MAGA_XENLA
ID MAGA_XENLA Reviewed; 303 AA.
AC P11006;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Magainins;
DE Contains:
DE RecName: Full=Small acidic peptide 1;
DE Contains:
DE RecName: Full=Small acidic peptide 2;
DE Contains:
DE RecName: Full=Small acidic peptide 3;
DE Contains:
DE RecName: Full=Magainin-1;
DE AltName: Full=Magainin I;
DE Contains:
DE RecName: Full=Magainin-2;
DE AltName: Full=Magainin II {ECO:0000303|PubMed:15193922};
DE Flags: Precursor;
GN Name=magainins;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2833514; DOI=10.1016/s0021-9258(18)60628-3;
RA Terry A.S., Poulter L., Williams D.H., Nutkins J.C., Giovannini M.G.,
RA Moore C.H., Gibson B.W.;
RT "The cDNA sequence coding for prepro-PGS (prepro-magainins) and aspects of
RT the processing of this prepro-polypeptide.";
RL J. Biol. Chem. 263:5745-5751(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-158 AND 297-303, AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Skin, and Skin secretion;
RX PubMed=3299384; DOI=10.1073/pnas.84.15.5449;
RA Zasloff M.;
RT "Magainins, a class of antimicrobial peptides from Xenopus skin: isolation,
RT characterization of two active forms, and partial cDNA sequence of a
RT precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5449-5453(1987).
RN [3]
RP PROTEIN SEQUENCE (MAGAININ-1 AND MAGAININ-2).
RC TISSUE=Stomach;
RX PubMed=1717472; DOI=10.1016/s0021-9258(18)55069-9;
RA Moore K.S., Bevins C.L., Brasseur M.M., Tomassini N., Turner K., Eck H.,
RA Zasloff M.;
RT "Antimicrobial peptides in the stomach of Xenopus laevis.";
RL J. Biol. Chem. 266:19851-19857(1991).
RN [4]
RP FUNCTION OF MAGAININ-2 AS ANTIVIRAL PEPTIDE.
RX PubMed=15193922; DOI=10.1016/j.virol.2004.02.029;
RA Chinchar V.G., Bryan L., Silphadaung U., Noga E., Wade D.,
RA Rollins-Smith L.;
RT "Inactivation of viruses infecting ectothermic animals by amphibian and
RT piscine antimicrobial peptides.";
RL Virology 323:268-275(2004).
RN [5]
RP STRUCTURE BY NMR OF MAGAININ-2.
RX PubMed=8298457; DOI=10.1002/pro.5560021208;
RA Bechinger B., Zasloff M., Opella S.J.;
RT "Structure and orientation of the antibiotic peptide magainin in membranes
RT by solid-state nuclear magnetic resonance spectroscopy.";
RL Protein Sci. 2:2077-2084(1993).
CC -!- FUNCTION: Antimicrobial peptides that inhibit the growth of numerous
CC species of bacteria and fungi and induce osmotic lysis of protozoa.
CC Rapidly inactivates channel catfish herpesvirus (ED(50)=48 uM) over a
CC wide temperature range (PubMed:15193922). Magainins are membrane lytic
CC agents. {ECO:0000269|PubMed:15193922}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Synthesized in the stomach and stored in a novel
CC granular multinucleated cell in the gastric mucosa. It is stored as
CC active, processed peptides in large granules within the granular gland
CC secretions of the skin.
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family. Magainin
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=When a frog swallows a fly
CC - Issue 7 of February 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/007";
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DR EMBL; J03193; AAA49930.1; -; mRNA.
DR PIR; A28620; A28620.
DR RefSeq; NP_001081306.1; NM_001087837.1.
DR PDB; 1D9J; NMR; -; A=267-278.
DR PDB; 1D9L; NMR; -; A=270-278.
DR PDB; 1D9M; NMR; -; A=270-278.
DR PDB; 1D9O; NMR; -; A=267-278.
DR PDB; 1D9P; NMR; -; A=267-278.
DR PDB; 1DUM; NMR; -; A/B=267-289.
DR PDB; 1F0D; NMR; -; A=267-278.
DR PDB; 1F0E; NMR; -; A=269-278.
DR PDB; 1F0F; NMR; -; A=270-278.
DR PDB; 1F0G; NMR; -; A=267-278.
DR PDB; 1F0H; NMR; -; A=267-278.
DR PDB; 2LSA; NMR; -; A=267-289.
DR PDB; 2MAG; NMR; -; A=267-289.
DR PDB; 4MGP; X-ray; 1.75 A; A=267-289.
