}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P57764}. Note=Cytoplasmic in the absence of rcd-
CC       1-1 (PubMed:32703806). Forms a gasdermin-like pore that associates with
CC       the cell membrane in the presence of rcd-1-1 (PubMed:32703806).
CC       {ECO:0000269|PubMed:32703806}.
CC   -!- SIMILARITY: Belongs to the gasdermin family. {ECO:0000305}.
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PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Membrane; Necrosis; Transmembrane;
KW   Transmembrane beta strand.
FT   CHAIN           1..244
FT                   /note="Gasdermin-like protein rcd-1-2"
FT                   /id="PRO_0000455982"
SQ   SEQUENCE   244 AA;  27188 MW;  1D4D17EE0E11DD29 CRC64;
     MDNEEWFPLK QTHYPPPTIP SMKTGHPTGP ISIGHIIPDL RHLDNVINCK GFEPFPPNMD
     VFTAHYEQCH FGDHLNSEFV VQAKAAAPIK NIVPGVDVTG SAGLHHTNIT SDRWEYDSVV
     EYAVYPTRQY IDRLLESKEV KQYIQKSKKL LGGWCVYMVT GIMVARGGGR NVVSEEKGAG
     VFGNVGFQVP GIGEXAPEVG WDTKTKTKVN AHHTTDFVCA IRLVKIAKSG LRSSWTMKKV
     TREF