位置:首页 > 蛋白库 > HETQ1_PODAN
HETQ1_PODAN
ID   HETQ1_PODAN             Reviewed;         278 AA.
AC   B2AXJ5;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Gasdermin-like protein het-Q1 {ECO:0000305};
DE   AltName: Full=Heterokaryon incompatibility protein Q1 {ECO:0000303|PubMed:35135876};
DE   Contains:
DE     RecName: Full=Gasdermin-like protein het-Q1, N-terminal {ECO:0000305};
GN   Name=het-Q1 {ECO:0000303|PubMed:35135876};
GN   ORFNames=PODANS_7_10775 {ECO:0000312|EMBL:CAP69119.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [3]
RP   FUNCTION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF GLY-234; LYS-235;
RP   VAL-236; LEU-237; PHE-238; GLY-240 AND GLY-241.
RX   PubMed=35135876; DOI=10.1073/pnas.2109418119;
RA   Clave C., Dyrka W., Turcotte E.A., Granger-Farbos A., Ibarlosa L.,
RA   Pinson B., Vance R.E., Saupe S.J., Daskalov A.;
RT   "Fungal gasdermin-like proteins are controlled by proteolytic cleavage.";
RL   Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
CC   -!- FUNCTION: [Gasdermin-like protein het-Q1]: Gasdermin-like protein
CC       involved in heterokaryon incompatibility, a process that ensures that
CC       during spontaneous vegetative cell fusion, only compatible cells from
CC       the same colony survive (non-self-recognition) (PubMed:35135876). In
CC       P.anserina, the het-q locus exists as 2 incompatible alleles, het-Q1
CC       (this entry) and het-Q2 (AC P0DW09) (PubMed:35135876). This form
CC       constitutes the precursor of the pore-forming protein: during the
CC       allorecognition process, it is cleaved by het-Q2, releasing the N-
CC       terminal moiety (Gasdermin-like protein het-Q1, N-terminal) that binds
CC       to membranes and forms pores, triggering cell death (PubMed:35135876).
CC       {ECO:0000269|PubMed:35135876}.
CC   -!- FUNCTION: [Gasdermin-like protein het-Q1, N-terminal]: Pore-forming
CC       protein that causes membrane permeabilization and cell death
CC       (PubMed:35135876). Released upon cleavage and maturation by het-Q2 and
CC       binds to membrane inner leaflet lipids (PubMed:35135876).
CC       Homooligomerizes within the membrane and forms pores of 10-15
CC       nanometers (nm) of inner diameter, triggering cell death (By
CC       similarity). {ECO:0000250|UniProtKB:P57764,
CC       ECO:0000269|PubMed:35135876}.
CC   -!- SUBUNIT: [Gasdermin-like protein het-Q1, N-terminal]: Homooligomer;
CC       forms a homooligomeric ring-shaped pore complex when inserted in the
CC       membrane. {ECO:0000250|UniProtKB:P57764}.
CC   -!- SUBCELLULAR LOCATION: [Gasdermin-like protein het-Q1, N-terminal]: Cell
CC       membrane {ECO:0000250|UniProtKB:P57764}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P57764}.
CC   -!- PTM: [Gasdermin-like protein het-Q1]: The precursor form is cleaved by
CC       het-Q2, generating the pore-forming protein (Gasdermin-like protein
CC       het-Q1, N-terminal). {ECO:0000269|PubMed:35135876}.
CC   -!- SIMILARITY: Belongs to the gasdermin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU633900; CAP69119.1; -; Genomic_DNA.
DR   EMBL; FO904942; CDP32598.1; -; Genomic_DNA.
DR   RefSeq; XP_001908446.1; XM_001908411.1.
DR   EnsemblFungi; CAP69119; CAP69119; PODANS_7_10775.
DR   GeneID; 6192626; -.
DR   KEGG; pan:PODANSg5481; -.
DR   VEuPathDB; FungiDB:PODANS_7_10775; -.
DR   eggNOG; ENOG502T8QF; Eukaryota.
DR   HOGENOM; CLU_1001576_0_0_1; -.
DR   OrthoDB; 1535722at2759; -.
DR   Proteomes; UP000001197; Chromosome 7.
DR   GO; GO:0022829; F:wide pore channel activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Necrosis; Reference proteome; Transmembrane;
KW   Transmembrane beta strand.
FT   CHAIN           1..278
FT                   /note="Gasdermin-like protein het-Q1"
FT                   /id="PRO_0000455983"
FT   CHAIN           1..237
FT                   /note="Gasdermin-like protein het-Q1, N-terminal"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000455984"
FT   SITE            237..238
FT                   /note="Cleavage; by het-Q2"
FT                   /evidence="ECO:0000269|PubMed:35135876"
FT   MUTAGEN         234
FT                   /note="G->A: Does not affect ability to trigger cell death
FT                   during the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
FT   MUTAGEN         235
FT                   /note="K->A: Does not affect ability to trigger cell death
FT                   during the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
FT   MUTAGEN         236
FT                   /note="V->A: Does not affect ability to trigger cell death
FT                   during the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
FT   MUTAGEN         237
FT                   /note="L->A: Abolished cleavage by het-Q2 and ability to
FT                   trigger cell death during the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
FT   MUTAGEN         238
FT                   /note="F->A: Abolished cleavage by het-Q2 and ability to
FT                   trigger cell death during the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
FT   MUTAGEN         240
FT                   /note="G->A: Does not affect ability to trigger cell death
FT                   during the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
FT   MUTAGEN         241
FT                   /note="G->A: Does not affect ability to trigger cell death
FT                   during the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
SQ   SEQUENCE   278 AA;  29695 MW;  FA3AF64A213952A9 CRC64;
     MPTKTSQHAF AGSERWVVPR YSSKPGTLIR LGSVLTDPED LESSLNLDSI PPIPPHLLRD
     ATPEVRMSVQ TELSKSDSTL AKAAPALEGI LTLGGGVEAS RSQGVSSSLN ISGTVKATVF
     RADKSYMDVL LKDKNVISYA KRGLGKPMFV VVGVATAGRV EMKETRHVTR KAGVSGKVGV
     EVIGEGEVGL ERERSDKSCN EVRGEGGLDF AYRVREFGYS RVRGTVKDKG DWTGKVLFAG
     GKGPVVEKGG EVVPVFKEFK EGEVKLRATG SFDVAAKA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024