WTF27_SCHPM
ID WTF27_SCHPM Reviewed; 375 AA.
AC A0A1X9Q9H1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Meiotic driver cw27 {ECO:0000303|PubMed:28631610};
GN Name=cw27 {ECO:0000312|EMBL:ARQ19057.1};
OS Schizosaccharomyces pombe (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=4896 {ECO:0000312|EMBL:ARQ19057.1};
RN [1] {ECO:0000312|EMBL:ARQ19057.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE INITIATION
RP (ISOFORMS 1 AND 2), AND DISRUPTION PHENOTYPE.
RC STRAIN=CBS5557 {ECO:0000312|EMBL:ARQ19057.1};
RX PubMed=28631610; DOI=10.7554/elife.26057;
RA Hu W., Jiang Z.D., Suo F., Zheng J.X., He W.Z., Du L.L.;
RT "A large gene family in fission yeast encodes spore killers that subvert
RT Mendel's law.";
RL Elife 6:e26057-e26057(2017).
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:28631610}.
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}; Multi-pass membrane protein
CC {ECO:0000255}. Vacuole {ECO:0000250|UniProtKB:A0A218N034}. Membrane
CC {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
CC Note=Contained within spores expressing the isoform and localizes
CC isoform 2 to the vacuole. {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}; Multi-pass membrane protein
CC {ECO:0000255}. Vacuole {ECO:0000250|UniProtKB:A0A218N034}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:A0A218N034}. Membrane {ECO:0000255};
CC Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to
CC all spores within an ascus. Localization to the spore vacuole is
CC dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Antidote {ECO:0000303|PubMed:28631610}, Suppressor
CC {ECO:0000305};
CC IsoId=A0A1X9Q9H1-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000303|PubMed:28631610};
CC IsoId=A0A1X9Q9H1-2; Sequence=VSP_060936;
CC -!- DISRUPTION PHENOTYPE: Abnormal spore maturation in presence of cw27-
CC encoded poison (PubMed:28631610). Sensitises cells to cw27-encoded
CC poison; simultaneous disruption of cw9 enhances sensitivity
CC (PubMed:28631610). {ECO:0000269|PubMed:28631610}.
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR EMBL; KY926742; ARQ19057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9Q9H1; -.
DR VEuPathDB; FungiDB:SPCC1620.02; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0110134; P:meiotic drive; IMP:UniProtKB.
DR InterPro; IPR004982; WTF.
DR Pfam; PF03303; WTF; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Cytoplasm; Endoplasmic reticulum; Membrane; Toxin;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..375
FT /note="Meiotic driver cw27"
FT /id="PRO_0000452268"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..103
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..103
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:28631610"
FT /id="VSP_060936"
SQ SEQUENCE 375 AA; 42009 MW; BEBB124337FAB1E2 CRC64;
MKNKYYPLRS SMDELSTKND NEIDLEKGPL PEYNSEDGST LPPYSENLNL KDPKQMGQSI
TKLFNWNKST TPPDYDENRL LITDEGNNPP NTHRENHSSG TTDNSSPFLI KLLISFTSII
LFNAPAVCYL KYKDAFFKNY GAAEWTLIGF WCASSLIIFT FSWCFYETWT KAVKVTVIFL
AQCIKVTAIS LAKCVKVISI GLFNIRREMM IIIWILWLII CCILFGCVKD GRLNLNKALI
CSTCTISAVL FLIVSSVCIP IWTLWRALSG MLQVLGIHGI IALLVNGLMS LFGKHFGWRG
YEIEGFVLFF TGNALFLYEM ERPGVLKRMR NTTRNVIGFI LGGIANAIGG IANAIGGAND
NNDIPLGELE VESEV
