ID   PA1C_LITPA              Reviewed;          68 AA.
AC   P84276; A7WNV8;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Palustrin-1c;
DE   Flags: Precursor;
OS   Lithobates palustris (Pickerel frog) (Rana palustris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=298395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin secretion;
RX   PubMed=17698247; DOI=10.1016/j.peptides.2007.07.019;
RA   Zhou M., Wang L., Owens D.E., Chen T., Walker B., Shaw C.;
RT   "Rapid identification of precursor cDNAs encoding five structural classes
RT   of antimicrobial peptides from pickerel frog (Rana palustris) skin
RT   secretion by single step 'shotgun' cloning.";
RL   Peptides 28:1605-1610(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 42-68, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, MASS SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:11087945};
RX   PubMed=11087945; DOI=10.1016/s0167-4838(00)00191-6;
RA   Basir Y.J., Knoop F.C., Dulka J., Conlon J.M.;
RT   "Multiple antimicrobial peptides and peptides related to bradykinin and
RT   neuromedin N isolated from skin secretions of the pickerel frog, Rana
RT   palustris.";
RL   Biochim. Biophys. Acta 1543:95-105(2000).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 42-68, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:15128283};
RX   PubMed=15128283; DOI=10.1677/joe.0.1810347;
RA   Marenah L., Flatt P.R., Orr D.F., McClean S., Shaw C., Abdel-Wahab Y.H.A.;
RT   "Brevinin-1 and multiple insulin-releasing peptides in the skin of the frog
RT   Rana palustris.";
RL   J. Endocrinol. 181:347-354(2004).
CC   -!- FUNCTION: Antimicrobial activity against Gram-negative bacterium
CC       E.coli. Stimulates insulin release. {ECO:0000269|PubMed:11087945,
CC       ECO:0000269|PubMed:15128283}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11087945,
CC       ECO:0000269|PubMed:15128283}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:11087945, ECO:0000269|PubMed:15128283}.
CC   -!- MASS SPECTROMETRY: Mass=2873.6; Mass_error=0.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11087945};
CC   -!- MASS SPECTROMETRY: Mass=2873.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15128283};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000269|PubMed:11087945,
CC       ECO:0000269|PubMed:15128283}.
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DR   EMBL; AM745092; CAN87014.1; -; mRNA.
DR   AlphaFoldDB; P84276; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
DR   InterPro; IPR012521; Antimicrobial_frog_2.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08023; Antimicrobial_2; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..39
FT                   /id="PRO_0000412997"
FT   PEPTIDE         42..68
FT                   /note="Palustrin-1c"
FT                   /id="PRO_0000043820"
FT   DISULFID        62..68
FT                   /evidence="ECO:0000269|PubMed:11087945"
SQ   SEQUENCE   68 AA;  7494 MW;  3E1C5884177D565B CRC64;
     MFTTKKSLLL LFFLGTISLS LCEEERGADE EEGDGEKLTK RALSILRGLE KLAKMGIALT
     NCKATKKC