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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
 
 
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