DR PDB; 5CGN; X-ray; 2.20 A; E/F/G/H=267-289.
DR PDB; 5CGO; X-ray; 1.50 A; A/B=267-289.
DR PDBsum; 1D9J; -.
DR PDBsum; 1D9L; -.
DR PDBsum; 1D9M; -.
DR PDBsum; 1D9O; -.
DR PDBsum; 1D9P; -.
DR PDBsum; 1DUM; -.
DR PDBsum; 1F0D; -.
DR PDBsum; 1F0E; -.
DR PDBsum; 1F0F; -.
DR PDBsum; 1F0G; -.
DR PDBsum; 1F0H; -.
DR PDBsum; 2LSA; -.
DR PDBsum; 2MAG; -.
DR PDBsum; 4MGP; -.
DR PDBsum; 5CGN; -.
DR PDBsum; 5CGO; -.
DR AlphaFoldDB; P11006; -.
DR SMR; P11006; -.
DR TCDB; 1.C.16.1.1; the magainin (magainin) family.
DR ABCD; P11006; 2 sequenced antibodies.
DR GeneID; 397766; -.
DR KEGG; xla:397766; -.
DR CTD; 397766; -.
DR Xenbase; XB-GENE-6252596; magainins.L.
DR EvolutionaryTrace; P11006; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397766; Expressed in zone of skin and 16 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Antiviral protein; Cleavage on pair of basic residues; Cytolysis;
KW Direct protein sequencing; Fungicide; Hemolysis; Immunity; Innate immunity;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..26
FT /id="PRO_0000010677"
FT PEPTIDE 27..32
FT /note="Small acidic peptide 1"
FT /id="PRO_0000010678"
FT PROPEP 33..36
FT /id="PRO_0000010679"
FT PEPTIDE 37..59
FT /note="Magainin-1"
FT /id="PRO_0000010680"
FT PROPEP 62..72
FT /id="PRO_0000010681"
FT PEPTIDE 73..78
FT /note="Small acidic peptide 2"
FT /id="PRO_0000010682"
FT PROPEP 79..82
FT /id="PRO_0000010683"
FT PEPTIDE 83..105
FT /note="Magainin-2"
FT /id="PRO_0000010684"
FT PROPEP 108..118
FT /id="PRO_0000010685"
FT PEPTIDE 119..124
FT /note="Small acidic peptide 2"
FT /id="PRO_0000010686"
FT PROPEP 125..128
FT /id="PRO_0000010687"
FT PEPTIDE 129..151
FT /note="Magainin-2"
FT /id="PRO_0000010688"
FT PROPEP 154..164
FT /id="PRO_0000010689"
FT PEPTIDE 165..170
FT /note="Small acidic peptide 2"
FT /id="PRO_0000010690"
FT PROPEP 171..174
FT /id="PRO_0000010691"
FT PEPTIDE 175..197
FT /note="Magainin-2"
FT /id="PRO_0000010692"
FT PROPEP 200..210
FT /id="PRO_0000010693"
FT PEPTIDE 211..216
FT /note="Small acidic peptide 3"
FT /id="PRO_0000010694"
FT PROPEP 217..220
FT /id="PRO_0000010695"
FT PEPTIDE 221..243
FT /note="Magainin-2"
FT /id="PRO_0000010696"
FT PROPEP 246..256
FT /id="PRO_0000010697"
FT PEPTIDE 257..262
FT /note="Small acidic peptide 2"
FT /id="PRO_0000010698"
FT PROPEP 263..266
FT /id="PRO_0000010699"
FT PEPTIDE 267..289
FT /note="Magainin-2"
FT /id="PRO_0000010700"
FT PROPEP 292..303
FT /id="PRO_0000010701"
FT CONFLICT 74
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 269..287
FT /evidence="ECO:0007829|PDB:5CGO"
SQ SEQUENCE 303 AA; 33380 MW; E369B0DBB033EA80 CRC64;
MFKGLFICSL IAVICANALP QPEASADEDM DEREVRGIGK FLHSAGKFGK AFVGEIMKSK
RDAEAVGPEA FADEDLDERE VRGIGKFLHS AKKFGKAFVG EIMNSKRDAE AVGPEAFADE
DLDEREVRGI GKFLHSAKKF GKAFVGEIMN SKRDAEAVGP EAFADEDLDE REVRGIGKFL
HSAKKFGKAF VGEIMNSKRD AEAVGPEAFA DEDFDEREVR GIGKFLHSAK KFGKAFVGEI
MNSKRDAEAV GPEAFADEDL DEREVRGIGK FLHSAKKFGK AFVGEIMNSK RDAEAVDDRR
WVE
