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 27-MAR-2024, entry version 122. 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"; 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; 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 AGR; Xenbase:XB-GENE-6252596; -. 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 cell types or 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: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 //