RCD11_NEUCR
ID RCD11_NEUCR Reviewed; 257 AA.
AC Q7SBA0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Gasdermin-like protein rcd-1-1 {ECO:0000305};
DE AltName: Full=Regulator of cell death 1-1 {ECO:0000303|PubMed:31636083};
GN Name=rcd-1-1 {ECO:0000303|PubMed:31636083};
GN ORFNames=NCU05712 {ECO:0000312|EMBL:EAA33662.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP 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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF
RP 129-ARG--LYS-134; ARG-129 AND 147-LYS--LYS-149.
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
CC (this entry) and rcd-1-2 (AC P0DW10) (PubMed:31636083). During the
CC allorecognition process, forms a heterooligomer with rcd-1-2, 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-1-2 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 1-2 (PubMed:32703806). Forms a gasdermin-like pore that associates with
CC the cell membrane in the presence of rcd-1-2 (PubMed:32703806).
CC {ECO:0000269|PubMed:32703806}.
CC -!- SIMILARITY: Belongs to the gasdermin family. {ECO:0000305}.
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DR EMBL; CM002238; EAA33662.1; -; Genomic_DNA.
DR RefSeq; XP_962898.1; XM_957805.2.
DR EnsemblFungi; EAA33662; EAA33662; NCU05712.
DR GeneID; 3879056; -.
DR KEGG; ncr:NCU05712; -.
DR VEuPathDB; FungiDB:NCU05712; -.
DR HOGENOM; CLU_081916_0_0_1; -.
DR InParanoid; Q7SBA0; -.
DR OMA; VWFKLRQ; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0022829; F:wide pore channel activity; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Necrosis; Reference proteome;
KW Transmembrane; Transmembrane beta strand.
FT CHAIN 1..257
FT /note="Gasdermin-like protein rcd-1-1"
FT /id="PRO_0000455981"
FT MUTAGEN 129..134
FT /note="RSYVQK->ASYVQA: Impaired localization to the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:32703806"
FT MUTAGEN 129
FT /note="R->A: Impaired localization to the cell membrane.
FT Abolished localization to the cell membrane; when
FT associated with A-147--149-A."
FT /evidence="ECO:0000269|PubMed:32703806"
FT MUTAGEN 147..149
FT /note="KNK->ANA: Abolished localization to the cell
FT membrane; when associated with A-129."
FT /evidence="ECO:0000269|PubMed:32703806"
SQ SEQUENCE 257 AA; 28778 MW; 1D55ABB754D044E6 CRC64;
MDKCWFTLDN AHYPPPSLDS MRSGHPISPA SLGHLIPSLA HLDQIINAKA IEPFPATMDI
HGPTIIEDFK WDHSHEYSLS LGGKVPIPLA PAGVPFVDLN VGLGGAFSRS VANYWEFDRL
ERYIMQPTRS YVQKCIERDE VKRWIAKNKS MMMMGRWEVY MITGIIVARG GGRKKKEKTT
GKEFSVEVTV EVPLIVEAGP GGKRNTARQK TWGTSQTGDF VWAVRLAKIT KSGLHSDWKM
ETVFGKTSSF RGQKAIF
