WTF13_SCHPO
ID WTF13_SCHPO Reviewed; 388 AA.
AC O74420;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 3.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Meiotic driver wtf13 {ECO:0000303|PubMed:30475921};
GN Name=wtf13 {ECO:0000312|PomBase:SPCC162.04c}; Synonyms=wtf12;
GN ORFNames=SPCC162.04c {ECO:0000312|PomBase:SPCC162.04c};
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, FUNCTION, INTERACTION OF ISOFORMS 1 AND 2,
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND ALTERNATIVE INITIATION
RP (ISOFORMS 1 AND 2).
RX PubMed=30475921; DOI=10.1371/journal.pgen.1007836;
RA Bravo Nunez M.A., Lange J.J., Zanders S.E.;
RT "A suppressor of a wtf poison-antidote meiotic driver acts via mimicry of
RT the driver's antidote.";
RL PLoS Genet. 14:e1007836-e1007836(2018).
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).
RN [4]
RP FUNCTION (ISOFORM 1), AND SUBCELLULAR LOCATION.
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:30475921, ECO:0000269|PubMed:32032353,
CC ECO:0000269|PubMed:32790622}.
CC -!- FUNCTION: [Isoform 1]: Localizes isoform 2 to the vacuole thereby
CC facilitating its degradation (By similarity). In addition to
CC suppressing isoform 2, also suppresses S.pombe strain FY29033 wtf18
CC isoform 2 (PubMed:32032353). {ECO:0000250|UniProtKB:A0A218N034,
CC ECO:0000269|PubMed:32032353}.
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 (PubMed:30475921). {ECO:0000250|UniProtKB:A0A218N034,
CC ECO:0000269|PubMed:30475921}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000255,
CC ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353}; Multi-pass
CC membrane 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:0000269|PubMed:30475921}. Cytoplasm
CC {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000255,
CC ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353}; Multi-pass
CC membrane 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:30475921}, Suppressor
CC {ECO:0000305};
CC IsoId=O74420-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000303|PubMed:30475921};
CC IsoId=O74420-2; Sequence=VSP_060943;
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA19584.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU329672; CAA19584.2; ALT_SEQ; Genomic_DNA.
DR PIR; T41027; T41027.
DR RefSeq; NP_588240.1; NM_001023230.2.
DR AlphaFoldDB; O74420; -.
DR BioGRID; 275277; 15.
DR STRING; 4896.SPCC162.04c.1; -.
DR iPTMnet; O74420; -.
DR PaxDb; O74420; -.
DR EnsemblFungi; SPCC162.04c.1; SPCC162.04c.1:pep; SPCC162.04c.
DR GeneID; 2538692; -.
DR KEGG; spo:SPCC162.04c; -.
DR PomBase; SPCC162.04c; wtf13.
DR VEuPathDB; FungiDB:SPCC162.04c; -.
DR HOGENOM; CLU_763247_0_0_1; -.
DR PhylomeDB; O74420; -.
DR PRO; PR:O74420; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
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 1: Evidence at protein level;
KW Alternative initiation; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Reference proteome; Toxin; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..388
FT /note="Meiotic driver wtf13"
FT /id="PRO_0000193227"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
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:0000269|PubMed:30475921"
FT /id="VSP_060943"
SQ SEQUENCE 388 AA; 42607 MW; 5E261A0EC8BE57CD CRC64;
MKNKDYPLRS SMDELSTKND NEIDLEKGPL PEYNSEDGST LPPYSEIWKY IKTVSEDSST
GPTEIANPNV ERRQEFKDSH PNIYSLLRLL ISVLAVIVVF FTAWVCVNPL EKSIFGKVAF
SVTIGITCPI VFIAIFCFFE TWTQAVAQCI KVTVIFLAQC VKVTAISLAQ CVKVTAVFLA
KCVKVTAVFL AKCVKVIAVG LYNSKKDLVV TIWLAWVVIC FILFGCVKDG RLNLNKALIC
STCSISAALF FILLLVCIPI WTLKHMLFGL FQVLGVQSCV VIVTKGLMYL FDKHIDATGY
EIEASSLFVI GNFLFFYEME RPGALKRMPK FIGNGIASFL GGLGNAFGGI GNAFGGIGNA
IGRIGNAFRG ANDNNDIPLG EMDVESEV
