HETS_PODAN
ID HETS_PODAN Reviewed; 289 AA.
AC B2ACC7; A0A090CFF4; Q1K9D3;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Heterokaryon incompatibility protein S;
DE AltName: Full=Big S protein;
DE AltName: Full=Vegetative incompatibility protein S;
GN Name=het-S; Synonyms=big S; OrderedLocusNames=Pa_3_620;
GN ORFNames=PODANS_3_620;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=1886611; DOI=10.1007/bf00282475;
RA Turcq B., Deleu C., Denayrolles M., Begueret J.;
RT "Two allelic genes responsible for vegetative incompatibility in the fungus
RT Podospora anserina are not essential for cell viability.";
RL Mol. Gen. Genet. 228:265-269(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF HIS-33.
RC STRAIN=D, S / ATCC MYA-4624 / DSM 980 / FGSC 10383, U, and X;
RX PubMed=8224826; DOI=10.1093/genetics/135.1.45;
RA Deleu C., Clave C., Begueret J.;
RT "A single amino acid difference is sufficient to elicit vegetative
RT incompatibility in the fungus Podospora anserina.";
RL Genetics 135:45-52(1993).
RN [3]
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 [4]
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 [5]
RP PRION IDENTIFICATION, FUNCTION, AND INTERACTION WITH HET-S.
RX PubMed=9275200; DOI=10.1073/pnas.94.18.9773;
RA Coustou V., Deleu C., Saupe S., Begueret J.;
RT "The protein product of the het-s heterokaryon incompatibility gene of the
RT fungus Podospora anserina behaves as a prion analog.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9773-9778(1997).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=15159455; DOI=10.1242/jcs.01116;
RA Balguerie A., Dos Reis S., Coulary-Salin B., Chaignepain S., Sabourin M.,
RA Schmitter J.M., Saupe S.J.;
RT "The sequences appended to the amyloid core region of the HET-s prion
RT protein determine higher-order aggregate organization in vivo.";
RL J. Cell Sci. 117:2599-2610(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-227, AND DOMAIN.
RX PubMed=20620958; DOI=10.1016/j.molcel.2010.05.019;
RA Greenwald J., Buhtz C., Ritter C., Kwiatkowski W., Choe S., Maddelein M.L.,
RA Ness F., Cescau S., Soragni A., Leitz D., Saupe S.J., Riek R.;
RT "The mechanism of prion inhibition by HET-S.";
RL Mol. Cell 38:889-899(2010).
CC -!- FUNCTION: Responsible for heterokaryon incompatibility, a process that
CC ensures that during spontaneous, vegetative cell fusion only compatible
CC cells from the same colony survive (non-self-recognition). Interaction
CC with the prion form [het-s] of incompatible cells triggers a lethal
CC reaction that prevents the formation of viable heterokaryons.
CC {ECO:0000269|PubMed:15159455, ECO:0000269|PubMed:1886611,
CC ECO:0000269|PubMed:8224826, ECO:0000269|PubMed:9275200}.
CC -!- SUBUNIT: Homodimer. Forms heterodimers with het-s.
CC -!- INTERACTION:
CC B2ACC7; B2ACC7: het-S; NbExp=2; IntAct=EBI-16031574, EBI-16031574;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The globular domain exerts a prion-inhibitory effect (in cis)
CC on its own C-terminal prion domain. The het-S globular domain, but not
CC the het-s globular domain, is essential for programmed cell death.
CC -!- DOMAIN: The protein contains a prion domain (PrD), but beta-structuring
CC in this domain due to incorporation into a het-s fibril induces a
CC change in its globular domain, generating a molecular species that is
CC incompetent for fibril growth.
CC -!- MISCELLANEOUS: In P.anserina, the het-s locus exists as 2 incompatible
CC alleles, het-s and het-S. Strains of het-s genotype (e.g. A, C, s, and
CC V) can display 2 distinct phenoypes, the neutral (prion-free) [Het-s*],
CC which is compatible with het-S strains (e.g. D, S, U, and X), and the
CC reactive [Het-s] phenotype, which causes rapid cell death in het-S
CC strains. Although the two alleles het-s and het-S differ from each
CC other by 14 amino acids, vegetative incompatibility between s and S
CC strains can be attributed to a single amino acid difference in the
CC proteins encoded by the het-s locus (PubMed:8224826). A sequence for
CC the het-s allele can be found in strain s (AC Q03689).
CC {ECO:0000305|PubMed:8224826}.
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DR EMBL; M38530; AAB88771.1; -; Unassigned_DNA.
DR EMBL; CU633448; CAP61092.1; -; Genomic_DNA.
DR EMBL; FO904938; CDP26545.1; -; Genomic_DNA.
DR RefSeq; XP_001903320.1; XM_001903285.1.
DR PDB; 2WVO; X-ray; 2.30 A; A/B=1-227.
DR PDBsum; 2WVO; -.
DR AlphaFoldDB; B2ACC7; -.
DR SMR; B2ACC7; -.
DR DIP; DIP-59996N; -.
DR IntAct; B2ACC7; 1.
DR EnsemblFungi; CAP61092; CAP61092; PODANS_3_620.
DR GeneID; 6187356; -.
DR KEGG; pan:PODANSg332; -.
DR VEuPathDB; FungiDB:PODANS_3_620; -.
DR eggNOG; ENOG502RDGS; Eukaryota.
DR HOGENOM; CLU_058675_0_0_1; -.
DR OrthoDB; 1492404at2759; -.
DR Proteomes; UP000001197; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1020; -; 1.
DR InterPro; IPR029498; HeLo_dom.
DR InterPro; IPR038305; HeLo_sf.
DR InterPro; IPR021084; Het-s_prion_dom.
DR Pfam; PF14479; HeLo; 1.
DR Pfam; PF11558; HET-s_218-289; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Reference proteome.
FT CHAIN 1..289
FT /note="Heterokaryon incompatibility protein S"
FT /id="PRO_0000417568"
FT REGION 1..227
FT /note="Globular domain"
FT REGION 218..289
FT /note="Prion domain (PrD)"
FT MUTAGEN 33
FT /note="H->P: Converts its specificity to [Het-s]."
FT /evidence="ECO:0000269|PubMed:8224826"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:2WVO"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:2WVO"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 38..59
FT /evidence="ECO:0007829|PDB:2WVO"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 75..104
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:2WVO"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 153..172
FT /evidence="ECO:0007829|PDB:2WVO"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:2WVO"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:2WVO"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:2WVO"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2WVO"
SQ SEQUENCE 289 AA; 31960 MW; 3AB199A2596E85C2 CRC64;
MSEPFEIVAG ALGVAGLFNN CVACFEYVQL GRHFGRDYER CQLRLDIAKV RLSRWGEAVQ
INDDPRFHSS APIDKSVQLA KSIVEEILLL FESAQKTSKR YELVADQQDL VVFEDKDMKP
IGRALHRRLK DLVSRRQKQT SLAKKTAWAL YDGKSLEKIV DQVAGFVDEL EKAFPIEAVC
HKLAENEIEE VEDEASLTIL KDAAGGIDAA MSDAAAQKID AIVGRNSAKD IRTEKRARVQ
LGNVVTAAAL HGEIRISDQT TNSVETVVGK GESKVLIGNE YGGKGFWDN
