BRK4_PITHY
ID BRK4_PITHY Reviewed; 61 AA.
AC P84899; L0PHN1; P84894;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=[Val1,Thr6]-bradykinyl-Gln,Ser {ECO:0000303|PubMed:24394432};
DE AltName: Full=Bradykinin-related peptide VS-11 {ECO:0000303|PubMed:24394432};
DE Contains:
DE RecName: Full=[Val1,Thr6]-bradykinin {ECO:0000303|PubMed:24394432};
DE Flags: Precursor;
OS Pithecopus hypochondrialis (Orange-legged leaf frog) (Phyllomedusa
OS hypochondrialis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Pithecopus.
OX NCBI_TaxID=317381;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-61, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, HYDROXYLATION
RP AT PRO-52, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Skin {ECO:0000312|EMBL:CCJ67652.1}, and
RC Skin secretion {ECO:0000303|PubMed:24394432};
RX PubMed=24394432; DOI=10.1016/j.peptides.2013.12.013;
RA Jiang Y., Xi X., Ge L., Yang N., Hou X., Ma J., Ma C., Wu Y., Guo X.,
RA Li R., Zhou M., Wang L., Chen T., Shaw C.;
RT "Bradykinin-related peptides (BRPs) from skin secretions of three genera of
RT phyllomedusine leaf frogs and their comparative pharmacological effects on
RT mammalian smooth muscles.";
RL Peptides 52:122-133(2014).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 51-61, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, HYDROXYLATION AT PRO-52, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:16797783};
RX PubMed=16797783; DOI=10.1016/j.peptides.2006.04.020;
RA Brand G.D., Krause F.C., Silva L.P., Leite J.R.S.A., Melo J.A.T.,
RA Prates M.V., Pesquero J.B., Santos E.L., Nakaie C.R., Costa-Neto C.M.,
RA Bloch C. Jr.;
RT "Bradykinin-related peptides from Phyllomedusa hypochondrialis.";
RL Peptides 27:2137-2146(2006).
CC -!- FUNCTION: [[Val1,Thr6]-bradykinin]: Induces contraction of rat ileum
CC smooth muscle (EC(50)=2.73 uM) but has no activity towards smooth
CC muscle from tail artery, urinary bladder or uterus up to concentrations
CC of 100 uM. Binds to both bradykinin receptor B1 (BDKRB1) and B2
CC (BDKRB2); the effect via BDKRB1 is stronger.
CC {ECO:0000269|PubMed:24394432}.
CC -!- FUNCTION: [Val1,Hyp2,Thr6]-bradykinin-Gln,Ser: Induces contraction of
CC rat ileum smooth muscle (EC(50)=710 nM) but has no activity towards
CC smooth muscle from tail artery, urinary bladder or uterus up to
CC concentrations of 100 uM. Binds to both bradykinin receptor B1 (BDKRB1)
CC and B2 (BDKRB2); the effect via BDKRB1 is stronger (PubMed:24394432).
CC Induces contraction of guinea pig ileum smooth muscle
CC (PubMed:16797783). {ECO:0000269|PubMed:16797783,
CC ECO:0000269|PubMed:24394432}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16797783,
CC ECO:0000269|PubMed:24394432}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:16797783, ECO:0000269|PubMed:24394432}.
CC -!- MASS SPECTROMETRY: [[Val1,Thr6]-bradykinyl-Gln,Ser]: Mass=1231.95;
CC Method=MALDI; Note=[Val1,Thr6]-bradykinyl-Gln,Ser.;
CC Evidence={ECO:0000269|PubMed:24394432};
CC -!- MASS SPECTROMETRY: [[Val1,Thr6]-bradykinyl-Gln,Ser]: Mass=1247.85;
CC Method=MALDI; Note=[Val1,Hyp2,Thr6]-bradykinyl-Gln,Ser.;
CC Evidence={ECO:0000269|PubMed:24394432};
CC -!- MASS SPECTROMETRY: [[Val1,Thr6]-bradykinin]: Mass=1016.50;
CC Method=MALDI; Note=[Val1,Thr6]-bradykinin.;
CC Evidence={ECO:0000269|PubMed:24394432};
CC -!- MASS SPECTROMETRY: [[Val1,Thr6]-bradykinin]: Mass=1032.65;
CC Method=MALDI; Note=[Val1,Hyp2,Thr6]-bradykinin.;
CC Evidence={ECO:0000269|PubMed:24394432};
CC -!- MASS SPECTROMETRY: [[Val1,Thr6]-bradykinyl-Gln,Ser]: Mass=1232.66;
CC Mass_error=0.1; Method=MALDI; Note=[Val1,Thr6]-bradykinyl-Gln,Ser.;
CC Evidence={ECO:0000269|PubMed:16797783};
CC -!- MASS SPECTROMETRY: [[Val1,Thr6]-bradykinyl-Gln,Ser]: Mass=1248.69;
CC Mass_error=0.1; Method=MALDI; Note=[Val1,Hyp2,Thr6]-bradykinyl-
CC Gln,Ser.; Evidence={ECO:0000269|PubMed:16797783};
CC -!- MASS SPECTROMETRY: [[Val1,Thr6]-bradykinin]: Mass=1017.54;
CC Mass_error=0.1; Method=MALDI; Note=[Val1,Thr6]-bradykinin.;
CC Evidence={ECO:0000269|PubMed:16797783};
CC -!- MASS SPECTROMETRY: [[Val1,Thr6]-bradykinin]: Mass=1033.54;
CC Mass_error=0.1; Method=MALDI; Note=[Val1,Hyp2,Thr6]-bradykinin.;
CC Evidence={ECO:0000269|PubMed:16797783};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Bradykinin-related peptide subfamily. {ECO:0000305}.
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DR EMBL; HE967331; CCJ67652.1; -; mRNA.
DR AlphaFoldDB; P84899; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; 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; Direct protein sequencing;
KW G-protein coupled receptor impairing toxin; Hydroxylation; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..50
FT /evidence="ECO:0000305|PubMed:16797783,
FT ECO:0000305|PubMed:24394432"
FT /id="PRO_0000438929"
FT PEPTIDE 51..61
FT /note="[Val1,Thr6]-bradykinyl-Gln,Ser"
FT /evidence="ECO:0000269|PubMed:16797783,
FT ECO:0000269|PubMed:24394432"
FT /id="PRO_0000438930"
FT PEPTIDE 51..59
FT /note="[Val1,Thr6]-bradykinin"
FT /evidence="ECO:0000269|PubMed:16797783,
FT ECO:0000269|PubMed:24394432"
FT /id="PRO_0000438931"
FT REGION 25..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="4-hydroxyproline; in form [Val1,Hyp2,Thr6]-
FT Bradykinyl-Gln,Ser and [Val1,Hyp2,Thr6]-Bradykinin"
FT /evidence="ECO:0000269|PubMed:16797783,
FT ECO:0000269|PubMed:24394432"
SQ SEQUENCE 61 AA; 7180 MW; A25F3BE619D413AC CRC64;
MSILKKSLFL VLFLGLVSFS ICEEEKREAE EEENEDEIEE QSEEKKRFEP VPPGFTPFRQ
S
