ID   DRS1_AGASP              Reviewed;          28 AA.
AC   P86941;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Dermaseptin-SP1 {ECO:0000303|PubMed:31671555};
DE            Short=DRS-SP1 {ECO:0000303|PubMed:31671555};
DE   AltName: Full=Dermaseptin-LI1 {ECO:0000303|PubMed:18644413};
DE            Short=DRS-LI1 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Insulinotropic peptide 1 {ECO:0000303|PubMed:15177918};
DE            Short=FSIP {ECO:0000303|PubMed:15177918};
OS   Agalychnis spurrelli (Gliding leaf frog) (Agalychnis litodryas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=317303;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=15177918; DOI=10.1016/j.regpep.2004.02.007;
RA   Marenah L., Shaw C., Orr D.F., McClean S., Flatt P.R., Abdel-Wahab Y.H.;
RT   "Isolation and characterisation of an unexpected class of insulinotropic
RT   peptides in the skin of the frog Agalychnis litodryas.";
RL   Regul. Pept. 120:33-38(2004).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=18644413; DOI=10.1016/j.peptides.2008.06.017;
RA   Amiche M., Ladram A., Nicolas P.;
RT   "A consistent nomenclature of antimicrobial peptides isolated from frogs of
RT   the subfamily Phyllomedusinae.";
RL   Peptides 29:2074-2082(2008).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=31671555; DOI=10.3390/biom9110667;
RA   Proano-Bolanos C., Blasco-Zuniga A., Almeida J.R., Wang L.,
RA   Llumiquinga M.A., Rivera M., Zhou M., Chen T., Shaw C.;
RT   "Unravelling the skin secretion peptides of the gliding leaf frog,
RT   Agalychnis spurrelli (Hylidae).";
RL   Biomolecules 9:1-20(2019).
CC   -!- FUNCTION: Probable antimicrobial peptide which stimulates insulin-
CC       release in glucose-responsive BRIN-BD 11 cells.
CC       {ECO:0000269|PubMed:15177918, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15177918}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:15177918}.
CC   -!- MASS SPECTROMETRY: Mass=3020.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15177918};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000255}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=0960";
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DR   AlphaFoldDB; P86941; -.
DR   SMR; P86941; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR022731; Dermaseptin.
DR   Pfam; PF12121; DD_K; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antimicrobial; Direct protein sequencing;
KW   Immunity; Innate immunity; Secreted.
FT   PEPTIDE         1..28
FT                   /note="Dermaseptin-SP1"
FT                   /evidence="ECO:0000269|PubMed:15177918"
FT                   /id="PRO_0000412976"
SQ   SEQUENCE   28 AA;  3020 MW;  683704EFB3A571B6 CRC64;
     AVWKDFLKNI GKAAGKAVLN SVTDMVNE