TX1AB_MYRPI
ID TX1AB_MYRPI Reviewed; 112 AA.
AC Q07932; Q9TWC1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=M-myrmeciitoxin-Mp1 {ECO:0000303|PubMed:26805882};
DE Short=M-MIITX-Mp1 {ECO:0000303|PubMed:26805882};
DE AltName: Full=Allergen Myr p I;
DE AltName: Full=Major allergen Myr p 1 {ECO:0000303|PubMed:7508264};
DE AltName: Full=Pilosulin-1 {ECO:0000303|PubMed:15019477};
DE AltName: Allergen=Myr p 1;
DE Contains:
DE RecName: Full=M-myrmeciitoxin-Mp1a {ECO:0000303|PubMed:26805882};
DE Short=M-MIITX-Mp1a {ECO:0000303|PubMed:26805882};
DE AltName: Full=M-myrmeciitoxin-Mp1b {ECO:0000303|PubMed:26805882};
DE Short=M-MIITX-Mp1b {ECO:0000303|PubMed:26805882};
DE AltName: Full=Pilosulin-1 57->112 {ECO:0000303|PubMed:15019477};
DE Short=Myr p 1 57->112 {ECO:0000303|PubMed:15019477};
DE Short=Myr p 1 57->112 (Ile5) {ECO:0000303|PubMed:15019477};
DE AltName: Full=[Ile-5]pilosulin-1 {ECO:0000303|PubMed:15019477};
DE Contains:
DE RecName: Full=M-myrmeciitoxin-Mp1c {ECO:0000303|PubMed:26805882};
DE Short=M-MIITX-Mp1c {ECO:0000303|PubMed:26805882};
DE AltName: Full=Pilosulin-1 65->112 {ECO:0000303|PubMed:15019477};
DE Short=Myr p 1 65->112 {ECO:0000303|PubMed:15019477};
DE Contains:
DE RecName: Full=M-myrmeciitoxin-Mp1d {ECO:0000303|PubMed:26805882};
DE Short=M-MIITX-Mp1d {ECO:0000303|PubMed:26805882};
DE AltName: Full=Pilosulin-1 68->112 {ECO:0000303|PubMed:15019477};
DE Short=Myr p 1 68->112 {ECO:0000303|PubMed:15019477};
DE Contains:
DE RecName: Full=M-myrmeciitoxin-Mp1e {ECO:0000303|PubMed:26805882};
DE Short=M-MIITX-Mp1e {ECO:0000303|PubMed:26805882};
DE AltName: Full=Pilosulin-1 71->112 {ECO:0000303|PubMed:15019477};
DE Short=Myr p 1 71->112 {ECO:0000303|PubMed:15019477};
DE Contains:
DE RecName: Full=U1-myrmeciitoxin-Mp1f {ECO:0000303|PubMed:26805882};
DE Short=U1-MIITX-Mp1f {ECO:0000303|PubMed:26805882};
DE AltName: Full=Pilosulin-1 86->112 {ECO:0000303|PubMed:15019477};
DE Short=Myr p 1 86->112 {ECO:0000303|PubMed:15019477};
DE Flags: Precursor;
OS Myrmecia pilosula (Jack jumper ant) (Australian jumper ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmeciinae; Myrmeciini; Myrmecia.
OX NCBI_TaxID=13618;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=7678752; DOI=10.1016/0167-4781(93)90065-l;
RA Donovan G.R., Baldo B.A., Sutherland S.K.;
RT "Molecular cloning and characterization of a major allergen (Myr p I) from
RT the venom of the Australian jumper ant, Myrmecia pilosula.";
RL Biochim. Biophys. Acta 1171:272-280(1993).
RN [2]
RP PROTEIN SEQUENCE OF 57-112; 65-112; 68-112; 71-112 AND 86-112, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8866004; DOI=10.1080/15216549600201022;
RA Donovan G.R., Street M.D., Tetaz T., Smith A.I., Alewood D., Alewood P.F.,
RA Sutherland S.K., Baldo B.A.;
RT "Expression of jumper ant (Myrmecia pilosula) venom allergens: post-
RT translational processing of allergen gene products.";
RL Biochem. Mol. Biol. Int. 39:877-885(1996).
RN [3]
RP PROTEIN SEQUENCE OF 57-66 (VARIANT), AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=15019477; DOI=10.1016/j.toxicon.2003.11.021;
RA Davies N.W., Wiese M.D., Brown S.G.A.;
RT "Characterisation of major peptides in 'jack jumper' ant venom by mass
RT spectrometry.";
RL Toxicon 43:173-183(2004).
RN [4]
RP PROTEIN SEQUENCE OF 68-83.
RC TISSUE=Venom;
RX PubMed=8605256; DOI=10.1016/0167-4781(95)00197-2;
RA Street M.D., Donovan G.R., Baldo B.A.;
RT "Molecular cloning and characterization of the major allergen Myr p II from
RT the venom of the jumper ant Myrmecia pilosula: Myr p I and Myr p II share a
RT common protein leader sequence.";
RL Biochim. Biophys. Acta 1305:87-97(1996).
RN [5]
RP FUNCTION, AND SYNTHESIS OF 57-78; 57-112; 67-112; 79-112; 93-112 AND
RP 103-112.
RX PubMed=9813247; DOI=10.1016/s0304-4165(98)00052-x;
RA Wu Q.-X., King M.A., Donovan G.R., Alewood D., Alewood P.F., Sawyer W.H.,
RA Baldo B.A.;
RT "Cytotoxicity of pilosulin 1, a peptide from the venom of the jumper ant
RT Myrmecia pilosula.";
RL Biochim. Biophys. Acta 1425:74-80(1998).
RN [6]
RP FUNCTION, AND SYNTHESIS OF 57-112.
