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WTF19_SCHPO
ID   WTF19_SCHPO             Reviewed;         393 AA.
AC   O74486; P78881;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Meiotic driver wtf19 {ECO:0000303|PubMed:32032353};
GN   Name=wtf19 {ECO:0000312|PomBase:SPCC1906.03};
GN   ORFNames=SPCC1906.03 {ECO:0000312|PomBase:SPCC1906.03};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-393.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
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).
RN   [4]
RP   FUNCTION.
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:0000305}, Suppressor {ECO:0000305};
CC         IsoId=O74486-1; Sequence=Displayed;
CC       Name=2; Synonyms=Poison {ECO:0000305};
CC         IsoId=O74486-2; Sequence=VSP_060944;
CC   -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13893.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CU329672; CAA20772.1; -; Genomic_DNA.
DR   EMBL; D89232; BAA13893.1; ALT_FRAME; mRNA.
DR   PIR; T41211; T41211.
DR   PIR; T43136; T43136.
DR   RefSeq; NP_588407.1; NM_001023398.2.
DR   AlphaFoldDB; O74486; -.
DR   BioGRID; 275827; 2.
DR   STRING; 4896.SPCC1906.03.1; -.
DR   PaxDb; O74486; -.
DR   EnsemblFungi; SPCC1906.03.1; SPCC1906.03.1:pep; SPCC1906.03. [O74486-1]
DR   GeneID; 2539257; -.
DR   KEGG; spo:SPCC1906.03; -.
DR   PomBase; SPCC1906.03; wtf19.
DR   VEuPathDB; FungiDB:SPCC1906.03; -.
DR   HOGENOM; CLU_763247_0_0_1; -.
DR   PhylomeDB; O74486; -.
DR   PRO; PR:O74486; -.
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: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; IDA:UniProtKB.
DR   InterPro; IPR004982; WTF.
DR   Pfam; PF03303; WTF; 2.
PE   2: Evidence at transcript level;
KW   Alternative initiation; Cytoplasm; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Toxin; Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..393
FT                   /note="Meiotic driver wtf19"
FT                   /id="PRO_0000193231"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
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_060944"
FT   CONFLICT        183
FT                   /note="L -> S (in Ref. 2; BAA13893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="L -> F (in Ref. 2; BAA13893)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  43945 MW;  933049A43EE1D39B CRC64;
     MKNKYYPLRS SMDELSAKND NEIDLEKGPL PEYNSEDGST LPPYSENINL KDPKQMGANN
     PNLFNTDEST TPPDYGEDSL SITHRENHSS GTADNSSTSP LKKAFLSFIS IFVLNVPAVC
     YLTYKDALFK DYGKDEWVYF AVWCASCLMI FISLWYFYET WIKAVKVTVI FLAQCIKVTV
     VFLAQCVKVT SISLAKCVKL TAVFLAQCVK VTAVFLAQCV KVISIGLFNI RREMMIIIWL
     LWLIICCILF GCVKSGDLNL NKALIYSTCT ISAVLLLIVS SVCIPFWTFE RTLAKLAKVF
     LLQSGIVLVL NGTMFLRGKH FEWTGCEIEA SVLFIMGNVL FLCEMECPGA LIRTRNSIRN
     GIAFILEGAG RAIRGANDNN DIPLGEMEVE SEV
 
 
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