BRKRN_SYLVI
ID BRKRN_SYLVI Reviewed; 58 AA.
AC P86093;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Ranakinin-N {ECO:0000303|PubMed:17994619};
DE Flags: Precursor;
OS Sylvirana nigrovittata (Black-striped frog) (Hylarana nigrovittata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Sylvirana.
OX NCBI_TaxID=127021;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-56, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:17994619};
RX PubMed=17994619; DOI=10.1002/psc.958;
RA Liu X., You D., Chen L., Wang X., Zhang K., Lai R.;
RT "A novel bradykinin-like peptide from skin secretions of the frog, Rana
RT nigrovittata.";
RL J. Pept. Sci. 14:626-630(2008).
CC -!- FUNCTION: Induces contraction of intestinal smooth muscle in isolated
CC guinea pig ileum. May induce relaxation of arterial smooth muscle. May
CC target bradykinin receptors (BDKRB). Lacks antibacterial activity
CC against the Gram-positive bacterium S.aureus and the Gram-negative
CC bacteria E.coli and B.dysenteria, and antifungal activity against
CC C.albicans. {ECO:0000269|PubMed:17994619}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17994619}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:17994619}.
CC -!- MASS SPECTROMETRY: Mass=1442.5; Method=FAB;
CC Evidence={ECO:0000269|PubMed:17994619};
CC -!- SIMILARITY: Belongs to the bradykinin family. {ECO:0000255}.
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DR AlphaFoldDB; P86093; -.
DR TCDB; 1.C.52.1.17; the dermaseptin (dermaseptin) family.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0045933; P:positive regulation of muscle contraction; IDA:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Cleavage on pair of basic residues;
KW Direct protein sequencing; Secreted; Signal; Vasoactive; Vasodilator.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..43
FT /evidence="ECO:0000255, ECO:0000269|PubMed:17994619"
FT /id="PRO_0000363162"
FT PEPTIDE 44..58
FT /note="Ranakinin-N"
FT /evidence="ECO:0000269|PubMed:17994619"
FT /id="PRO_0000363163"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 58 AA; 6641 MW; 8BA722C89D886C91 CRC64;
MFTMKKSLLL LFFLGTISMS LCEEKRDADE EETEGEAKME DIKRAEAVPP GFTPFRKP