RX PubMed=9701394;
RX DOI=10.1002/(sici)1097-0320(19980801)32:4<268::aid-cyto2>3.0.co;2-e;
RA King M.A., Wu Q.-X., Donovan G.R., Baldo B.A.;
RT "Flow cytometric analysis of cell killing by the jumper ant venom peptide
RT pilosulin 1.";
RL Cytometry 32:268-273(1998).
RN [7]
RP FUNCTION, AND SYNTHESIS OF 57-76.
RX PubMed=15639237; DOI=10.1016/j.abb.2004.11.006;
RA Zelezetsky I., Pag U., Antcheva N., Sahl H.-G., Tossi A.;
RT "Identification and optimization of an antimicrobial peptide from the ant
RT venom toxin pilosulin.";
RL Arch. Biochem. Biophys. 434:358-364(2005).
RN [8]
RP SYNTHESIS OF 67-112; 79-112; 87-112; 93-112; 95-112; 97-112; 99-112
RP 101-112; 93-100; 93-102; 93-104 AND 93-106, AND IGE-BINDING DETERMINANT.
RX PubMed=7508264; DOI=10.1016/0167-4838(94)90031-0;
RA Donovan G.R., Street M.D., Baldo B.A., Alewood D., Alewood P.F.,
RA Sutherland S.K.;
RT "Identification of an IgE-binding determinant of the major allergen Myr p I
RT from the venom of the Australian jumper ant Myrmecia pilosula.";
RL Biochim. Biophys. Acta 1204:48-52(1994).
RN [9]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=26805882; DOI=10.3390/toxins8010030;
RA Touchard A., Aili S.R., Fox E.G., Escoubas P., Orivel J., Nicholson G.M.,
RA Dejean A.;
RT "The biochemical toxin arsenal from ant venoms.";
RL Toxins 8:1-28(2016).
CC -!- FUNCTION: Has strong cytotoxic and hemolytic activities. Is more potent
CC against mononuclear leukocytes than against granulocytes. The
CC synthesized peptide 57-76 shows a potent and broad spectrum
CC antimicrobial activity against both Gram-positive and Gram-negative
CC bacteria, and also against the fungus C.albicans. Adopts an alpha-
CC helical structure. {ECO:0000269|PubMed:15639237,
CC ECO:0000269|PubMed:9701394, ECO:0000269|PubMed:9813247}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8866004}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8866004}.
CC -!- MASS SPECTROMETRY: [M-myrmeciitoxin-Mp1d]: Mass=4938;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:15019477};
CC -!- MASS SPECTROMETRY: [M-myrmeciitoxin-Mp1c]: Mass=5279;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:15019477};
CC -!- MASS SPECTROMETRY: [M-myrmeciitoxin-Mp1a]: Mass=6052;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:15019477};
CC -!- MASS SPECTROMETRY: [M-myrmeciitoxin-Mp1a]: Mass=6067;
CC Method=Electrospray; Note=Variant Ile-61.;
CC Evidence={ECO:0000269|PubMed:15019477};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC -!- SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily.
CC Ant pilosulin family. {ECO:0000305}.
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DR EMBL; X70256; CAA49760.1; -; mRNA.
DR PIR; S28180; S28180.
DR PIR; S65709; S65709.
DR PDB; 5X3L; NMR; -; A=57-76.
DR PDBsum; 5X3L; -.
DR AlphaFoldDB; Q07932; -.
DR SMR; Q07932; -.
DR Allergome; 3380; Myr p 1.0101.
DR Allergome; 480; Myr p 1.
DR TCDB; 1.C.51.1.1; the pilosulin (pilosulin) family.
DR GO; GO:0005615; C:extracellular space; IMP:CAFA.
DR GO; GO:0001897; P:cytolysis by symbiont of host cells; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:CAFA.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:CAFA.
DR GO; GO:0044179; P:hemolysis in another organism; IMP:CAFA.
DR DisProt; DP00567; -.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Fungicide; Hemolysis; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..56
FT /evidence="ECO:0000269|PubMed:15019477,
FT ECO:0000269|PubMed:8866004"
FT /id="PRO_0000035158"
FT PEPTIDE 57..112
FT /note="M-myrmeciitoxin-Mp1a"
FT /evidence="ECO:0000269|PubMed:8866004"
FT /id="PRO_0000035159"
FT PEPTIDE 65..112
FT /note="M-myrmeciitoxin-Mp1c"
FT /evidence="ECO:0000269|PubMed:8866004"
FT /id="PRO_0000035160"
FT PEPTIDE 68..112
FT /note="M-myrmeciitoxin-Mp1d"
FT /evidence="ECO:0000269|PubMed:8866004"
FT /id="PRO_0000035161"
FT PEPTIDE 71..112
FT /note="M-myrmeciitoxin-Mp1e"
FT /evidence="ECO:0000269|PubMed:8866004"
FT /id="PRO_0000035162"
FT PEPTIDE 86..112
FT /note="U1-myrmeciitoxin-Mp1f"
FT /evidence="ECO:0000269|PubMed:8866004"
FT /id="PRO_0000035163"
FT REGION 57..78
FT /note="Critical for cytotoxic activity"
FT REGION 93..106
FT /note="IgE-binding determinant"
FT VARIANT 61
FT /note="V -> I (m-MIITX-Mp1b)"
FT CONFLICT 82..83
FT /note="PK -> KT (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:5X3L"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:5X3L"
SQ SEQUENCE 112 AA; 11849 MW; F1F90510A82ED4EF CRC64;
MKLSCLLLTL TIIFVLTIVH APNVEAKDLA DPESEAVGFA DAFGEADAVG EADPNAGLGS
VFGRLARILG RVIPKVAKKL GPKVAKVLPK VMKEAIPMAV EMAKSQEEQQ PQ
