WTF9_SCHKA
ID WTF9_SCHKA Reviewed; 357 AA.
AC A0A482AQV2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Meiotic driver wtf9 {ECO:0000303|PubMed:32032353};
GN Name=wtf9 {ECO:0000312|EMBL:QBL54500.1};
OS Schizosaccharomyces kambucha (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=204045 {ECO:0000312|EMBL:QBL54500.1};
RN [1] {ECO:0000312|EMBL:QBL54500.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ALTERNATIVE INITIATION
RP (ISOFORMS 1 AND 2).
RX PubMed=32032353; DOI=10.1371/journal.pgen.1008350;
RA Bravo Nunez M.A., Sabbarini I.M., Eickbush M.T., Liang Y., Lange J.J.,
RA Kent A.M., Zanders S.E.;
RT "Dramatically diverse Schizosaccharomyces pombe wtf meiotic drivers all
RT display high gamete-killing efficiency.";
RL PLoS Genet. 16:e1008350-e1008350(2020).
CC -!- FUNCTION: Promotes unequal transmission of alleles from the parental
CC zygote to progeny spores by acting as poison/antidote system where the
CC poison and antidote proteins are produced from the same locus; the
CC poison component is trans-acting and targets all spores within an ascus
CC whereas the antidote component is spore-specific, leading to poisoning
CC of all progeny that do not inherit the allele.
CC {ECO:0000269|PubMed:32032353}.
CC -!- FUNCTION: [Isoform 1]: Localizes isoform 2 to the vacuole thereby
CC facilitating its degradation. {ECO:0000250|UniProtKB:A0A218N034}.
CC -!- FUNCTION: [Isoform 2]: Forms toxic aggregates that disrupt spore
CC maturation. {ECO:0000250|UniProtKB:A0A218N034}.
CC -!- SUBUNIT: Homomer (By similarity). Forms protein aggregates (By
CC similarity). The two isoforms can interact with each other and with
CC themselves (By similarity). High sequence similarity is required for
CC their interaction (By similarity). {ECO:0000250|UniProtKB:A0A218N034,
CC ECO:0000250|UniProtKB:O74420}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane
CC {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Contained within spores expressing the
CC isoform and localizes isoform 2 to the vacuole.
CC {ECO:0000250|UniProtKB:A0A218N034}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm
CC {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm
CC {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane
CC {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Localizes in trans to all spores within an
CC ascus. Localization to the spore vacuole is dependent on isoform 1.
CC {ECO:0000250|UniProtKB:A0A218N034}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Antidote {ECO:0000303|PubMed:32032353}, Suppressor
CC {ECO:0000305};
CC IsoId=A0A482AQV2-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000303|PubMed:32032353};
CC IsoId=A0A482AQV2-2; Sequence=VSP_060932;
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR EMBL; MH837435; QBL54500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482AQV2; -.
DR GO; GO:0072324; C:ascus epiplasm; IC:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0110134; P:meiotic drive; IDA:UniProtKB.
DR InterPro; IPR004982; WTF.
DR Pfam; PF03303; WTF; 2.
PE 3: Inferred from homology;
KW Alternative initiation; Cytoplasm; Endoplasmic reticulum; Membrane; Toxin;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..357
FT /note="Meiotic driver wtf9"
FT /id="PRO_0000452258"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..44
FT /note="MKNKYYPLRSSMDEMSAKNDNEIDLEKGPLPEYNSEDGSTLPPY -> ML
FT (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:32032353"
FT /id="VSP_060932"
SQ SEQUENCE 357 AA; 40132 MW; 1EA9F9B5E5CDF172 CRC64;
MKNKYYPLRS SMDEMSAKND NEIDLEKGPL PEYNSEDGST LPPYSEIWKY IKTVSEDSST
GPTETTNPNV ERRQEFKDSH PNIYSLLRLL ISVLAVIVVF FTAWVCVNPL EKSIFGKVAF
FVTIGITCPI LLITIFCFFE TWTQAVAQCI KVTVIFLAQC VKVTVISLAK CVKVTAISLA
KCVKVTAVGL YNSREKWVVI IWLLWVVICY TLFLRSKFGN LNLNKALICS TCSISAALLL
FLLYVRLPFW TLKHMFSGLF QVLGVQSCVV IVTKGLMHLF DKHIDATGYE IEASSLFVIG
NFLFFYEMEC PGALRRMPKS IRNGIASFLE GTGKAIRGAN DNNNNIPLEE TEAESEV
