WTF25_SCHPO
ID WTF25_SCHPO Reviewed; 249 AA.
AC U3H0P2;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Meiotic drive suppressor wtf25 {ECO:0000312|PomBase:SPCC1919.06c};
GN Name=wtf25 {ECO:0000312|PomBase:SPCC1919.06c};
GN ORFNames=SPCC1919.06c {ECO:0000312|PomBase:SPCC1919.06c};
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Acts as a suppressor component of the dual wtf meiotic drive
CC system, and can suppress but not confer meiotic drive by compatible
CC poisons (By similarity). Wtf meiotic drive systems promote unequal
CC transmission of alleles from the parental zygote to progeny spores by
CC encoding a poison and an antidote from the same locus; the poison is
CC trans-acting and forms toxic aggregates in all spores within an ascus,
CC wherease the antidote is spore-specific and targets aggregates for
CC degradation by the vacuole (By similarity). Meiotic drive by wtf
CC systems therefore lead to poisoning of all progeny that do not inherit
CC the dual poison/antidote allele, or express a compatible antidote (By
CC similarity). {ECO:0000250|UniProtKB:A0A218N034,
CC ECO:0000250|UniProtKB:A0A482ATU4}.
CC -!- SUBUNIT: Homomer (By similarity). Interacts with other proteins that
CC exhibit high sequence similarity (By similarity).
CC {ECO:0000250|UniProtKB:A0A218N034, ECO:0000250|UniProtKB:O74420}.
CC -!- SUBCELLULAR LOCATION: Spore membrane {ECO:0000250|UniProtKB:A0A218N034,
CC ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole
CC membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR EMBL; CU329672; CAO77699.1; -; Genomic_DNA.
DR RefSeq; XP_004001756.1; XM_004001707.1.
DR AlphaFoldDB; U3H0P2; -.
DR BioGRID; 280225; 3.
DR STRING; 4896.SPCC1919.06c.1; -.
DR PaxDb; U3H0P2; -.
DR EnsemblFungi; SPCC1919.06c.1; SPCC1919.06c.1:pep; SPCC1919.06c.
DR PomBase; SPCC1919.06c; wtf25.
DR VEuPathDB; FungiDB:SPCC1919.06c; -.
DR HOGENOM; CLU_092895_0_0_1; -.
DR PRO; PR:U3H0P2; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; ISS:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
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 Membrane; Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..249
FT /note="Meiotic drive suppressor wtf25"
FT /id="PRO_0000429003"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 249 AA; 28441 MW; A88470A57581DBB5 CRC64;
MKNNYTSLKS PLDEEDELKT DHEIDLEKGP LPEYDSEEEG ALPPYSDHAL VNNPLNTHRE
NHSYGTTDNS SPLLIILLIS FTSIILFNAP AFCYLKYKDA FFKNYGAAEW TLFGFWCLVC
TLALIFLTYF YETWSKACGK GIKHFLKNWR NMIFAFCKSS LFCLVLLKAE NKLSSHLGDQ
RWGWKCSASA FTFMAVSSIL IFIAETVEPG SCSTDLVKRT LAFYGYEIRQ HVNEDATILL
REMNPESEA
