WTF28_SCHKA
ID WTF28_SCHKA Reviewed; 397 AA.
AC A0A218N035;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=Meiotic driver wtf28 {ECO:0000303|PubMed:28631612};
GN Name=wtf28 {ECO:0000312|EMBL:ASF62180.1};
OS Schizosaccharomyces kambucha (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=204045 {ECO:0000312|EMBL:ASF62180.1};
RN [1] {ECO:0000312|EMBL:ASF62180.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE INITIATION
RP (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
RX PubMed=28631612; DOI=10.7554/elife.26033;
RA Nuckolls N.L., Bravo Nunez M.A., Eickbush M.T., Young J.M., Lange J.J.,
RA Yu J.S., Smith G.R., Jaspersen S.L., Malik H.S., Zanders S.E.;
RT "wtf genes are prolific dual poison-antidote meiotic drivers.";
RL Elife 6:e26033-e26033(2017).
RN [2] {ECO:0000305}
RP FUNCTION, AND ALTERNATIVE INITIATION (ISOFORMS 1 AND 2).
RX PubMed=32790622; DOI=10.7554/elife.57936;
RA Bravo Nunez M.A., Sabbarini I.M., Eide L.E., Unckless R.L., Zanders S.E.;
RT "Atypical meiosis can be adaptive in outcrossed Schizosaccharomyces pombe
RT due to wtf meiotic drivers.";
RL Elife 9:e57936-e57936(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:28631612, ECO:0000269|PubMed:32790622}.
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:28631612}, Suppressor
CC {ECO:0000305};
CC IsoId=A0A218N035-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000303|PubMed:28631612};
CC IsoId=A0A218N035-2; Sequence=VSP_060937;
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR EMBL; KY652739; ASF62180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218N035; -.
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..397
FT /note="Meiotic driver wtf28"
FT /id="PRO_0000452269"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..102
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 COMPBIAS 84..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:28631612"
FT /id="VSP_060937"
SQ SEQUENCE 397 AA; 44495 MW; 08F2F69195D6EAF4 CRC64;
MKNKYYPLRS SMDELSTKND NEIDLEKGPL PEYNSEDGNT LPPYSENINL KDPKQMGQNI
TKLFNWNKST TPPDYDENRL PITDEGNNPP NTHRENHSSG TADNSSPFLI KLIISFTPIF
VLNVPAVCYL TYKDALFKDY GKDEWVYFGV WCAICLMSFI SLWCFYETWT KAVKVTVIFL
AQCVKVTVIF LAQCVKVTAI FSAQCIKVTV ISLAKCVKVI AVGLYNSKKD LVVTIWLAWV
VICFILFGCV KDGRLNLNKA LICSTSSISA ALFFILLLVC IPIWTLKHML FGLFQVLGVQ
SCVVIVTKGL MYLFDKHIDA TGYEIEASSL FVIGNFLFFY EMERPGALKR MPKFIRNGIA
SFLGGIANAF GGIANAIRGA NDNNDIPLGE MEVESEV
