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WTF36_SCHPM
ID   WTF36_SCHPM             Reviewed;         415 AA.
AC   A0A482AQK7;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Meiotic driver wtf36 {ECO:0000303|PubMed:32032353};
GN   Name=wtf36 {ECO:0000312|EMBL:QBL54290.1};
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=4896 {ECO:0000312|EMBL:QBL54290.1};
RN   [1] {ECO:0000312|EMBL:QBL54290.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ALTERNATIVE INITIATION
RP   (ISOFORMS 1 AND 2).
RC   STRAIN=FY29033 {ECO:0000312|EMBL:QBL54290.1};
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).
RN   [2]
RP   FUNCTION.
RC   STRAIN=FY29033 {ECO:0000303|PubMed:32790622};
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:32032353, 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:0000303|PubMed:32032353}, Suppressor
CC       {ECO:0000305};
CC         IsoId=A0A482AQK7-1; Sequence=Displayed;
CC       Name=2; Synonyms=Poison {ECO:0000303|PubMed:32032353};
CC         IsoId=A0A482AQK7-2; Sequence=VSP_060941;
CC   -!- SIMILARITY: Belongs to the WTF family. {ECO:0000305}.
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DR   EMBL; MH837224; QBL54290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A482AQK7; -.
DR   VEuPathDB; FungiDB:SPCC970.11c; -.
DR   GO; GO:0072324; C:ascus epiplasm; IC:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
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   3: Inferred from homology;
KW   Alternative initiation; Cytoplasm; Endoplasmic reticulum; Membrane; Toxin;
KW   Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..415
FT                   /note="Meiotic driver wtf36"
FT                   /id="PRO_0000452274"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..99
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        71..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..52
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000269|PubMed:32032353"
FT                   /id="VSP_060941"
SQ   SEQUENCE   415 AA;  46573 MW;  0B30501C9971A27C CRC64;
     MKNKYYPLRS SMDEMSAKND NEIDLEKGPL PEYNSEDGST LPPYSDLNNP KQMGQNITKL
     FNWNKSTTPP DYDENRLHIT DEGNNPPNTH RENHSSGTAD NSSPFLIKLL ISFTPIVLLN
     APAVCYLKYK DAFFKNYGAA EWTLFGFWCL VCTLALIFLT YFYETWTKAV KVTVIFLAQC
     VKVTVIFLAK CVKVTVIFLA KCVKVTAISL AKCIKVTAIF LAQCVKVTAV GLYNSREKWV
     VIIWLLWVVI CYTLFLRSKF GNLNLNKALI CSTCSISAAL LLFLLYVRLP FWTLKHMFSG
     LFQVLGVQSC VVIVTKGLTY LFDKHIDATG YEIEASSLFV IGNFLFFYEM ECPGALKRMP
     KFIRNGIASF LEGIGNIGNA IGRIGNAIGR IGNAFRGAND NNDIPLGEME VESEV
 
 
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