M11P_SCVM1
ID M11P_SCVM1 Reviewed; 316 AA.
AC P01546;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 78.
DE RecName: Full=M1-1 protoxin;
DE AltName: Full=Killer toxin K1;
DE Contains:
DE RecName: Full=M1-1 delta chain;
DE Contains:
DE RecName: Full=M1-1 alpha chain;
DE Contains:
DE RecName: Full=M1-1 gamma immunity chain;
DE Contains:
DE RecName: Full=M1-1 beta chain;
DE Flags: Precursor;
OS Saccharomyces cerevisiae killer virus M1 (ScV-M1) (Saccharomyces cerevisiae
OS virus M1).
OC Viruses; Riboviria; dsRNA viruses.
OX NCBI_TaxID=12450;
OH NCBI_TaxID=4932; Saccharomyces cerevisiae (Baker's yeast).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6697395; DOI=10.1016/0092-8674(84)90354-4;
RA Bostian K.A., Elliott Q., Bussey H., Burn V., Smith A., Tipper D.J.;
RT "Sequence of the preprotoxin dsRNA gene of type I killer yeast: multiple
RT processing events produce a two-component toxin.";
RL Cell 36:741-751(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6368221; DOI=10.1002/j.1460-2075.1984.tb01769.x;
RA Skipper N., Thomas D.Y., Lau P.C.K.;
RT "Cloning and sequencing of the preprotoxin-coding region of the yeast M1
RT double-stranded RNA.";
RL EMBO J. 3:107-111(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=TF325;
RX PubMed=9234671;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<829::aid-yea144>3.0.co;2-r;
RA Russell P.J., Bennett A.M., Love Z., Baggott D.M.;
RT "Cloning, sequencing and expression of a full-length cDNA copy of the M1
RT double-stranded RNA virus from the yeast, Saccharomyces cerevisiae.";
RL Yeast 13:829-836(1997).
RN [4]
RP FUNCTION.
RX PubMed=1696721; DOI=10.1073/pnas.87.16.6228;
RA Martinac B., Zhu H., Kubalski A., Zhou X.L., Culbertson M., Bussey H.,
RA Kung C.;
RT "Yeast K1 killer toxin forms ion channels in sensitive yeast spheroplasts
RT and in artificial liposomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6228-6232(1990).
RN [5]
RP REVIEW.
RX PubMed=18291112; DOI=10.1016/j.bbamcr.2008.01.017;
RA Schmitt M.J., Reiter J.;
RT "Viral induced yeast apoptosis.";
RL Biochim. Biophys. Acta 1783:1413-1417(2008).
CC -!- FUNCTION: Ionophoric toxin secreted by an infected host and lethal to
CC non-infected sensitive strains. Cell killing is achieved in a receptor-
CC mediated process, requiring initial toxin binding to a cell wall
CC (1->6)-beta-D-glucan and, probably, subsequent transfer to a plasma
CC membrane receptor. K1 toxin disrupts the cell by creating a pore across
CC the target cell membrane. {ECO:0000269|PubMed:1696721}.
CC -!- SUBUNIT: The secreted toxin contains alpha and beta chains that are
CC linked by three disulfide bonds.
CC -!- SUBCELLULAR LOCATION: Secreted. Host membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Pore-forming in target cell.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: The killer phenotype requires the presence of two
CC different dsRNA viruses: an L-A helper virus and the toxin-coding (M)
CC killer virus. Killer strains of S.cerevisiae producing the toxin K1
CC kill sensitive cells but are resistant to their own toxin. The gamma
CC and delta chains may play a role, on there own or as part of the
CC protoxin, in the self-protection of the virus-infected killer yeast
CC (toxin immunity).
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DR EMBL; K02042; AAA34748.1; -; mRNA.
DR EMBL; X00285; CAA25078.1; -; mRNA.
DR EMBL; X00285; CAA25079.1; -; mRNA.
DR EMBL; U78817; AAC58005.1; -; Genomic_RNA.
DR RefSeq; NP_044402.1; NC_001782.1.
DR TCDB; 1.C.6.1.1; the yeast killer toxin k1 (ykt-k1) family.
DR GeneID; 1494398; -.
DR KEGG; vg:1494398; -.
DR Proteomes; UP000243666; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Host membrane; Lectin; Membrane; Reference proteome; Secreted; Signal;
KW Toxin; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT CHAIN 27..316
FT /note="M1-1 protoxin"
FT /id="PRO_0000041343"
FT CHAIN 27..44
FT /note="M1-1 delta chain"
FT /id="PRO_0000041344"
FT CHAIN 45..147
FT /note="M1-1 alpha chain"
FT /id="PRO_0000041345"
FT CHAIN 150..233
FT /note="M1-1 gamma immunity chain"
FT /id="PRO_0000041346"
FT CHAIN 234..316
FT /note="M1-1 beta chain"
FT /id="PRO_0000041347"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 92..248
FT /evidence="ECO:0000250"
FT DISULFID 95..312
FT /evidence="ECO:0000250"
FT DISULFID 107..239
FT /evidence="ECO:0000250"
FT CONFLICT 103
FT /note="I -> S (in Ref. 2; CAA25078)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="T -> A (in Ref. 2; CAA25078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 34826 MW; D44CF7797C56C432 CRC64;
MTKPTQVLVR SVSILFFITL LHLVVALNDV AGPAETAPVS LLPREAPWYD KIWEVKDWLL
QRATDGNWGK SITWGSFVAS DAGVVIFGIN VCKNCVGERK DDISTDCGKQ TLALLVSIFV
AVTSGHHLIW GGNRPVSQSD PNGATVARRD ISTVADGDIP LDFSALNDIL NEHGISILPA
NASQYVKRSD TAEHTTSFVV TNNYTSLHTD LIHHGNGTYT TFTTPHIPAV AKRYVYPMCE
HGIKASYCMA LNDAMVSANG NLYGLAEKLF SEDEGQWETN YYKLYWSTGQ WIMSMKFIEE
SIDNANNDFE GCDTGH
