WTF33_SCHKA
ID WTF33_SCHKA Reviewed; 411 AA.
AC A0A482AS24;
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 wtf33 {ECO:0000303|PubMed:32032353};
GN Name=wtf33 {ECO:0000312|EMBL:QBL54519.1};
OS Schizosaccharomyces kambucha (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=204045 {ECO:0000312|EMBL:QBL54519.1};
RN [1] {ECO:0000312|EMBL:QBL54519.1}
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=A0A482AS24-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000303|PubMed:32032353};
CC IsoId=A0A482AS24-2; Sequence=VSP_060939;
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR EMBL; MH837457; QBL54519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482AS24; -.
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..411
FT /note="Meiotic driver wtf33"
FT /id="PRO_0000452271"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..95
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 38..78
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_060939"
SQ SEQUENCE 411 AA; 45856 MW; E546FDC72BF0ED42 CRC64;
MKNKYYPLRS SMDELSTKND NEIDLEKGPL PEYNSEDGST LPPYSENLNL KDPKQMGANN
PNLFNTDEST TPPDYGEDSL STTHRENHSS GTADNSCAST LKKAILSFIP IFVLNVSAVC
YLTYKDALFK DYGKDEWVYF GMWCASCLMI LISLWCFYET WIKAVKVTAV FLAQCIKVTA
VFLPQCIKVT AVFLAKCVKV TAVFLAKCIK VTAVFLAQCV KVTAISLAKC VKVISIGLFN
IRREMMIIIW ILWLIICCIL FGCVKDGRLN FNKALICSTC TISAVLFLIV SSVCIPIWTL
WRALSGMLQV LGIHGIIAVL VNGSMSLFGK HFGWRGYEIE GFVLFFTSSA LFLYEMERPG
VLKRMRNTTG NVIGYICGVI GDAFRRIENA FRGANDNNNI PLGEMDVEGE V
