WTF9_SCHPM
ID WTF9_SCHPM Reviewed; 377 AA.
AC A0A1X9Q9F0;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Meiotic driver cw9 {ECO:0000303|PubMed:28631610};
GN Name=cw9 {ECO:0000312|EMBL:ARQ19037.1};
OS Schizosaccharomyces pombe (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=4896 {ECO:0000312|EMBL:ARQ19037.1};
RN [1] {ECO:0000312|EMBL:ARQ19037.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE INITIATION
RP (ISOFORMS 1 AND 2), AND DISRUPTION PHENOTYPE.
RC STRAIN=CBS5557 {ECO:0000312|EMBL:ARQ19037.1};
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, 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:28631610}, Suppressor
CC {ECO:0000305};
CC IsoId=A0A1X9Q9F0-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000303|PubMed:28631610};
CC IsoId=A0A1X9Q9F0-2; Sequence=VSP_060933;
CC -!- DISRUPTION PHENOTYPE: Abnormal spore maturation in presence of cw9-
CC encoded poison (PubMed:28631610). Sensitises cells to cw9-encoded
CC poison; simultaneous disruption of cw27 enhances sensitivity
CC (PubMed:28631610). {ECO:0000269|PubMed:28631610}.
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR EMBL; KY926722; ARQ19037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9Q9F0; -.
DR SMR; A0A1X9Q9F0; -.
DR VEuPathDB; FungiDB:SPCC970.11c; -.
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; IMP: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..377
FT /note="Meiotic driver cw9"
FT /id="PRO_0000452259"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..100
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 81..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:28631610"
FT /id="VSP_060933"
SQ SEQUENCE 377 AA; 42630 MW; 60106014725F610C CRC64;
MKNKYYPLRS SMDEMSAKND NEIDLEKGPL PEYNSEDGST LPPYSDLNNP KQMGQNITKL
FNWNKSTTPP DYDENRLPIT DEGNNPPNTH RENHSSGTTD NSSPFLIKLL ISFTSIILFN
APAVCYLKYK DAFFKNYGAA EWTLFGFWCL VCTLALLFLT YFYETWSKAV KVTIIFLAQC
IKVTAVFLAQ CVKVTAISLA KCVKVTAVGL YNSREKWVVI IWLLWVVICY TLFLRSKFGN
LNLNKALICS TCSISAALLL FLLYVRLPFW TLKHMFSGLF QVLGVQSCVV IVTKGLMHLF
DKHIDATGYE IEVSSLFVIG NFLFFYEMEC PGALRRMPKS IRNGIASFLE GTGRAIRGAN
DNNNSIPLEE TEAESEV
