WTF18_SCHPM
ID WTF18_SCHPM Reviewed; 410 AA.
AC A0A482ARC8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Meiotic driver wtf18 {ECO:0000303|PubMed:32032353};
GN Name=wtf18 {ECO:0000312|EMBL:QBL54276.1};
OS Schizosaccharomyces pombe (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=4896 {ECO:0000312|EMBL:QBL54276.1};
RN [1] {ECO:0000312|EMBL:QBL54276.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION (ISOFORM 1), AND ALTERNATIVE
RP INITIATION (ISOFORMS 1 AND 2).
RC STRAIN=FY29033 {ECO:0000312|EMBL:QBL54276.1};
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 (By similarity). In addition to
CC suppressing isoform 2, also suppresses S.pombe strain 972 wtf13 isoform
CC 2 (PubMed:32032353). {ECO:0000250|UniProtKB:A0A218N034,
CC ECO:0000269|PubMed:32032353}.
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=A0A482ARC8-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000303|PubMed:32032353};
CC IsoId=A0A482ARC8-2; Sequence=VSP_060934;
CC -!- SIMILARITY: Belongs to the WTF 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; MH837209; QBL54276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482ARC8; -.
DR VEuPathDB; FungiDB:SPCC162.04c; -.
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..410
FT /note="Meiotic driver wtf18"
FT /id="PRO_0000452264"
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 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
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="MKNKGYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPY -> ML
FT (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:32032353"
FT /id="VSP_060934"
SQ SEQUENCE 410 AA; 45032 MW; 6773D2E9B421E69B CRC64;
MKNKGYPLRS SMDELSTKND NEIDLEKGPL PEYNSEDGST LPPYSEIWKY IKTVSEDSST
GPTETTNPNV ERRQEFKDSH PNIYSLLRLL ISVLAVIVVF FTAWVCVNPL EKSIFGKVAF
FVTIGITCPI LLITIFCFFE TWTQAVAQCI KVTVIFLAQC VKVTAVFLAK CIKVTAVFLA
KCVKVTAVFL AKCIKVTAVF LAKCVKVTAV FLAKCVKVIA VGLYNSKKDL VVTIWLAWVV
ICFILFGCVK DGRLNLNKAL ICSTCSISAA LFFILLLVCI PIWTLKHMLF GLFQVLGVQS
CVVIVTKGLM YLFDKHIDAT GYEIEASSLF VIGNFLFFYE MERPGALKRM PKFIGNGIAS
FLGGLGNAFG GIGNAFGGIG NAIGRIGNAF RGANDNNDIP LGEMDVESEV
