ID   H2A_SPHLA               Reviewed;          21 AA.
AC   P0DQL2;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Buforin-2 {ECO:0000305};
DE            Short=BF2 {ECO:0000303|PubMed:30044391};
DE   AltName: Full=Buforin II {ECO:0000303|PubMed:30044391};
OS   Sphaenorhynchus lacteus (Orinoco lime treefrog) (Hyla lactea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Hylinae; Dendropsophini;
OC   Sphaenorhynchus.
OX   NCBI_TaxID=279984;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin;
RX   PubMed=30044391; DOI=10.3390/ijms19082170;
RA   Munoz-Camargo C., Salazar V.A., Barrero-Guevara L., Camargo S.,
RA   Mosquera A., Groot H., Boix E.;
RT   "Unveiling the multifaceted mechanisms of antibacterial activity of buforin
RT   II and frenatin 2.3S peptides from skin micro-organs of the Orinoco lime
RT   treefrog (Sphaenorhynchus lacteus).";
RL   Int. J. Mol. Sci. 19:0-0(2018).
CC   -!- FUNCTION: Antimicrobial peptide with potent activity against some Gram-
CC       positive and Gram-negative bacteria (PubMed:30044391). Does not
CC       permeabilize membrane, but internalizes into bacterial cells and alter
CC       specific gene expression involved in bacterial resistance mechanisms
CC       (PubMed:30044391). Has the ability to agglutinate E.coli, and lipid
CC       vesicles (PubMed:30044391). Shows a weak hemolytic activity, and is not
CC       cytotoxic to monocytes (PubMed:30044391).
CC       {ECO:0000269|PubMed:30044391}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30044391}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:30044391}.
CC   -!- DOMAIN: Adopts a distorted helix spanning from residues Gly-7 to Pro-11
CC       and a regular alpha-helix from Val-12 to Arg-20 in membrane mimetic
CC       environment, and a random structure in water.
CC       {ECO:0000250|UniProtKB:P55897}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=00308";
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DR   AlphaFoldDB; P0DQL2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
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; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Fungicide; Hydroxylation; Immunity;
KW   Innate immunity; Lipid-binding; Secreted.
FT   PEPTIDE         1..21
FT                   /note="Buforin-2"
FT                   /evidence="ECO:0000269|PubMed:30044391"
FT                   /id="PRO_0000450278"
FT   MOD_RES         21
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
SQ   SEQUENCE   21 AA;  2435 MW;  0139439F8FEC191F CRC64;
     TRSSRAGLQF PVGRVHRLLR K