ID   BR1R_PELRI              Reviewed;          24 AA.
AC   P86027;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Brevinin-1R {ECO:0000303|Ref.1};
OS   Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=8406;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000269|Ref.1};
RA   Artemenko K.A., Samgina T.Y., Lebedev A.T., Doyle J.R., Llewellyn L.E.,
RA   Bilusich D., Bowie J.H.;
RT   "Host-defence peptides from the skin secretion of the European marsh frog
RT   Rana ridibunda.";
RL   Mass Spectrom. 4:79-88(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:18855342};
RX   PubMed=18855342; DOI=10.1002/rcm.3759;
RA   Samgina T.Y., Artemenko K.A., Gorshkov V.A., Ogourtsov S.V., Zubarev R.A.,
RA   Lebedev A.T.;
RT   "De novo sequencing of peptides secreted by the skin glands of the
RT   caucasian green frog Rana ridibunda.";
RL   Rapid Commun. Mass Spectrom. 22:3517-3525(2008).
RN   [3]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, DISULFIDE BOND, MASS SPECTROMETRY,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:28012108};
RX   PubMed=28012108; DOI=10.1007/s00216-016-0143-3;
RA   Samgina T.Y., Artemenko K.A., Bergquist J., Trebse P., Torkar G.,
RA   Tolpina M.D., Lebedev A.T.;
RT   "Differentiation of frogs from two populations belonging to the Pelophylax
RT   esculentus complex by LC-MS/MS comparison of their skin peptidomes.";
RL   Anal. Bioanal. Chem. 409:1951-1961(2017).
CC   -!- FUNCTION: Antimicrobial peptide. {ECO:0000250|UniProtKB:P40835}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18855342,
CC       ECO:0000269|PubMed:28012108, ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands. {ECO:0000305|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=2663.51; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18855342, ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: Mass=2662; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18855342, ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: Mass=2663.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:28012108};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P86027; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR012520; Antimicrobial_frog_1.
DR   Pfam; PF08018; Antimicrobial_1; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   PEPTIDE         1..24
FT                   /note="Brevinin-1R"
FT                   /evidence="ECO:0000269|PubMed:18855342,
FT                   ECO:0000269|PubMed:28012108, ECO:0000269|Ref.1"
FT                   /id="PRO_0000351555"
FT   DISULFID        18..24
FT                   /evidence="ECO:0000269|PubMed:18855342,
FT                   ECO:0000269|PubMed:28012108"
SQ   SEQUENCE   24 AA;  2667 MW;  84DC46EDF59F2082 CRC64;
     FFPAIFRLVA KVVPSIICSV TKKC