WTF30_SCHKA
ID WTF30_SCHKA Reviewed; 350 AA.
AC A0A482ARN9;
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 wtf30 {ECO:0000303|PubMed:32032353};
GN Name=wtf30 {ECO:0000312|EMBL:QBL54516.1};
OS Schizosaccharomyces kambucha (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=204045 {ECO:0000312|EMBL:QBL54516.1};
RN [1] {ECO:0000312|EMBL:QBL54516.1}
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=A0A482ARN9-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000303|PubMed:32032353};
CC IsoId=A0A482ARN9-2; Sequence=VSP_060938;
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR EMBL; MH837454; QBL54516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482ARN9; -.
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; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Cytoplasm; Endoplasmic reticulum; Membrane; Toxin;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..350
FT /note="Meiotic driver wtf30"
FT /id="PRO_0000452270"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..92
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 58..76
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:32032353"
FT /id="VSP_060938"
SQ SEQUENCE 350 AA; 39386 MW; 64E7D0BB15D301D5 CRC64;
MKNKYYPLRS SIDELSTKND NEIDLEKGPL PEYNSEDGST LPPYSENLKL KDPKQMGANN
PNLFNTDEST TPPDYGEDSL SHRENHSSGT TDNSSPFLIK LLISFIPIFV LNVPAVCYLT
YKDALFKDYG KDEWVYFGMW CASCLMIFIS LWCFYETWTQ AVAQCVKVTA ISLAKCVKVI
SIGLFNIRRE MMIIIWILWL IICCILFVYI KSGDLNLNKA LIYSTCTISA VLLLIVSSVC
IPFWTFERTL AKLAKVFLLQ SGIVLVLNGT MFLRGKHFEW TGCEIEASVL FIMGNVLFLC
EMECPGALRR MPKSIRNGIA SFLGGIANAI RGANDNNDIP LGEMDVESEV
