ID KP4T_UMV4 Reviewed; 127 AA. AC Q90121; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 22-FEB-2023, entry version 89. DE RecName: Full=KP4 killer toxin; DE AltName: Full=Fungal toxin KP4; DE AltName: Full=Killer protein 4; DE Flags: Precursor; GN Name=M2A; OS Ustilago maydis P4 virus (UmV4) (UmV-P4). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes; OC Ghabrivirales; Totiviridae; Totivirus. OX NCBI_TaxID=11009; OH NCBI_TaxID=5270; Ustilago maydis (Corn smut fungus). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 23-79 AND 124-127, RP AND MASS SPECTROMETRY. RC STRAIN=77; RX PubMed=8145639; DOI=10.1111/j.1365-2958.1994.tb00297.x; RA Park C.-M., Bruenn J.A., Ganesa C., Flurkey W.F., Bozarth R.F., Koltin Y.; RT "Structure and heterologous expression of the Ustilago maydis viral toxin RT KP4."; RL Mol. Microbiol. 11:155-164(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=M2B; RA Gu F., Khimani A.K., Flurkey W.F., Bozarth R.F., Smith T.J., Rane S.; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 23-52. RX PubMed=1897946; DOI=10.1016/0003-9861(91)90027-g; RA Ganesa C., Flurkey W.H., Randhawa Z.I., Bozarth R.F.; RT "Ustilago maydis virus P4 killer toxin: characterization, partial amino RT terminus sequence, and evidence for glycosylation."; RL Arch. Biochem. Biophys. 286:195-200(1991). RN [4] RP FUNCTION. RX PubMed=11532143; DOI=10.1046/j.1365-2958.2001.02554.x; RA Gage M.J., Bruenn J., Fischer M., Sanders D., Smith T.J.; RT "KP4 fungal toxin inhibits growth in Ustilago maydis by blocking calcium RT uptake."; RL Mol. Microbiol. 41:775-785(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=7582897; DOI=10.1016/s0969-2126(01)00215-5; RA Gu F., Khimani A., Rane S.G., Flurkey W.H., Bozarth R.F., Smith T.J.; RT "Structure and function of a virally encoded fungal toxin from Ustilago RT maydis: a fungal and mammalian Ca2+ channel inhibitor."; RL Structure 3:805-814(1995). CC -!- FUNCTION: This protein is lethal to sensitive cells of the same or CC related species. It specifically inhibits voltage-gated calcium CC channels. It inhibits cell growth and division by blocking calcium CC import. {ECO:0000269|PubMed:11532143}. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- MASS SPECTROMETRY: Mass=11045; Mass_error=11; Method=MALDI; CC Evidence={ECO:0000269|PubMed:8145639}; CC -!- BIOTECHNOLOGY: The KP4 toxin expressed in transgenic plant can render CC them resistant to KP4-susceptible fungal pathogens such as grass smut CC fungi. Successful tests have been made in tobacco and wheat. CC -!- CAUTION: Was originally thought to be glycosylated, but this does not CC seem to be the case according to PubMed:8145639. CC {ECO:0000305|PubMed:1897946}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L12226; AAA89185.1; -; Genomic_RNA. DR EMBL; U25179; AAA75041.1; -; Genomic_RNA. DR PIR; S40034; S40034. DR PDB; 1KPT; X-ray; 1.75 A; A/B=23-127. DR PDBsum; 1KPT; -. DR SMR; Q90121; -. DR EvolutionaryTrace; Q90121; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.430.10; Killer Toxin P4, subunit A; 1. DR InterPro; IPR015131; Killer_tox_Kp4. DR InterPro; IPR011329; Killer_tox_Kp4/SMK. DR Pfam; PF09044; Kp4; 1. DR SUPFAM; SSF55221; Yeast killer toxins; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Signal; KW Toxin. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:1897946, FT ECO:0000269|PubMed:8145639" FT CHAIN 23..127 FT /note="KP4 killer toxin" FT /id="PRO_0000041338" FT DISULFID 27..100 FT DISULFID 33..103 FT DISULFID 49..89 FT DISULFID 57..82 FT DISULFID 66..127 FT CONFLICT 56 FT /note="W -> I (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="C -> E (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 67 FT /note="G -> C (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 73 FT /note="S -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 74 FT /note="A -> H (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 79 FT /note="T -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 31..35 FT /evidence="ECO:0007829|PDB:1KPT" FT HELIX 40..50 FT /evidence="ECO:0007829|PDB:1KPT" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:1KPT" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:1KPT" FT STRAND 71..80 FT /evidence="ECO:0007829|PDB:1KPT" FT HELIX 85..98 FT /evidence="ECO:0007829|PDB:1KPT" FT STRAND 104..109 FT /evidence="ECO:0007829|PDB:1KPT" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:1KPT" FT STRAND 118..125 FT /evidence="ECO:0007829|PDB:1KPT" SQ SEQUENCE 127 AA; 13489 MW; 34CAA729C9A63E1E CRC64; MQIINVVYSF LFAAAMLPVV HSLGINCRGS SQCGLSGGNL MVRIRDQACG NQGQTWCPGE RRAKVCGTGN SISAYVQSTN NCISGTEACR HLTNLVNHGC RVCGSDPLYA GNDVSRGQLT VNYVNSC //