WTF23_SCHPO
ID WTF23_SCHPO Reviewed; 368 AA.
AC O94409;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Meiotic driver wtf23 {ECO:0000312|PomBase:SPCC1620.02};
GN Name=wtf23 {ECO:0000312|PomBase:SPCC1620.02}; Synonyms=wtf10;
GN ORFNames=SPCC1620.02 {ECO:0000312|PomBase:SPCC1620.02};
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 ALTERNATIVE INITIATION (ISOFORMS 1 AND 2).
RX PubMed=30991417; DOI=10.1093/molbev/msz052;
RA Eickbush M.T., Young J.M., Zanders S.E.;
RT "Killer Meiotic Drive and Dynamic Evolution of the wtf Gene Family.";
RL Mol. Biol. Evol. 36:1201-1214(2019).
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:0000250|UniProtKB:A0A218N034}.
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=O94409-1; Sequence=Displayed;
CC Name=2; Synonyms=Poison {ECO:0000305};
CC IsoId=O94409-2; Sequence=VSP_060945;
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22486.1; -; Genomic_DNA.
DR PIR; T41032; T41032.
DR RefSeq; NP_588460.1; NM_001023451.2.
DR AlphaFoldDB; O94409; -.
DR SMR; O94409; -.
DR BioGRID; 275737; 1.
DR STRING; 4896.SPCC1620.02.1; -.
DR PaxDb; O94409; -.
DR EnsemblFungi; SPCC1620.02.1; SPCC1620.02.1:pep; SPCC1620.02. [O94409-1]
DR GeneID; 2539166; -.
DR KEGG; spo:SPCC1620.02; -.
DR PomBase; SPCC1620.02; wtf23.
DR VEuPathDB; FungiDB:SPCC1620.02; -.
DR HOGENOM; CLU_763247_0_0_1; -.
DR PhylomeDB; O94409; -.
DR PRO; PR:O94409; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA: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; ISM:PomBase.
DR InterPro; IPR004982; WTF.
DR Pfam; PF03303; WTF; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Reference proteome; Toxin; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..368
FT /note="Meiotic driver wtf23"
FT /id="PRO_0000193234"
FT TRANSMEM 105..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..98
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..77
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:0000250|UniProtKB:A0A218N035"
FT /id="VSP_060945"
SQ SEQUENCE 368 AA; 41197 MW; 2D05E5EB8606B507 CRC64;
MKNKYYPLRS SMDELSAKND NEIDLEKGPL PEYNSEDGST LPPYSENINL KDPKQMGANN
PNLFNTDEST TPPDYGEDSL SITHRENHSS GTADNSSTSP LKKAFLSFIS IFVLNVPAVC
YLTYKDALFK DYGKDEWVYF GVWCAICLMI FISLWYFYET WIKAVKVTVI FLAQCIKVTV
VFLAQCVKVI SIGLFNIRRE MMIIIWLLWL IICCILFGCV KSGDLNLNKA LIYSTCTISA
VLLLIVSSVC IPFWTFERTL AKLAKVFLLQ SGIVLVLNGT MFLRGKHFEW TGCEIEASVL
FIMGNVLFLC EMECPGALIR TRNSIRNGIA FILGGIGNAM MGLANAFRGG NDNNNNIPLG
EMDVEGEV
