WTF4_SCHPO
ID WTF4_SCHPO Reviewed; 366 AA.
AC Q9P3V0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Meiotic driver wtf4 {ECO:0000303|PubMed:32790622};
GN Name=wtf4 {ECO:0000312|PomBase:SPCC548.03c}; Synonyms=wtf13;
GN ORFNames=SPCC548.03c {ECO:0000312|PomBase:SPCC548.03c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL, AND ALTERNATIVE INITIATION (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 [3]
RP FUNCTION.
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: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:0000305}, Suppressor {ECO:0000305};
CC IsoId=Q9P3V0-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000305};
CC IsoId=Q9P3V0-2; Sequence=VSP_060942;
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAO77683.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU329672; CAO77683.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_004001741.1; XM_004001692.1.
DR AlphaFoldDB; Q9P3V0; -.
DR SMR; Q9P3V0; -.
DR BioGRID; 276119; 1.
DR STRING; 4896.SPCC548.03c.1; -.
DR PaxDb; Q9P3V0; -.
DR PRIDE; Q9P3V0; -.
DR EnsemblFungi; SPCC548.03c.1; SPCC548.03c.1:pep; SPCC548.03c.
DR PomBase; SPCC548.03c; wtf4.
DR VEuPathDB; FungiDB:SPCC548.03c; -.
DR HOGENOM; CLU_763247_0_0_1; -.
DR PhylomeDB; Q9P3V0; -.
DR PRO; PR:Q9P3V0; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
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:PomBase.
DR InterPro; IPR004982; WTF.
DR Pfam; PF03303; WTF; 2.
PE 3: Inferred from homology;
KW Alternative initiation; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Reference proteome; Toxin; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..366
FT /note="Meiotic driver wtf4"
FT /id="PRO_0000193221"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..44
FT /note="MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPY -> ML
FT (in isoform 2)"
FT /evidence="ECO:0000250|UniProtKB:O74420"
FT /id="VSP_060942"
SQ SEQUENCE 366 AA; 40360 MW; 5C795A0F5BCAA795 CRC64;
MKNKDYPLRS SMDELSTKND NEIDLEKGPL PEYNSEDGST LPPYSEIWKY IKTVSEDSST
GPTEIANPNV ERRQEFKDSH PNIYSLLRLL ISVLAVIVVF FTAWVCVNPL EKSIFGKVAF
SVTIGITCPI VFIVIFCFFE TWTQAVAQCI KVTVIFLAQC VKVTAVFLAK CVKVIAVGLY
NSKKDLVVTI WLAWVVICFI LFGCVKDGRL NLNKALICST CSISAALFFI LLLVCIPIWT
LKHMLFGLFQ VLGVQSCVVI VTKGLMYLFD KHIDATGYEI EASSLFVIGN FLFFYEMERP
GALKRMPKFI GNGIASFLGG LGNAFGGIGN AFGGIGNAIG RIGNAFRGAN DNNDIPLGEM
DVESEV
